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Conserved domains on  [gi|1720416759|ref|XP_030110959|]
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RAF proto-oncogene serine/threonine-protein kinase isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
255-537 0e+00

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 588.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 255 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd14149     1 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 414
Cdd:cd14149    81 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYK 494
Cdd:cd14149   161 WSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINR 537
Cdd:cd14149   241 NCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLPKINR 283
C1_A_C-Raf cd20870
protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated ...
55-106 7.26e-35

protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma) kinases, and similar proteins; This group includes A-Raf and C-Raf, both of which are serine/threonine-protein kinases. A-Raf, also called proto-oncogene A-Raf or proto-oncogene A-Raf-1, cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. C-Raf, also known as proto-oncogene Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around mid-gestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. Both A- and C-Raf are mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410420  Cd Length: 52  Bit Score: 125.07  E-value: 7.26e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759  55 LTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDW 106
Cdd:cd20870     1 LTTHNFVRKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDW 52
 
Name Accession Description Interval E-value
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
255-537 0e+00

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 588.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 255 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd14149     1 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 414
Cdd:cd14149    81 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYK 494
Cdd:cd14149   161 WSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINR 537
Cdd:cd14149   241 NCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLPKINR 283
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
268-525 5.38e-73

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 233.54  E-value: 5.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 268 VMLSTRIGSGSFGTVYKGKWHGD-------VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIV 339
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkikVAVKTLKE-GADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGePLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQ 419
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYaspdlsRLYK--NC 496
Cdd:pfam07714 160 KRGGGKLPIKWMAPESLK---DGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE-VLEFLEDGY------RLPQpeNC 229
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:pfam07714 230 PDELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
270-525 6.76e-67

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 217.78  E-value: 6.76e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  270 LSTRIGSGSFGTVYKGKWHG-------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQ 341
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKLKGkggkkkvEVAVKTLKE-DASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEePLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  342 WCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSR-WSGSQQ 420
Cdd:smart00219  82 YMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL----SRdLYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  421 VEQPTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYaspdlsRLYK--N 495
Cdd:smart00219 158 YRKRGGKlpIRWMAPESLK---EGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE-VLEYLKNGY------RLPQppN 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 1720416759  496 CPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:smart00219 228 CPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
273-548 1.03e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.97  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG---DVAVKILKV-VDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSS 347
Cdd:COG0515    14 LLGRGGMGVVYLARDLRlgrPVALKVLRPeLAADPEARERFRREARALARLNHPNIVRVYDVGEEDGrPYLVMEYVEGES 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwSGSQQVEQPTGS 427
Cdd:COG0515    94 LADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGG-ATLTQTGTVVGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGyASPDLSRLYKNCPKAMKRLVADC 507
Cdd:COG0515   172 PGYMAPEQARGE---PVDPRSDVYSLGVTLYELLTGRPPFDG-DSPAELLRAHLRE-PPPPPSELRPDLPPALDAIVLRA 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 508 VKKVKEERPlfpqilSSIELLQHSLPKINRSASEPSLHRAA 548
Cdd:COG0515   247 LAKDPEERY------QSAAELAAALRAVLRSLAAAAAAAAA 281
C1_A_C-Raf cd20870
protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated ...
55-106 7.26e-35

protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma) kinases, and similar proteins; This group includes A-Raf and C-Raf, both of which are serine/threonine-protein kinases. A-Raf, also called proto-oncogene A-Raf or proto-oncogene A-Raf-1, cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. C-Raf, also known as proto-oncogene Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around mid-gestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. Both A- and C-Raf are mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410420  Cd Length: 52  Bit Score: 125.07  E-value: 7.26e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759  55 LTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDW 106
Cdd:cd20870     1 LTTHNFVRKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDW 52
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
273-467 2.04e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.03  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGK---WHGDVAVKILK---VVDPTpeqLQA-FRNE---VAVLRktrHVNI-----------LLFmgym 331
Cdd:NF033483   14 RIGRGGMAEVYLAKdtrLDRDVAVKVLRpdlARDPE---FVArFRREaqsAASLS---HPNIvsvydvgedggIPY---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 tkdnlaIVTQWCEGSSL------YKHLHVQETkfqmfqlIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGlTVKIG 404
Cdd:NF033483   84 ------IVMEYVDGRTLkdyireHGPLSPEEA-------VEIMIQILSALEHAHRNGIVHRDIKPQNILItKDG-RVKVT 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 405 DFGLAtvksRWSGSQQVEQpTGSVL----WMAPEVIR--MQDdnpfsFQSDVYSYGIVLYELMAGELPY 467
Cdd:NF033483  150 DFGIA----RALSSTTMTQ-TNSVLgtvhYLSPEQARggTVD-----ARSDIYSLGIVLYEMLTGRPPF 208
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
226-545 2.88e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 95.28  E-value: 2.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 226 QPKTPVPAQRERAPGsgtqekNKIRPR---------GQRD-----------------------SSYYWEIEA---SEVML 270
Cdd:PLN00034    5 QPPPGVPLPSTARHT------TKSRPRrrpdltlplPQRDpslavplplpppsssssssssssASGSAPSAAkslSELER 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQlqAFRN----EVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEG 345
Cdd:PLN00034   79 VNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHED--TVRRqicrEIEILRDVNHPNVVKCHDmFDHNGEIQVLLEFMDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHlHVQETKFqmfqLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqQVEQP- 424
Cdd:PLN00034  157 GSLEGT-HIADEQF----LADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILA------QTMDPc 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 ---TGSVLWMAPEVIR--MQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGY-----ASPDLSRLYK 494
Cdd:PLN00034  226 nssVGTIAYMSPERINtdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMsqppeAPATASREFR 305
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 495 NcpkamkrLVADCVKKVKEERPlfpqilSSIELLQHSL---PKINRSASEPSLH 545
Cdd:PLN00034  306 H-------FISCCLQREPAKRW------SAMQLLQHPFilrAQPGQGQGGPNLH 346
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
58-106 1.74e-15

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 70.55  E-value: 1.74e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759  58 HNFARKTFLKLAFCDICQKFL----LNGFRCQTCGYKFHEHCSTKVPTMCVDW 106
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLwglgKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
58-103 6.18e-13

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.26  E-value: 6.18e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720416759   58 HNFARKTFLKLAFCDICQKFL----LNGFRCQTCGYKFHEHCSTKVPTMC 103
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIwgsfKQGLRCSECKVKCHKKCADKVPKAC 50
 
Name Accession Description Interval E-value
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
255-537 0e+00

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 588.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 255 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd14149     1 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 414
Cdd:cd14149    81 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYK 494
Cdd:cd14149   161 WSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINR 537
Cdd:cd14149   241 NCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLPKINR 283
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
274-526 0e+00

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 563.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLH 353
Cdd:cd14062     1 IGSGSFGTVYKGRWHGDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGSSLYKHLH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 354 VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAP 433
Cdd:cd14062    81 VLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQFEQPTGSILWMAP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 434 EVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKNCPKAMKRLVADCVKKVKE 513
Cdd:cd14062   161 EVIRMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGYLRPDLSKVRSDTPKALRRLMEDCIKFQRD 240
                         250
                  ....*....|...
gi 1720416759 514 ERPLFPQILSSIE 526
Cdd:cd14062   241 ERPLFPQILASLE 253
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
267-531 0e+00

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 530.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 267 EVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd14150     1 EVSMLKRIGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTG 426
Cdd:cd14150    81 SLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQVEQPSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKNCPKAMKRLVAD 506
Cdd:cd14150   161 SILWMAPEVIRMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPDLSKLSSNCPKAMKRLLID 240
                         250       260
                  ....*....|....*....|....*
gi 1720416759 507 CVKKVKEERPLFPQILSSIELLQHS 531
Cdd:cd14150   241 CLKFKREERPLFPQILVSIELLQRL 265
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
261-532 8.54e-166

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 472.24  E-value: 8.54e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVT 340
Cdd:cd14151     3 WEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQ 420
Cdd:cd14151    83 QWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQPTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKNCPKAM 500
Cdd:cd14151   163 FEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAM 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 501 KRLVADCVKKVKEERPLFPQILSSIELLQHSL 532
Cdd:cd14151   243 KRLMAECLKKKRDERPLFPQILASIELLARSL 274
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
274-525 2.91e-107

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 321.41  E-value: 2.91e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-DVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSSLYKH 351
Cdd:cd13999     1 IGSGSFGEVYKGKWRGtDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPpPLCIVTEYMPGGSLYDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGSVLWM 431
Cdd:cd13999    81 LHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKN--STTEKMTGVVGTPRWM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 432 APEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPdlsrLYKNCPKAMKRLVADCVKKV 511
Cdd:cd13999   159 APEVLRGE---PYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPP----IPPDCPPELSKLIKRCWNED 231
                         250
                  ....*....|....
gi 1720416759 512 KEERPLFPQILSSI 525
Cdd:cd13999   232 PEKRPSFSEIVKRL 245
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
267-529 2.13e-79

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 250.73  E-value: 2.13e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 267 EVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEG 345
Cdd:cd14063     1 ELEIKEVIGKGRFGRVHRGRWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGAcMDPPHLAIVTSLCKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVkIGDFGLATVKSRWSGSQQVEQ-- 423
Cdd:cd14063    81 RTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLFSLSGLLQPGRREDTlv 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 -PTGSVLWMAPEVIR-------MQDDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGYASPdLSRLykN 495
Cdd:cd14063   160 iPNGWLCYLAPEIIRalspdldFEESLPFTKASDVYAFGTVWYELLAGRWPFKE-QPAESIIWQVGCGKKQS-LSQL--D 235
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 496 CPKAMKRLVADCVKKVKEERPLFPQILSSIELLQ 529
Cdd:cd14063   236 IGREVKDILMQCWAYDPEKRPTFSDLLRMLERLP 269
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
268-525 5.38e-73

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 233.54  E-value: 5.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 268 VMLSTRIGSGSFGTVYKGKWHGD-------VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIV 339
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEgentkikVAVKTLKE-GADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGePLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQ 419
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYaspdlsRLYK--NC 496
Cdd:pfam07714 160 KRGGGKLPIKWMAPESLK---DGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE-VLEFLEDGY------RLPQpeNC 229
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:pfam07714 230 PDELYDLMKQCWAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
270-525 6.76e-67

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 217.78  E-value: 6.76e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  270 LSTRIGSGSFGTVYKGKWHG-------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQ 341
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKLKGkggkkkvEVAVKTLKE-DASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEePLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  342 WCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSR-WSGSQQ 420
Cdd:smart00219  82 YMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL----SRdLYDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  421 VEQPTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYaspdlsRLYK--N 495
Cdd:smart00219 158 YRKRGGKlpIRWMAPESLK---EGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEE-VLEYLKNGY------RLPQppN 227
                          250       260       270
                   ....*....|....*....|....*....|
gi 1720416759  496 CPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:smart00219 228 CPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
268-525 1.12e-65

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 214.72  E-value: 1.12e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  268 VMLSTRIGSGSFGTVYKGKWHG-------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIV 339
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGkgdgkevEVAVKTLKE-DASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEePLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  340 TQWCEGSSLYKHLHV-QETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGS 418
Cdd:smart00221  80 MEYMPGGDLLDYLRKnRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGL----SRDLYD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  419 QQVEQPTGS---VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYaspdlsRLYK 494
Cdd:smart00221 156 DDYYKVKGGklpIRWMAPESLK---EGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAE-VLEYLKKGY------RLPK 225
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1720416759  495 --NCPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:smart00221 226 ppNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
274-526 6.11e-63

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 207.39  E-value: 6.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGS 346
Cdd:cd00192     3 LGEGAFGEVYKGKLKGgdgktvDVAVKTLKE-DASESERKDFLKEARVMKKLGHPNVVRLLGvCTEEEPLYLVMEYMEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHL--------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRW-SG 417
Cdd:cd00192    82 DLLDFLrksrpvfpSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGL----SRDiYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVL---WMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIFMVGRGYaspdlsRLY 493
Cdd:cd00192   158 DDYYRKKTGGKLpirWMAPESLK---DGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSN-EEVLEYLRKGY------RLP 227
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 494 K--NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd00192   228 KpeNCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
274-530 1.85e-61

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 203.15  E-value: 1.85e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  274 IGSGSFGTVYKGKWHGD---VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:smart00220   7 LGEGSFGKVYLARDKKTgklVAIKVIKK-KKIKKDRERILREIKILKKLKHPNIVRLYDvFEDEDKLYLVMEYCEGGDLF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  350 KHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQPTGSVL 429
Cdd:smart00220  86 DLLK-KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR---QLDPGEKLTTFVGTPE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  430 WMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYasPDLSRLYKNCPKAMKRLVADCVK 509
Cdd:smart00220 162 YMAPEVLL---GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPK--PPFPPPEWDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|.
gi 1720416759  510 KVKEERPlfpqilSSIELLQH 530
Cdd:smart00220 237 KDPEKRL------TAEEALQH 251
Pkinase pfam00069
Protein kinase domain;
269-524 5.47e-58

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 192.84  E-value: 5.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 269 MLSTRIGSGSFGTVYKGK---WHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCE 344
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKAKhrdTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDaFEDKDNLYLVLEYVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQeTKFQMFQLIDIARQTAQGMDylhakniihrdmksnniflhegltvkigdfglatvksrwsGSQQVEQP 424
Cdd:pfam00069  82 GGSLFDLLSEK-GAFSEREAKFIMKQILEGLE----------------------------------------SGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 TGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPdlsRLYKNCPKAMKRLV 504
Cdd:pfam00069 121 VGTPWYMAPEVLG---GNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFP---ELPSNLSEEAKDLL 194
                         250       260
                  ....*....|....*....|
gi 1720416759 505 ADCVKKVKEERPLFPQILSS 524
Cdd:pfam00069 195 KKLLKKDPSKRLTATQALQH 214
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
261-532 9.38e-54

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 183.38  E-value: 9.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD--VAVKILKvvdPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LA 337
Cdd:cd05068     3 WEIDRKSLKLLRKLGSGQFGEVWEGLWNNTtpVAVKTLK---PGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEpIY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrWSG 417
Cdd:cd05068    80 IITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARV---IKV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGS---VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPDLSrly 493
Cdd:cd05068   157 EDEYEAREGAkfpIKWTAPEAANY---NRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNA-EVLQQVERGYRMPCPP--- 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 494 kNCPKAMKRLVADCVKKVKEERPLFpqilssiELLQHSL 532
Cdd:cd05068   230 -NCPPQLYDIMLECWKADPMERPTF-------ETLQWKL 260
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
274-534 1.48e-53

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 183.29  E-value: 1.48e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSSLYKHL 352
Cdd:cd14153     8 IGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGAcMSPPHLAIITSLCKGRTLYSVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 353 HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVkIGDFGLATVKSRWSGSQQVEQ---PTGSVL 429
Cdd:cd14153    88 RDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVV-ITDFGLFTISGVLQAGRREDKlriQSGWLC 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 430 WMAPEVIRM------QDDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGyASPDLSRLykncpkAMKRL 503
Cdd:cd14153   167 HLAPEIIRQlspeteEDKLPFSKHSDVFAFGTIWYELHAREWPFKT-QPAEAIIWQVGSG-MKPNLSQI------GMGKE 238
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 504 VAD----CVKKVKEERPLFPQILSSIEllqhSLPK 534
Cdd:cd14153   239 ISDillfCWAYEQEERPTFSKLMEMLE----KLPK 269
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
267-542 1.02e-51

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 178.62  E-value: 1.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 267 EVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEG 345
Cdd:cd14152     1 QIELGELIGQGRWGKVHRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGAcMHPPHLAIITSFCKG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTV--KIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd14152    81 RTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVQEGRRENELKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGSVLWMAPEVIRM------QDDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGYAspdLSRLYKNCP 497
Cdd:cd14152   161 PHDWLCYLAPEIVREmtpgkdEDCLPFSKAADVYAFGTIWYELQARDWPLKN-QPAEALIWQIGSGEG---MKQVLTTIS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 498 --KAMKRLVADCVKKVKEERPLFPQILSSIEllqhSLPKINRSASEP 542
Cdd:cd14152   237 lgKEVTEILSACWAFDLEERPSFTLLMDMLE----KLPKLNRRLSHP 279
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
274-525 2.39e-51

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 176.88  E-value: 2.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd08215     8 IGKGSFGSAYLVRRKSDgklYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYEsFEENGKLCIVMEYADGGDLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQMF---QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTG 426
Cdd:cd08215    88 QKIKKQKKKGQPFpeeQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLE--STTDLAKTVVG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGYASPdLSRLYkncPKAMKRLVAD 506
Cdd:cd08215   166 TPYYLSPELCE---NKPYNYKSDIWALGCVLYELCTLKHPFEA-NNLPALVYKIVKGQYPP-IPSQY---SSELRDLVNS 237
                         250
                  ....*....|....*....
gi 1720416759 507 CVKKVKEERPLFPQILSSI 525
Cdd:cd08215   238 MLQKDPEKRPSANEILSSP 256
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
274-530 7.92e-51

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 175.40  E-value: 7.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEGSSLY 349
Cdd:cd06606     8 LGKGSFGSVYLALNLDTgelMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTErTENTLNIFLEYVPGGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHvqetKFQMFQLIDI---ARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTG 426
Cdd:cd06606    88 SLLK----KFGKLPEPVVrkyTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEGTKSLRG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSrlyKNCPKAMKRLVAD 506
Cdd:cd06606   164 TPYWMAPEVIR---GEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKIGSSGEPPPIP---EHLSEEAKDFLRK 237
                         250       260
                  ....*....|....*....|....
gi 1720416759 507 CVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06606   238 CLQRDPKKRP------TADELLQH 255
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
273-516 1.59e-50

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 174.70  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKILKV-VDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd14014     7 LLGRGGMGEVYRArdtLLGRPVAIKVLRPeLAEDEEFRERFLREARALARLSHPNIVrVYDVGEDDGRPYIVMEYVEGGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwSGSQQVEQPTGS 427
Cdd:cd14014    87 LADLLR-ERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGD-SGLTQTGSVLGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVgrGYASPDLSRLYKNCPKAMKRLVADC 507
Cdd:cd14014   165 PAYMAPEQAR---GGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHL--QEAPPPPSPLNPDVPPALDAIILRA 239

                  ....*....
gi 1720416759 508 VKKVKEERP 516
Cdd:cd14014   240 LAKDPEERP 248
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
273-532 2.15e-50

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 174.01  E-value: 2.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG--DVAVKILKVVDPTPEqlqAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSSLY 349
Cdd:cd05034     2 KLGAGQFGEVWMGVWNGttKVAVKTLKPGTMSPE---AFLQEAQIMKKLRHDKLVQLYAVCSDeEPIYIVTELMSKGSLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRWSGSQQVEQPtg 426
Cdd:cd05034    79 DYLRTGEgRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLieDDEYTAREGAKFP-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 sVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPDLSrlykNCPKAMKRLVA 505
Cdd:cd05034   157 -IKWTAPEAAL---YGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNR-EVLEQVERGYRMPKPP----GCPDELYDIML 227
                         250       260
                  ....*....|....*....|....*..
gi 1720416759 506 DCVKKVKEERPLFpqilssiELLQHSL 532
Cdd:cd05034   228 QCWKKEPEERPTF-------EYLQSFL 247
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
273-530 2.37e-50

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 173.93  E-value: 2.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKVVdpTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSL 348
Cdd:cd05122     7 KIGKGGFGVVYKARHKKTgqiVAIKKINLE--SKEKKESILNEIAILKKCKHPNIVKYYGsYLKKDELWIVMEFCSGGSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsgSQQVEQPTGSV 428
Cdd:cd05122    85 KDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSD---GKTRNTFVGTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRGYAsPDLSRLYKNcPKAMKRLVADCV 508
Cdd:cd05122   162 YWMAPEVIQ---GKPYGFKADIWSLGITAIEMAEGKPPY-SELPPMKALFLIATNGP-PGLRNPKKW-SKEFKDFLKKCL 235
                         250       260
                  ....*....|....*....|..
gi 1720416759 509 KKVKEERPlfpqilSSIELLQH 530
Cdd:cd05122   236 QKDPEKRP------TAEQLLKH 251
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
274-533 1.12e-49

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 172.24  E-value: 1.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-DVAVKIlkvVDPTPEQlQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKH 351
Cdd:cd14058     1 VGRGSFGVVCKARWRNqIVAVKI---IESESEK-KAFEVEVRQLSRVDHPNIIKLYGACSNQKpVCLVMEYAEGGSLYNV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LHVQETK--FQMFQLIDIARQTAQGMDYLHA---KNIIHRDMKSNNIFLHEGLTV-KIGDFGLATVKSRWSGSQQveqpt 425
Cdd:cd14058    77 LHGKEPKpiYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDISTHMTNNK----- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 GSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAHINN-RDQIIFMVGRGYASPdlsrLYKNCPKAMKRLV 504
Cdd:cd14058   152 GSAAWMAPEVF---EGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGpAFRIMWAVHNGERPP----LIKNCPKPIESLM 224
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 505 ADCVKKVKEERPLFPQILSSIELLQHSLP 533
Cdd:cd14058   225 TRCWSKDPEKRPSMKEIVKIMSHLMQFFP 253
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
274-460 3.13e-49

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 169.76  E-value: 3.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTpEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd00180     1 LGKGSFGKVYKARDKETgkkVAVKVIPKEKLK-KLLEELLREIEILKKLNHPNIVKLYDvFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVL 429
Cdd:cd00180    80 DLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTPPY 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720416759 430 WMAPEvirMQDDNPFSFQSDVYSYGIVLYEL 460
Cdd:cd00180   160 YAPPE---LLGGRYYGPKVDIWSLGVILYEL 187
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
273-548 1.03e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.97  E-value: 1.03e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG---DVAVKILKV-VDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSS 347
Cdd:COG0515    14 LLGRGGMGVVYLARDLRlgrPVALKVLRPeLAADPEARERFRREARALARLNHPNIVRVYDVGEEDGrPYLVMEYVEGES 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwSGSQQVEQPTGS 427
Cdd:COG0515    94 LADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGG-ATLTQTGTVVGT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGyASPDLSRLYKNCPKAMKRLVADC 507
Cdd:COG0515   172 PGYMAPEQARGE---PVDPRSDVYSLGVTLYELLTGRPPFDG-DSPAELLRAHLRE-PPPPPSELRPDLPPALDAIVLRA 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 508 VKKVKEERPlfpqilSSIELLQHSLPKINRSASEPSLHRAA 548
Cdd:COG0515   247 LAKDPEERY------QSAAELAAALRAVLRSLAAAAAAAAA 281
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
274-526 1.47e-48

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 169.50  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-VAVKILKVvDPTPE---QLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSSL 348
Cdd:cd14061     2 IGVGGFGKVYRGIWRGEeVAVKAARQ-DPDEDisvTLENVRQEARLFWMLRHPNIIALRGVCLQPpNLCLVMEYARGGAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHL-------HVqetkfqmfqLIDIARQTAQGMDYLHAKN---IIHRDMKSNNIFLHEGL--------TVKIGDFGLAt 410
Cdd:cd14061    81 NRVLagrkippHV---------LVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIenedlenkTLKITDFGLA- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 411 vkSRWSGSQQVEQpTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHINNrdqiiFMVGRGYASPDLS 490
Cdd:cd14061   151 --REWHKTTRMSA-AGTYAWMAPEVIKSS---TFSKASDVWSYGVLLWELLTGEVPYKGIDG-----LAVAYGVAVNKLT 219
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720416759 491 -RLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd14061   220 lPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLE 256
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
261-528 1.23e-46

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 164.06  E-value: 1.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKVVDPTpeqLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAI 338
Cdd:cd05039     1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQkVAVKCLKDDSTA---AQAFLAEASVMTTLRHPNLVQLLGVvLEGNGLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHL-----HVQETKfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvks 413
Cdd:cd05039    78 VTEYMAKGSLVDYLrsrgrAVITRK----DQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 rwSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGY--ASPDls 490
Cdd:cd05039   151 --EASSNQDGGKLPIKWTAPEALR---EKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKD-VVPHVEKGYrmEAPE-- 222
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720416759 491 rlykNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05039   223 ----GCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
261-526 4.53e-46

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 163.29  E-value: 4.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD--VAVKILKvvdPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LA 337
Cdd:cd05072     2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNStkVAVKTLK---PGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEpIY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSR 414
Cdd:cd05072    79 IITEYMAKGSLLDFLKSDEgGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVieDNE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYASPDLsrly 493
Cdd:cd05072   159 YTAREGAKFP---IKWTAPEAINF---GSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSD-VMSALQRGYRMPRM---- 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 494 KNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05072   228 ENCPDELYDIMKTCWKEKAEERPTFDYLQSVLD 260
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
263-523 2.15e-45

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 161.00  E-value: 2.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHG------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN- 335
Cdd:cd05033     1 IDASYVTIEKVIGGGEFGEVCSGSLKLpgkkeiDVAIKTLKS-GYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRW 415
Cdd:cd05033    80 VMIVTEYMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYASPDLsrlyK 494
Cdd:cd05033   160 EATYTTKGGKIPIRWTAPEAIAYRK---FTSASDVWSFGIVMWEVMSyGERPYWDMSNQD-VIKAVEDGYRLPPP----M 231
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd05033   232 DCPSALYQLMLDCWQKDRNERPTFSQIVS 260
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
274-527 2.35e-45

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 159.97  E-value: 2.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-VAVKilKVVDPTpeqlqafRNEVAVLRKTRHVNILLFMGYMTKDNL-AIVTQWCEGSSLYKH 351
Cdd:cd14059     1 LGSGAQGAVFLGKFRGEeVAVK--KVRDEK-------ETDIKHLRKLNHPNIIKFKGVCTQAPCyCILMEYCPYGQLYEV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQPTGSVLWM 431
Cdd:cd14059    72 LR-AGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSK---ELSEKSTKMSFAGTVAWM 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 432 APEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHInnrDQIIFMVGRGYASPDLSrLYKNCPKAMKRLVADCVKKV 511
Cdd:cd14059   148 APEVIR---NEPCSEKVDIWSFGVVLWELLTGEIPYKDV---DSSAIIWGVGSNSLQLP-VPSTCPDGFKLLMKQCWNSK 220
                         250
                  ....*....|....*.
gi 1720416759 512 KEERPLFPQILSSIEL 527
Cdd:cd14059   221 PRNRPSFRQILMHLDI 236
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
261-518 4.86e-45

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 159.91  E-value: 4.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKW--HGDVAVKILKVVDPTpeQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLA 337
Cdd:cd05148     1 WERPREEFTLERKLGSGYFGEVWEGLWknRVRVAIKILKSDDLL--KQQDFQKEVQALKRLRHKHLIsLFAVCSVGEPVY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV-KSRW 415
Cdd:cd05148    79 IITELMEKGSLLAFLRSPEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLiKEDV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPtgsVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPDLSRlyk 494
Cdd:cd05148   159 YLSSDKKIP---YKWTAPEAASHGT---FSTKSDVWSFGILLYEMFTyGQVPYPGMNNH-EVYDQITAGYRMPCPAK--- 228
                         250       260
                  ....*....|....*....|....
gi 1720416759 495 nCPKAMKRLVADCVKKVKEERPLF 518
Cdd:cd05148   229 -CPQEIYKIMLECWAAEPEDRPSF 251
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
274-528 7.12e-45

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 159.75  E-value: 7.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG--DVAVKILKVVDPtPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSSLYK 350
Cdd:cd14066     1 IGSGGFGTVYKGVLENgtVVAVKRLNEMNC-AASKKEFLTELEMLGRLRHPNLVRLLGYcLESDEKLLVYEYMPNGSLED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLHVQETKFQM--FQLIDIARQTAQGMDYLH---AKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPT 425
Cdd:cd14066    80 RLHCHKGSPPLpwPQRLKIAKGIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSAVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 GSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI-----IFM-----VGRGYASPDLSRLYKN 495
Cdd:cd14066   160 GTIGYLAPEYIRT---GRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRkdlveWVEskgkeELEDILDKRLVDDDGV 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 496 CPKAMK---RLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd14066   237 EEEEVEallRLALLCTRSDPSLRPSMKEVVQMLEKL 272
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
273-526 3.53e-44

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 157.39  E-value: 3.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG--DVAVKILKVVDPTPEqlqAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYK 350
Cdd:cd14203     2 KLGQGCFGEVWMGTWNGttKVAIKTLKPGTMSPE---AFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSLLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLHVQETKF-QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRWSGSQQVEQPtgs 427
Cdd:cd14203    79 FLKDGEGKYlKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLieDNEYTARQGAKFP--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPdlsrLYKNCPKAMKRLVAD 506
Cdd:cd14203   156 IKWTAPEAALY---GRFTIKSDVWSFGILLTELVTkGRVPYPGMNNR-EVLEQVERGYRMP----CPPGCPESLHELMCQ 227
                         250       260
                  ....*....|....*....|
gi 1720416759 507 CVKKVKEERPLFPQILSSIE 526
Cdd:cd14203   228 CWRKDPEERPTFEYLQSFLE 247
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
261-526 2.47e-43

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 156.00  E-value: 2.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD--VAVKILKVVDPTPEqlqAFRNEVAVLRKTRHVNILLFMGYMTKDNLAI 338
Cdd:cd05070     4 WEIPRESLQLIKRLGNGQFGEVWMGTWNGNtkVAIKTLKPGTMSPE---SFLEEAQIMKKLKHDKLVQLYAVVSEEPIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRW 415
Cdd:cd05070    81 VTEYMSKGSLLDFLKDGEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLieDNEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPdlsrLYK 494
Cdd:cd05070   161 TARQGAKFP---IKWTAPEAALY---GRFTIKSDVWSFGILLTELVTkGRVPYPGMNNR-EVLEQVERGYRMP----CPQ 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05070   230 DCPISLHELMIHCWKKDPEERPTFEYLQGFLE 261
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
261-526 3.33e-43

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 155.04  E-value: 3.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD--VAVKILKVVDPTPEqlqAFRNEVAVLRKTRHVNILLFMGYMTKDNLAI 338
Cdd:cd05067     2 WEVPRETLKLVERLGAGQFGEVWMGYYNGHtkVAIKSLKQGSMSPD---AFLAEANLMKQLQHQRLVRLYAVVTQEPIYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRW 415
Cdd:cd05067    79 ITEYMENGSLVDFLKTPSgIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLieDNEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIFMVGRGY--ASPDlsrl 492
Cdd:cd05067   159 TAREGAKFP---IKWTAPEAINY---GTFTIKSDVWSFGILLTEIVThGRIPYPGMTN-PEVIQNLERGYrmPRPD---- 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 493 ykNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05067   228 --NCPEELYQLMRLCWKERPEDRPTFEYLRSVLE 259
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
261-526 3.71e-43

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 155.61  E-value: 3.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--DVAVKILKVVDPTPEqlqAFRNEVAVLRKTRHVNILLFMGYMTKDNLAI 338
Cdd:cd05069     7 WEIPRESLRLDVKLGQGCFGEVWMGTWNGttKVAIKTLKPGTMMPE---AFLQEAQIMKKLRHDKLVPLYAVVSEEPIYI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHLHVQETKF-QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRW 415
Cdd:cd05069    84 VTEFMGKGSLLDFLKEGDGKYlKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLieDNEY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPdlsrLYK 494
Cdd:cd05069   164 TARQGAKFP---IKWTAPEAALY---GRFTIKSDVWSFGILLTELVTkGRVPYPGMVNR-EVLEQVERGYRMP----CPQ 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05069   233 GCPESLHELMKLCWKKDPDERPTFEYIQSFLE 264
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
270-466 4.09e-43

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 154.56  E-value: 4.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEG 345
Cdd:cd05117     4 LGKVLGRGSFGVVRLAVHKKTgeeYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEvFEDDKNLYLVMELCTG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLATvksRWSGSQQVE 422
Cdd:cd05117    84 GELFDRI-VKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAK---IFEEGEKLK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 423 QPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELP 466
Cdd:cd05117   160 TVCGTPYYVAPEVLK---GKGYGKKCDIWSLGVILYILLCGYPP 200
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
261-526 4.25e-42

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 152.53  E-value: 4.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--DVAVKILKVVDPTPEqlqAFRNEVAVLRKTRHVNILLFMGYMTKDNLAI 338
Cdd:cd05071     4 WEIPRESLRLEVKLGQGCFGEVWMGTWNGttRVAIKTLKPGTMSPE---AFLQEAQVMKKLRHEKLVQLYAVVSEEPIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHLHVQETKF-QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRW 415
Cdd:cd05071    81 VTEYMSKGSLLDFLKGEMGKYlRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLieDNEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPDLSRlyk 494
Cdd:cd05071   161 TARQGAKFP---IKWTAPEAALY---GRFTIKSDVWSFGILLTELTTkGRVPYPGMVNR-EVLDQVERGYRMPCPPE--- 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 495 nCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05071   231 -CPESLHDLMCQCWRKEPEERPTFEYLQAFLE 261
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
273-530 1.19e-41

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 150.53  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGK--WHGD-VAVKILKVVDPtpEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSL 348
Cdd:cd06613     7 RIGSGTYGDVYKARniATGElAAVKVIKLEPG--DDFEIIQQEISMLKECRHPNIVAYFGsYLRRDKLWIVMEYCGGGSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQveQPTGSV 428
Cdd:cd06613    85 QDIYQVTGP-LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRK--SFIGTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKNCPKaMKRLVADCV 508
Cdd:cd06613   162 YWMAPEVAAVERKGGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFDPPKLKDKEKWSPD-FHDFIKKCL 240
                         250       260
                  ....*....|....*....|..
gi 1720416759 509 KKVKEERPlfpqilSSIELLQH 530
Cdd:cd06613   241 TKNPKKRP------TATKLLQH 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
269-530 1.47e-41

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 150.45  E-value: 1.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 269 MLSTRIGSGSFGTVYKG--KWHGD-VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCE 344
Cdd:cd06627     3 QLGDLIGRGAFGSVYKGlnLNTGEfVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVkTKDSLYIILEYVE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHvqetKFQMFQLIDIARQTAQ---GMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQV 421
Cdd:cd06627    83 NGSLASIIK----KFGKFPESLVAVYIYQvleGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLN--EVEKDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAhinNRDQIIFMvgrgYA--SPDLSRLYKNCPKA 499
Cdd:cd06627   157 NSVVGTPYWMAPEVIEMS---GVTTASDIWSVGCTVIELLTGNPPYY---DLQPMAAL----FRivQDDHPPLPENISPE 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720416759 500 MKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06627   227 LRDFLLQCFQKDPTLRP------SAKELLKH 251
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
263-528 2.95e-41

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 150.02  E-value: 2.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTV------YKGKWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNL 336
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVcsgrlkLPGKREIPVAIKTLKA-GYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 A-IVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrw 415
Cdd:cd05066    80 VmIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLE-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPTGS---VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYASPDLsr 491
Cdd:cd05066   158 DDPEAAYTTRGGkipIRWTAPEAIAYRK---FTSASDVWSYGIVMWEVMSyGERPYWEMSNQD-VIKAIEEGYRLPAP-- 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720416759 492 lyKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05066   232 --MDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKL 266
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
263-525 3.09e-41

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 149.52  E-value: 3.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHG--DVAVKILKVVDPTPEQlqaFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIV 339
Cdd:cd05059     1 IDPSELTFLKELGSGQFGVVHLGKWRGkiDVAIKMIKEGSMSEDD---FIEEAKVMMKLSHPKLVQLYGVCTKQRpIFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA--TVKSRWSG 417
Cdd:cd05059    78 TEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLAryVLDDEYTS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPtgsVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIFMVGRGYaspdlsRLYK-- 494
Cdd:cd05059   158 SVGTKFP---VKWSPPEVF---MYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSN-SEVVEHISQGY------RLYRph 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd05059   225 LAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
273-525 8.64e-41

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 147.98  E-value: 8.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKVVDPtPEQLQAFRNEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQWCEGSSL 348
Cdd:cd05041     2 KIGRGNFGDVYRGVLKPDnteVAVKTCRETLP-PDLKRKFLQEARILKQYDHPNIVKLIGVCVqKQPIMIVMELVPGGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA-----TVKSRWSGSQQVeq 423
Cdd:cd05041    81 LTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSreeedGEYTVSDGLKQI-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 ptgSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGY--ASPDLsrlyknCPKAM 500
Cdd:cd05041   159 ---PIKWTAPEALNY---GRYTSESDVWSFGILLWEIFSlGATPYPGMSNQ-QTREQIESGYrmPAPEL------CPEAV 225
                         250       260
                  ....*....|....*....|....*
gi 1720416759 501 KRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd05041   226 YRLMLQCWAYDPENRPSFSEIYNEL 250
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
262-525 9.57e-41

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 148.65  E-value: 9.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKVvDP---TPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NL 336
Cdd:cd14145     2 EIDFSELVLEEIIGIGGFGKVYRAIWIGDeVAVKAARH-DPdedISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEpNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSSLYKHLHVQETKFQMfqLIDIARQTAQGMDYLHAKNI---IHRDMKSNNIFLHEGL--------TVKIGD 405
Cdd:cd14145    81 CLVMEFARGGPLNRVLSGKRIPPDI--LVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKVengdlsnkILKITD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 406 FGLAtvkSRWSGSQQVeQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNrdqiiFMVGRGYA 485
Cdd:cd14145   159 FGLA---REWHRTTKM-SAAGTYAWMAPEVIR---SSMFSKGSDVWSYGVLLWELLTGEVPFRGIDG-----LAVAYGVA 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 486 SPDLS-RLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd14145   227 MNKLSlPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQL 267
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
274-531 1.11e-40

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 147.80  E-value: 1.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILkvvdPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd06612    11 LGEGSYGSVYKAIHKETgqvVAIKVV----PVEEDLQEIIKEISILKQCDSPYIVKYYGsYFKNTDLWIVMEYCGAGSVS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGSVL 429
Cdd:cd06612    87 DIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLT--DTMAKRNTVIGTPF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 430 WMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQiIFMVGR----GYASPdlsrlyKNCPKAMKRLVA 505
Cdd:cd06612   165 WMAPEVIQ---EIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRA-IFMIPNkpppTLSDP------EKWSPEFNDFVK 234
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 506 DCVKKVKEERPlfpqilSSIELLQHS 531
Cdd:cd06612   235 KCLVKDPEERP------SAIQLLQHP 254
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
274-518 1.35e-40

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 147.98  E-value: 1.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK---WHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd13978     1 LGSGGFGTVSKARhvsWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGvCVERRSLGLVMEYMENGSLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQET------KFQmfqlidIARQTAQGMDYLH--AKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrWSGSQQV 421
Cdd:cd13978    81 SLLEREIQdvpwslRFR------IIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGM-KSISANR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPT----GSVLWMAPEVIRMQDDNPfSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYAS--PDLSRLYKN 495
Cdd:cd13978   154 RRGTenlgGTPIYMAPEAFDDFNKKP-TSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQIVSKGDRPslDDIGRLKQI 232
                         250       260
                  ....*....|....*....|....
gi 1720416759 496 -CPKAMKRLVADCVKKVKEERPLF 518
Cdd:cd13978   233 eNVQELISLMIRCWDGNPDARPTF 256
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
274-528 2.26e-40

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 147.44  E-value: 2.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-VAVKILKVvDP------TPEQLqafRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEG 345
Cdd:cd14148     2 IGVGGFGKVYKGLWRGEeVAVKAARQ-DPdediavTAENV---RQEARLFWMLQHPNIIALRGVCLNPpHLCLVMEYARG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQMfqLIDIARQTAQGMDYLHAKN---IIHRDMKSNNIFLHE--------GLTVKIGDFGLAtvkSR 414
Cdd:cd14148    78 GALNRALAGKKVPPHV--LVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpienddlsGKTLKITDFGLA---RE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVeQPTGSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMAGELPYAHINnrdqiIFMVGRGYASPDLS-RLY 493
Cdd:cd14148   153 WHKTTKM-SAAGTYAWMAPEVIRL---SLFSKSSDVWSFGVLLWELLTGEVPYREID-----ALAVAYGVAMNKLTlPIP 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 494 KNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd14148   224 STCPEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
261-526 2.65e-40

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 147.48  E-value: 2.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKW--HGDVAVKILKvvdPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAI 338
Cdd:cd05073     6 WEIPRESLKLEKKLGAGQFGEVWMATYnkHTKVAVKTMK---PGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRW 415
Cdd:cd05073    83 ITEFMAKGSLLDFLKSDEgSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVieDNEY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIFMVGRGYASPDLsrlyK 494
Cdd:cd05073   163 TAREGAKFP---IKWTAPEAINF---GSFTIKSDVWSFGILLMEIVTyGRIPYPGMSN-PEVIRALERGYRMPRP----E 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05073   232 NCPEELYNIMMRCWKNRPEERPTFEYIQSVLD 263
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
263-528 3.63e-40

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 146.94  E-value: 3.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKG------KWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN- 335
Cdd:cd05065     1 IDVSCVKIEEVIGAGEFGEVCRGrlklpgKREIFVAIKTLKS-GYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRW 415
Cdd:cd05065    80 VMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPTGS---VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYASPDLSr 491
Cdd:cd05065   160 TSDPTYTSSLGGkipIRWTAPEAIAYRK---FTSASDVWSYGIVMWEVMSyGERPYWDMSNQD-VINAIEQDYRLPPPM- 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720416759 492 lykNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05065   235 ---DCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKM 268
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
267-528 4.77e-40

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 146.71  E-value: 4.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 267 EVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKVvDPTPE---QLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQ 341
Cdd:cd14147     4 ELRLEEVIGIGGFGKVYRGSWRGElVAVKAARQ-DPDEDisvTAESVRQEARLFAMLAHPNIIALKAVcLEEPNLCLVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHVQETKFQMfqLIDIARQTAQGMDYLHAKNI---IHRDMKSNNIFL--------HEGLTVKIGDFGLAt 410
Cdd:cd14147    83 YAAGGPLSRALAGRRVPPHV--LVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLlqpienddMEHKTLKITDFGLA- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 411 vkSRWSGSQQVEQpTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNrdqiiFMVGRGYASPDLS 490
Cdd:cd14147   160 --REWHKTTQMSA-AGTYAWMAPEVIK---ASTFSKGSDVWSFGVLLWELLTGEVPYRGIDC-----LAVAYGVAVNKLT 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 491 -RLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd14147   229 lPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
261-526 4.79e-40

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 146.72  E-value: 4.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILkVVDPTPEQLQAFRNEVAVLRK--TRHVNILL---- 326
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAKGvvkgepetRVAIKTV-NENASMRERIEFLNEASVMKEfnCHHVVRLLgvvs 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 327 -------FMGYMTKDNLAIVTQWC----EGSSLYKHLHVQEtKFQMfqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFL 395
Cdd:cd05032    80 tgqptlvVMELMAKGDLKSYLRSRrpeaENNPGLGPPTLQK-FIQM------AAEIADGMAYLAAKKFVHRDLAARNCMV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 396 HEGLTVKIGDFGLAtvksRWSGSQQVEQPTGS----VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYElMA--GELPYAH 469
Cdd:cd05032   153 AEDLTVKIGDFGMT----RDIYETDYYRKGGKgllpVRWMAPESLK---DGVFTTKSDVWSFGVVLWE-MAtlAEQPYQG 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 470 INNRDQIIFMVGRGYAspdlsRLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05032   225 LSNEEVLKFVIDGGHL-----DLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
262-528 1.40e-39

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 145.50  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKG------KWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTK-D 334
Cdd:cd05063     1 EIHPSHITKQKVIGAGEFGEVFRGilkmpgRKEVAVAIKTLKP-GYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKfK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV-KS 413
Cdd:cd05063    80 PAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVlED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RWSGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPdlsrL 492
Cdd:cd05063   160 DPEGTYTTSGGKIPIRWTAPEAIAYRK---FTSASDVWSFGIVMWEVMSfGERPYWDMSNH-EVMKAINDGFRLP----A 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 493 YKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05063   232 PMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
274-526 1.54e-39

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 144.98  E-value: 1.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-VAVKILKVVD-PTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD--NLAIVTQWCEGSSLY 349
Cdd:cd14064     1 IGSGSFGKVYKGRCRNKiVAIKRYRANTyCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpsQFAIVTQYVSGGSLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQMFQLIDIARQTAQGMDYLH--AKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvKSRWSGSQQVE----Q 423
Cdd:cd14064    81 SLLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFG----ESRFLQSLDEDnmtkQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PtGSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPdlsrLYKNCPKAMKRL 503
Cdd:cd14064   157 P-GNLRWMAPEV--FTQCTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAYHHIRPP----IGYSIPKPISSL 229
                         250       260
                  ....*....|....*....|...
gi 1720416759 504 VADCVKKVKEERPLFPQILSSIE 526
Cdd:cd14064   230 LMRGWNAEPESRPSFVEIVALLE 252
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
275-526 1.70e-39

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 144.33  E-value: 1.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 275 GSGSFGTVYKGKW---HGDVAVKILKVVDptpeqlqafrNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSSLYK 350
Cdd:cd14060     2 GGGSFGSVYRAIWvsqDKEVAVKKLLKIE----------KEAEILSVLSHRNIIQFYGAILEaPNYGIVTEYASYGSLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLHVQET-KFQMFQLIDIARQTAQGMDYLHAK---NIIHRDMKSNNIFLHEGLTVKIGDFGlatvKSRWSGSQQVEQPTG 426
Cdd:cd14060    72 YLNSNESeEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFG----ASRFHSHTTHMSLVG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGYASPDLSrlyKNCPKAMKRLVAD 506
Cdd:cd14060   148 TFPWMAPEVIQ---SLPVSETCDTYSYGVVLWEMLTREVPFKGLEGL-QVAWLVVEKNERPTIP---SSCPRSFAELMRR 220
                         250       260
                  ....*....|....*....|
gi 1720416759 507 CVKKVKEERPLFPQILSSIE 526
Cdd:cd14060   221 CWEADVKERPSFKQIIGILE 240
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
273-521 2.06e-38

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 141.71  E-value: 2.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWH---GD---VAVKILKVVDPT-PEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05040     2 KLGDGSFGVVRRGEWTtpsGKviqVAVKCLKSDVLSqPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLMMVTELAPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGSQQ---VE 422
Cdd:cd05040    82 GSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGL----MRALPQNEdhyVM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTGSV--LWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYaspdlSRLYK--NCP 497
Cdd:cd05040   158 QEHRKVpfAWCAPESLKTRK---FSHASDVWMFGVTLWEMFTyGEEPWLGLNGS-QILEKIDKEG-----ERLERpdDCP 228
                         250       260
                  ....*....|....*....|....
gi 1720416759 498 KAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd05040   229 QDIYNVMLQCWAHKPADRPTFVAL 252
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
273-524 2.42e-38

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 141.78  E-value: 2.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVD----PTPEQLQAFrNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSS 347
Cdd:cd08529     7 KLGKGSFGVVYKVVRKVDGRVYALKQIDisrmSRKMREEAI-DEARVLSKLNSPYVIKYYdSFVDKGKLNIVMEYAENGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTG 426
Cdd:cd08529    86 LHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILS--DTTNFAQTIVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEvirMQDDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRGYASPdLSRLYKncpKAMKRLVAD 506
Cdd:cd08529   164 TPYYLSPE---LCEDKPYNEKSDVWALGCVLYELCTGKHPF-EAQNQGALILKIVRGKYPP-ISASYS---QDLSQLIDS 235
                         250
                  ....*....|....*...
gi 1720416759 507 CVKKVKEERPLFPQILSS 524
Cdd:cd08529   236 CLTKDYRQRPDTTELLRN 253
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
261-526 4.93e-38

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 140.78  E-value: 4.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKVvDPTPeqlQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIV 339
Cdd:cd05083     1 WLLNLQKLTLGEIIGEGEFGAVLQGEYMGQkVAVKNIKC-DVTA---QAFLEETAVMTKLQHKNLVRLLGVILHNGLYIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHLHVQ-ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrwsGS 418
Cdd:cd05083    77 MELMSKGNLVNFLRSRgRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV-----GS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGY--ASPDlsrlykN 495
Cdd:cd05083   152 MGVDNSRLPVKWTAPEALK---NKKFSSKSDVWSYGVLLWEVFSyGRAPYPKMSVK-EVKEAVEKGYrmEPPE------G 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720416759 496 CPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05083   222 CPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
274-530 8.01e-38

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 140.23  E-value: 8.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGkWHGD----VAVKILKVVD---PTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEG 345
Cdd:cd06632     8 LGSGSFGSVYEG-FNGDtgdfFAVKEVSLVDddkKSRESVKQLEQEIALLSKLRHPNIVQYYGTeREEDNLYIFLEYVPG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvqetKFQMFQLIDIA---RQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVE 422
Cdd:cd06632    87 GSIHKLLQ----RYGAFEEPVIRlytRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 qptGSVLWMAPEVIrMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGYASP----DLSrlykncPK 498
Cdd:cd06632   163 ---GSPYWMAPEVI-MQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGV-AAIFKIGNSGELPpipdHLS------PD 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 499 AmKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06632   232 A-KDFIRLCLQRDPEDRP------TASQLLEH 256
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
272-530 1.15e-37

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 139.65  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLqafRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSS 347
Cdd:cd06614     6 EKIGEGASGEVYKATDRATgkeVAIKKMRLRKQNKELI---INEILIMKECKHPNIVDYYDsYLVGDELWVVMEYMDGGS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksrwSGSQQVEQPT-- 425
Cdd:cd06614    83 LTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAA-----QLTKEKSKRNsv 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 -GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAhinnRD---QIIFMVgRGYASPDLSRLYKNCPKaMK 501
Cdd:cd06614   158 vGTPYWMAPEVIK---RKDYGPKVDIWSLGIMCIEMAEGEPPYL----EEpplRALFLI-TTKGIPPLKNPEKWSPE-FK 228
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 502 RLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06614   229 DFLNKCLVKDPEKRP------SAEELLQH 251
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
274-523 1.61e-37

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 139.19  E-value: 1.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLY 349
Cdd:cd14003     8 LGEGSFGKVKLArhkLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIkLYEVIETENKIYLVMEYASGGELF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KH------LHVQETKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQ 423
Cdd:cd14003    88 DYivnngrLSEDEARRFFQQLIS-------AVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN---EFRGGSLLKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGSVLWMAPEVIrmQDDNPFSFQSDVYSYGIVLYELMAGELPY--AHINNRDQIIFmvgRG------YASPDLSRLYKN 495
Cdd:cd14003   158 FCGTPAYAAPEVL--LGRKYDGPKADVWSLGVILYAMLTGYLPFddDNDSKLFRKIL---KGkypipsHLSPDARDLIRR 232
                         250       260
                  ....*....|....*....|....*...
gi 1720416759 496 CpkamkrLVADcvkkvKEERPLFPQILS 523
Cdd:cd14003   233 M------LVVD-----PSKRITIEEILN 249
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
273-526 1.98e-37

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 139.94  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG-DVAVKIL-KVVDPTPEQL-QAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSSL 348
Cdd:cd14158    22 KLGEGGFGVVFKGYINDkNVAVKKLaAMVDISTEDLtKQFEQEIQVMAKCQHENLVELLGYSCDgPQLCLVYTYMPNGSL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLH-VQETKFQMFQL-IDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTG 426
Cdd:cd14158   102 LDRLAcLNDTPPLSWHMrCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMTERIVG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRMQddnpFSFQSDVYSYGIVLYELMAGeLPYAHINNRDQIIFMVGR----------GYASPDLSRLYKNC 496
Cdd:cd14158   182 TTAYMAPEALRGE----ITPKSDIFSFGVVLLEIITG-LPPVDENRDPQLLLDIKEeiedeektieDYVDKKMGDWDSTS 256
                         250       260       270
                  ....*....|....*....|....*....|
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd14158   257 IEAMYSVASQCLNDKKNRRPDIAKVQQLLQ 286
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
274-525 2.56e-37

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 139.02  E-value: 2.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-DVAVKILKVvDPTPE---QLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSSL 348
Cdd:cd14146     2 IGVGGFGKVYRATWKGqEVAVKAARQ-DPDEDikaTAESVRQEAKLFSMLRHPNIIKLEGVcLEEPNLCLVMEFARGGTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQ--------LIDIARQTAQGMDYLHAKN---IIHRDMKSNNIFLHEGL--------TVKIGDFGLA 409
Cdd:cd14146    81 NRALAAANAAPGPRRarripphiLVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKIehddicnkTLKITDFGLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 tvkSRWSGSQQVEQpTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNrdqiiFMVGRGYASPDL 489
Cdd:cd14146   161 ---REWHRTTKMSA-AGTYAWMAPEVIK---SSLFSKGSDIWSYGVLLWELLTGEVPYRGIDG-----LAVAYGVAVNKL 228
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720416759 490 S-RLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd14146   229 TlPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
274-525 6.13e-37

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 138.19  E-value: 6.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd13996    14 LGSGGFGSVYKVRNKVDgvtYAIKKIRLTEKSSASEKVLR-EVKALAKLNHPNIVRYYTaWVEEPPLYIQMELCEGGTLR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQ--ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG-LTVKIGDFGLATV-----KSRWS----- 416
Cdd:cd13996    93 DWIDRRnsSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSignqkRELNNlnnnn 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 --GSQQVEQPTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMageLPYAHINNRDQIIFMVGRGYASPDLSRLYK 494
Cdd:cd13996   173 ngNTSNNSVGIGTPLYASPEQL---DGENYNEKADIYSLGIILFEML---HPFKTAMERSTILTDLRNGILPESFKAKHP 246
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720416759 495 NcpkaMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd13996   247 K----EADLIQSLLSKNPEERPSAEQLLRSL 273
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
274-528 1.11e-36

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 137.90  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKW--HGD-----VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD---NLAIVTQWC 343
Cdd:cd05038    12 LGEGHFGSVELCRYdpLGDntgeqVAVKSLQP-SGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrrSLRLIMEYL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd05038    91 PSGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEYYYVKE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGS-VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRGYASPDLSRLYK------- 494
Cdd:cd05038   171 PGESpIFWYAPECLR---ESRFSSASDVWSFGVTLYELFTyGDPSQSPPALFLRMIGIAQGQMIVTRLLELLKsgerlpr 247
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 495 --NCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05038   248 ppSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRL 283
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
262-521 2.17e-36

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 137.12  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTK 333
Cdd:cd05048     1 EIPLSAVRFLEELGEGAFGKVYKGELLGpsseesaiSVAIKTLKE-NASPKTQQDFRREAELMSDLQHPNIVCLLGVCTK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DN-LAIVTQWCEGSSLYKHL-------------HVQETKFQMFQ--LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE 397
Cdd:cd05048    80 EQpQCMLFEYMAHGDLHEFLvrhsphsdvgvssDDDGTASSLDQsdFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 398 GLTVKIGDFGLAtvKSRWSgSQQVEQPTGSVL---WMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNR 473
Cdd:cd05048   160 GLTVKISDFGLS--RDIYS-SDYYRVQSKSLLpvrWMPPEAILY---GKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQ 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 474 DqIIFMVgRG---YASPDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd05048   234 E-VIEMI-RSrqlLPCPE------DCPARVYSLMVECWHEIPSRRPRFKEI 276
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
261-526 2.58e-36

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 137.16  E-value: 2.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG---------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMGY 330
Cdd:cd05053     7 WELPRDRLTLGKPLGEGAFGQVVKAEAVGldnkpnevvTVAVKMLKD-DATEKDLSDLVSEMEMMKMIgKHKNIINLLGA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 331 MTKDN-LAIVTQWCEGSSLYKHL---------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIF 394
Cdd:cd05053    86 CTQDGpLYVVVEYASKGNLREFLrarrppgeeaspddpRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 395 LHEGLTVKIGDFGLAtvksRWSGSQQVEQPTGS----VLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMA-GELPYAH 469
Cdd:cd05053   166 VTEDNVMKIADFGLA----RDIHHIDYYRKTTNgrlpVKWMAPEAL---FDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 470 InNRDQIIFMVGRGYaspdlsRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05053   239 I-PVEELFKLLKEGH------RMEKpqNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLD 290
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
270-530 2.85e-36

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 135.82  E-value: 2.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKG--KWHG-DVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY---MTKDNLAIVTQWC 343
Cdd:cd13983     5 FNEVLGRGSFKTVYRAfdTEEGiEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSwesKSKKEVIFITELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLhvqetkfQMFQLIDI------ARQTAQGMDYLHAKN--IIHRDMKSNNIFL--HEGLtVKIGDFGLATVKs 413
Cdd:cd13983    85 TSGTLKQYL-------KRFKRLKLkvikswCRQILEGLNYLHTRDppIIHRDLKCDNIFIngNTGE-VKIGDLGLATLL- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 rwsgsqQVEQPTgSVL----WMAPEvirMQDDNpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDL 489
Cdd:cd13983   156 ------RQSFAK-SVIgtpeFMAPE---MYEEH-YDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPESL 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 490 SRLyKNcpKAMKRLVADCVKKvKEERPlfpqilSSIELLQH 530
Cdd:cd13983   225 SKV-KD--PELKDFIEKCLKP-PDERP------SARELLEH 255
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
263-522 1.16e-35

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 134.31  E-value: 1.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKIlKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQ 341
Cdd:cd05112     1 IDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAI-KTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQApICLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGSQQV 421
Cdd:cd05112    80 FMEHGCLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGM----TRFVLDDQY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGS---VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIFMVGRGYaspdlsRLYKN-- 495
Cdd:cd05112   156 TSSTGTkfpVKWSSPEVFSFSR---YSSKSDVWSFGVLMWEVFSeGKIPYENRSN-SEVVEDINAGF------RLYKPrl 225
                         250       260
                  ....*....|....*....|....*..
gi 1720416759 496 CPKAMKRLVADCVKKVKEERPLFPQIL 522
Cdd:cd05112   226 ASTHVYEIMNHCWKERPEDRPSFSLLL 252
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
274-474 1.36e-35

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 134.85  E-value: 1.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-------VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05057    15 LGSGAFGTVYKGVWIPEgekvkipVAIKVLRE-ETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQLITQLMPLG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTG 426
Cdd:cd05057    94 CLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGGKV 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 427 SVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRD 474
Cdd:cd05057   174 PIKWMALESIQYRI---YTHKSDVWSYGVTVWELMTfGAKPYEGIPAVE 219
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
261-526 2.60e-35

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 134.54  E-value: 2.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVDPTPEQlQAFRNEVAVLRKT-RHVNILLFMGYM 331
Cdd:cd05055    30 WEFPRNNLSFGKTLGAGAFGKVVEATAYGlsksdavmKVAVKMLKPTAHSSER-EALMSELKIMSHLgNHENIVNLLGAC 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDN-LAIVTQWCEGSSLYKHLHVQETKFQMFQ-LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd05055   109 TIGGpILVITEYCCYGDLLNFLRRKRESFLTLEdLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 tvKSRWSGSQQVEQptGS----VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRGY 484
Cdd:cd05055   189 --RDIMNDSNYVVK--GNarlpVKWMAPESIF---NCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGY 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 485 --ASPDLSrlykncPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05055   262 rmAQPEHA------PAEIYDIMKTCWDADPLKRPTFKQIVQLIG 299
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
267-516 6.61e-35

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 132.51  E-value: 6.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 267 EVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKVVDPTPEQLQAFRNEVAVLRkTRHVNILLFMGYMTKDNLA----IVTQ 341
Cdd:cd13979     4 PLRLQEPLGSGGFGSVYKATYKGEtVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVLAAETGTDFAslglIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvksrwsGSQQV 421
Cdd:cd13979    83 YCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFG---------CSVKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQP----------TGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHInnRDQIIFMVGRGYASPDLSR 491
Cdd:cd13979   154 GEGnevgtprshiGGTYTYRAPELLKGERVTP---KADIYSFGITLWQMLTRELPYAGL--RQHVLYAVVAKDLRPDLSG 228
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 492 LYKNCPK-AMKRLVADCVKKVKEERP 516
Cdd:cd13979   229 LEDSEFGqRLRSLISRCWSAQPAERP 254
C1_A_C-Raf cd20870
protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated ...
55-106 7.26e-35

protein kinase C conserved region 1 (C1 domain) found in A- and C-Raf (Rapidly Accelerated Fibrosarcoma) kinases, and similar proteins; This group includes A-Raf and C-Raf, both of which are serine/threonine-protein kinases. A-Raf, also called proto-oncogene A-Raf or proto-oncogene A-Raf-1, cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. C-Raf, also known as proto-oncogene Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around mid-gestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. Both A- and C-Raf are mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410420  Cd Length: 52  Bit Score: 125.07  E-value: 7.26e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759  55 LTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDW 106
Cdd:cd20870     1 LTTHNFVRKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDW 52
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
274-467 8.16e-35

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 131.61  E-value: 8.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEGSsLY 349
Cdd:cd14002     9 IGEGSFGKVYKGRRKYTgqvVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFeTKKEFVVVTEYAQGE-LF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGSVL 429
Cdd:cd14002    88 QILE-DDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS--CNTLVLTSIKGTPL 164
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720416759 430 WMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14002   165 YMAPELVQEQ---PYDHTADLWSLGCILYELFVGQPPF 199
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
263-526 1.31e-34

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 131.16  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHG--DVAVKILKVVDPTPEQlqaFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIV 339
Cdd:cd05113     1 IDPKDLTFLKELGTGQFGVVKYGKWRGqyDVAIKMIKEGSMSEDE---FIEEAKVMMNLSHEKLVQLYGVCTKQRpIFII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGSQ 419
Cdd:cd05113    78 TEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGL----SRYVLDD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPTGS---VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYaspdlsRLYKN 495
Cdd:cd05113   154 EYTSSVGSkfpVRWSPPEVLMY---SKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNS-ETVEHVSQGL------RLYRP 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 496 --CPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05113   224 hlASEKVYTIMYSCWHEKADERPTFKILLSNIL 256
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
274-528 3.31e-34

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 130.71  E-value: 3.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK--GKWHGDVAVkiLKVVDPTPEQLQA-FRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLY 349
Cdd:cd14154     1 LGKGFFGQAIKvtHRETGEVMV--MKELIRFDEEAQRnFLKEVKVMRSLDHPNVLKFIGVLYKDKkLNLITEYIPGGTLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA---------------TVKSR 414
Cdd:cd14154    79 DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerlpsgnmspSETLR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQP---TGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELmagelpyahinnrdqiifmVGRGYASPD--- 488
Cdd:cd14154   159 HLKSPDRKKRytvVGNPYWMAPEMLNGRS---YDEKVDIFSFGIVLCEI-------------------IGRVEADPDylp 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 489 ------------LSRLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd14154   217 rtkdfglnvdsfREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
274-474 4.65e-34

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 129.65  E-value: 4.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwH----GDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEGSSL 348
Cdd:cd14009     1 IGRGSFATVWKGR-HkqtgEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQkTEDFIYLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLH----VQETKFQMFQlidiaRQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLATVKSRWSGSQQV 421
Cdd:cd14009    80 SQYIRkrgrLPEAVARHFM-----QQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSLQPASMAETL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 422 eqpTGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRD 474
Cdd:cd14009   155 ---CGSPLYMAPEILQFQKYDA---KADLWSVGAILFEMLVGKPPFRGSNHVQ 201
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
261-526 4.70e-34

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 130.23  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd05056     1 YEIQREDITLGRCIGEGQFGDVYQGVYMSpenekiAVAVKTCKN-CTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSR 414
Cdd:cd05056    80 PVWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGL----SR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPTGSVL---WMAPEVIRMQDdnpFSFQSDVYSYGIVLYE-LMAGELPYAHINNRDqIIFMVGRGyaspdlS 490
Cdd:cd05056   156 YMEDESYYKASKGKLpikWMAPESINFRR---FTSASDVWMFGVCMWEiLMLGVKPFQGVKNND-VIGRIENG------E 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720416759 491 RLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05056   226 RLPMppNCPPTLYSLMTKCWAYDPSKRPRFTELKAQLS 263
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
266-530 1.11e-33

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 128.86  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 266 SEVMLSTRIGSGSFGTVYKG--KWHGD-VAVKILKVVDpTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQ 341
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVrhKPTGKiYALKKIHVDG-DEEFRKQLLRELKTLRSCESPYVVKCYGaFYKEGEISIVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSL----YKHLHVQETkfqmfQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFL-HEGlTVKIGDFGLATVKSRw 415
Cdd:cd06623    80 YMDGGSLadllKKVGKIPEP-----VLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLInSKG-EVKIADFGISKVLEN- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 sGSQQVEQPTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRD-----QIIFMVgrgyASPDLS 490
Cdd:cd06623   153 -TLDQCNTFVGTVTYMSPERI---QGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSffelmQAICDG----PPPSLP 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1720416759 491 rlYKNCPKAMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06623   225 --AEEFSPEFRDFISACLQKDPKKRP------SAAELLQH 256
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
261-530 1.13e-33

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 128.56  E-value: 1.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKVvDPTPeqlQAFRNEVAVLRKTRHVNILLFMGYMTKDN--LA 337
Cdd:cd05082     1 WALNMKELKLLQTIGKGEFGDVMLGDYRGNkVAVKCIKN-DATA---QAFLAEASVMTQLRHSNLVQLLGVIVEEKggLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLHVQ-ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRws 416
Cdd:cd05082    77 IVTEYMAKGSLVDYLRSRgRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASS-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 gsqqvEQPTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYA--SPDlsr 491
Cdd:cd05082   155 -----TQDTGKlpVKWTAPEALR---EKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKD-VVPRVEKGYKmdAPD--- 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 492 lykNCPKAMKRLVADCVKKVKEERPLFPQILssiELLQH 530
Cdd:cd05082   223 ---GCPPAVYDVMKNCWHLDAAMRPSFLQLR---EQLEH 255
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
261-530 2.03e-33

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 128.71  E-value: 2.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIeASEvmlstrIGSGSFGTVYKGKWHGDVAVKILKVVD-PTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAI 338
Cdd:cd06611     7 WEI-IGE------LGDGAFGKVYKAQHKETGLFAAAKIIQiESEEELEDFMVEIDILSECKHPNIVgLYEAYFYENKLWI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL-ATVKSRwsg 417
Cdd:cd06611    80 LIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVsAKNKST--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVLWMAPEVIRMQD--DNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGyASPDLSRLYKn 495
Cdd:cd06611   157 LQKRDTFIGTPYWMAPEVVACETfkDNPYDYKADIWSLGITLIELAQMEPPHHELNPM-RVLLKILKS-EPPTLDQPSK- 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 496 CPKAMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06611   234 WSSSFNDFLKSCLVKDPDDRP------TAAELLKH 262
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
262-526 6.31e-33

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 127.12  E-value: 6.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVdPTPEQLQAFRNEVAVLRKTRHVNILLFMG--YM 331
Cdd:cd05036     2 EVPRKNLTLIRALGQGAFGEVYEGTVSGmpgdpsplQVAVKTLPEL-CSEQDEMDFLMEALIMSKFNHPNIVRCIGvcFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDNLaIVTQWCEGSSLYKHLH------VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVK 402
Cdd:cd05036    81 RLPRF-ILLELMAGGDLKSFLRenrprpEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLtckGPGRVAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 403 IGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVG 481
Cdd:cd05036   160 IGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFL---DGIFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFVTS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 482 RGYASPDlsrlyKNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05036   237 GGRMDPP-----KNCPGPVYRIMTQCWQHIPEDRPNFSTILERLN 276
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
273-544 6.82e-33

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 126.98  E-value: 6.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG--KWHGD-VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSSL 348
Cdd:cd06609     8 RIGKGSFGEVYKGidKRTNQvVAIKVIDL-EEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGsKLWIIMEYCGGGSV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 yKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksrwsgsqQVEQPT--- 425
Cdd:cd06609    87 -LDL-LKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSG---------QLTSTMskr 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 ----GSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHInnrdqiifmvgrgYASPDLSRLYKNCP---- 497
Cdd:cd06609   156 ntfvGTPFWMAPEVIKQSG---YDEKADIWSLGITAIELAKGEPPLSDL-------------HPMRVLFLIPKNNPpsle 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 498 -----KAMKRLVADCVKKVKEERPlfpqilSSIELLQHSLPKINRSASEPSL 544
Cdd:cd06609   220 gnkfsKPFKDFVELCLNKDPKERP------SAKELLKHKFIKKAKKTSYLTL 265
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
274-539 1.22e-32

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 127.46  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK-WHGDVAVKILKVV---DPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLA-IVTQWCEGSSl 348
Cdd:cd06633    29 IGHGSFGAVYFATnSHTNEVVAIKKMSysgKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAwLVMEYCLGSA- 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqQVEQPTGSV 428
Cdd:cd06633   108 SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS------PANSFVGTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMvgrgyASPDLSRLYKN-CPKAMKRLVADC 507
Cdd:cd06633   182 YWMAPEVILAMDEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHI-----AQNDSPTLQSNeWTDSFRGFVDYC 256
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 508 VKKVKEERPlfpqilSSIELLQHSLPKINRSA 539
Cdd:cd06633   257 LQKIPQERP------SSAELLRHDFVRRERPP 282
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
264-529 1.89e-32

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 126.28  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 264 EASEVMLSTRIGSGSFGTVYKGKWH------GDVaVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY---MTKD 334
Cdd:cd14205     2 EERHLKFLQQLGKGNFGSVEMCRYDplqdntGEV-VAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVcysAGRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 414
Cdd:cd14205    81 NLRLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPTGS-VLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAgelpYAHINNRDQIIFMVGRGYASP------ 487
Cdd:cd14205   161 DKEYYKVKEPGESpIFWYAPESL---TESKFSVASDVWSFGVVLYELFT----YIEKSKSPPAEFMRMIGNDKQgqmivf 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 488 DLSRLYKN---------CPKAMKRLVADCVKKVKEERPLFPQILSSIELLQ 529
Cdd:cd14205   234 HLIELLKNngrlprpdgCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIR 284
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
274-522 3.85e-32

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 124.69  E-value: 3.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQ---AFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLY 349
Cdd:cd08225     8 IGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKekeASKKEVILLAKMKHPNIVTFFASFQENGrLFIVMEYCDGGDLM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE-GLTVKIGDFGLATVksrWSGSQQVEQP-TG 426
Cdd:cd08225    88 KRINRQRgVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKnGMVAKLGDFGIARQ---LNDSMELAYTcVG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGYASPdlsrLYKNCPKAMKRLVAD 506
Cdd:cd08225   165 TPYYLSPEICQ---NRPYNNKTDIWSLGCVLYELCTLKHPFEG-NNLHQLVLKICQGYFAP----ISPNFSRDLRSLISQ 236
                         250
                  ....*....|....*.
gi 1720416759 507 CVKKVKEERPLFPQIL 522
Cdd:cd08225   237 LFKVSPRDRPSITSIL 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
273-521 4.92e-32

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 123.89  E-value: 4.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKVVDPtPEQLQAFRNEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQWCEGSSL 348
Cdd:cd05084     3 RIGRGNFGEVFSGRLRADntpVAVKSCRETLP-PDLKAKFLQEARILKQYSHPNIVRLIGVCTqKQPIYIVMELVQGGDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT-----VKSRWSGSQQVeq 423
Cdd:cd05084    82 LTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSReeedgVYAATGGMKQI-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 ptgSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYASPdlsrLYKNCPKAMKR 502
Cdd:cd05084   160 ---PVKWTAPEALNY---GRYSSESDVWSFGILLWETFSlGAVPYANLSNQ-QTREAVEQGVRLP----CPENCPDEVYR 228
                         250
                  ....*....|....*....
gi 1720416759 503 LVADCVKKVKEERPLFPQI 521
Cdd:cd05084   229 LMEQCWEYDPRKRPSFSTV 247
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
273-521 5.19e-32

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 124.00  E-value: 5.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05060     2 ELGHGNFGSVRKGVYLMksgkevEVAVKTLKQ-EHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLMLVMELAPLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTG 426
Cdd:cd05060    81 PLLKYL-KKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMS--RALGAGSDYYRATTA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 S---VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYaspdlsRLYK--NCPKAM 500
Cdd:cd05060   158 GrwpLKWYAPECINYGK---FSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPE-VIAMLESGE------RLPRpeECPQEI 227
                         250       260
                  ....*....|....*....|.
gi 1720416759 501 KRLVADCVKKVKEERPLFPQI 521
Cdd:cd05060   228 YSIMLSCWKYRPEDRPTFSEL 248
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
274-531 7.50e-32

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 123.80  E-value: 7.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG--KWHGDV-AVK--ILKVVDPTPEQ-----LQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQW 342
Cdd:cd06628     8 IGSGSFGSVYLGmnASSGELmAVKqvELPSVSAENKDrkksmLDALQREIALLRELQHENIVQYLGSsSDANHLNIFLEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--KSRWSGSQQ 420
Cdd:cd06628    88 VPGGSVATLLN-NYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKleANSLSTKNN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQPT--GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGrGYASPDLSrlyKNCPK 498
Cdd:cd06628   167 GARPSlqGSVFWMAPEVVK---QTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQM-QAIFKIG-ENASPTIP---SNISS 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 499 AMKRLVADCVKKVKEERPlfpqilSSIELLQHS 531
Cdd:cd06628   239 EARDFLEKTFEIDHNKRP------TADELLKHP 265
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
274-510 1.50e-31

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 122.63  E-value: 1.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK------GKWHgdvAVKILK--VVDPTPEQLQAFrNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCE 344
Cdd:cd05123     1 LGKGSFGKVLLvrkkdtGKLY---AMKVLRkkEIIKRKEVEHTL-NERNILERVNHPFIVkLHYAFQTEEKLYLVLDYVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHvQETKFQMfqliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQ 420
Cdd:cd05123    77 GGELFSHLS-KEGRFPE----ERARfyaaEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELS--SDGDR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRG------YASPD----LS 490
Cdd:cd05123   150 TYTFCGTPEYLAPEVLLGK---GYGKAVDWWSLGVLLYEMLTGKPPF-YAENRKEIYEKILKSplkfpeYVSPEakslIS 225
                         250       260
                  ....*....|....*....|...
gi 1720416759 491 RLYKNCPKamKRL---VADCVKK 510
Cdd:cd05123   226 GLLQKDPT--KRLgsgGAEEIKA 246
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
274-530 1.56e-31

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 123.18  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwHGD----VAVKILkvvDPTPEQLQAFRNEVAVLRK-TRHVNILLFMGYMTK-------DNLAIVTQ 341
Cdd:cd06608    14 IGEGTYGKVYKAR-HKKtgqlAAIKIM---DIIEDEEEEIKLEINILRKfSNHPNIATFYGAFIKkdppggdDQLWLVME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSS---LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGS 418
Cdd:cd06608    90 YCGGGSvtdLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGV----SAQLDS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPT--GSVLWMAPEVI--RMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNrDQIIFMVGRGyASPDLSRlYK 494
Cdd:cd06608   166 TLGRRNTfiGTPYWMAPEVIacDQQPDASYDARCDVWSLGITAIELADGKPPLCDMHP-MRALFKIPRN-PPPTLKS-PE 242
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06608   243 KWSKEFNDFISECLIKNYEQRP------FTEELLEH 272
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
274-467 1.73e-31

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 122.50  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDpTPEQLQAFR----NEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSL 348
Cdd:cd08530     8 LGKGSYGSVYKVKRLSDNQVYALKEVN-LGSLSQKERedsvNEIRLLASVNHPNIIRYKEAFLDGNrLCIVMEYAPFGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIAR---QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQveqpT 425
Cdd:cd08530    87 SKLISKRKKKRRLFPEDDIWRifiQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLAKTQ----I 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 426 GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd08530   163 GTPLYAAPEVWK---GRPYDYKSDIWSLGCLLYEMATFRPPF 201
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
274-523 1.84e-31

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 122.66  E-value: 1.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPT----PEQLQAFRNEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQWCEGSSL 348
Cdd:cd14099     9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSsltkPKQREKLKSEIKIHRSLKHPNIVKFHDCFEdEENVYILLELCSNGSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 Y------KHLHVQETKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksrwsgsqQVE 422
Cdd:cd14099    89 MellkrrKALTEPEVRYFMRQILS-------GVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAA---------RLE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPT-------GSVLWMAPEVIRmqDDNPFSFQSDVYSYGIVLYELMAGELP---------YAHINNRDqiifmvgrgYAS 486
Cdd:cd14099   153 YDGerkktlcGTPNYIAPEVLE--KKKGHSFEVDIWSLGVILYTLLVGKPPfetsdvketYKRIKKNE---------YSF 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720416759 487 PDlsrlYKNCPKAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd14099   222 PS----HLSISDEAKDLIRSMLQPDPTKRPSLDEILS 254
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
274-531 3.55e-31

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 122.08  E-value: 3.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKW---HGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd06610     9 IGSGATAVVYAAYClpkKEKVAIKRIDL-EKCQTSMDELRKEIQAMSQCNHPNVVSYYTsFVVGDELWLVMPLLSGGSLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 kHLHVQETKFQMFQLIDIA---RQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPT- 425
Cdd:cd06610    88 -DIMKSSYPRGGLDEAIIAtvlKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRTRKVRKTf 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 -GSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDqiIFMVGRGYASPDL--SRLYKNCPKAMKR 502
Cdd:cd06610   167 vGTPCWMAPEV--MEQVRGYDFKADIWSFGITAIELATGAAPYSKYPPMK--VLMLTLQNDPPSLetGADYKKYSKSFRK 242
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 503 LVADCVKKVKEERPlfpqilSSIELLQHS 531
Cdd:cd06610   243 MISLCLQKDPSKRP------TAEELLKHK 265
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
262-525 3.75e-31

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 121.95  E-value: 3.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKG------KWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN 335
Cdd:cd05064     1 ELDNKSIKIERILGTGRFGELCRGclklpsKRELPVAIHTLRA-GCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 -LAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG------L 408
Cdd:cd05064    80 tMMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRrlqedkS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 409 ATVKSRWSGSQqveqptgSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqIIFMVGRGYASP 487
Cdd:cd05064   160 EAIYTTMSGKS-------PVLWAAPEAIQYHH---FSSASDVWSFGIVMWEVMSyGERPYWDMSGQD-VIKAVEDGFRLP 228
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720416759 488 DLsrlyKNCPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd05064   229 AP----RNCPNLLHQLMLDCWQKERGERPRFSQIHSIL 262
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
274-530 3.98e-31

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 121.44  E-value: 3.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKHL 352
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLK-EVKLMRRLSHPNILRFIGVCVKDNkLNFITEYVNGGTLEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 353 HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE---GLTVKIGDFGLAT---VKSRWSGSQQVEQPT- 425
Cdd:cd14065    80 KSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREanrGRNAVVADFGLARempDEKTKKPDRKKRLTVv 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 GSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELmagelpyahinnrdqiifmVGRGYASPD---------------LS 490
Cdd:cd14065   160 GSPYWMAPEMLRGE---SYDEKVDVFSFGIVLCEI-------------------IGRVPADPDylprtmdfgldvrafRT 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1720416759 491 RLYKNCPKAMKRLVADCVKKVKEERPLFpqilssIELLQH 530
Cdd:cd14065   218 LYVPDCPPSFLPLAIRCCQLDPEKRPSF------VELEHH 251
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
273-530 4.97e-31

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 122.00  E-value: 4.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD-VAVKILkvvdPTPEQlQAFRNEVAV--LRKTRHVNILLFMGYMTKDN-----LAIVTQWCE 344
Cdd:cd14056     2 TIGKGRYGEVWLGKYRGEkVAVKIF----SSRDE-DSWFRETEIyqTVMLRHENILGFIAADIKSTgswtqLWLITEYHE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLhvQETKFQMFQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwS 416
Cdd:cd14056    77 HGSLYDYL--QRNTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADLGLAVRYD--S 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 GSQQVEQPT----GSVLWMAPEVIRmQDDNPFSFQS----DVYSYGIVLYELM-----AG-----ELPYAHINNRDqiif 478
Cdd:cd14056   153 DTNTIDIPPnprvGTKRYMAPEVLD-DSINPKSFESfkmaDIYSFGLVLWEIArrceiGGiaeeyQLPYFGMVPSD---- 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 479 mvgrgyasPDLSRlykncpkaMKRLVadCVKKvkeERPLFPQILSSIELLQH 530
Cdd:cd14056   228 --------PSFEE--------MRKVV--CVEK---LRPPIPNRWKSDPVLRS 258
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
272-522 7.60e-31

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 120.57  E-value: 7.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKT-RHVNILLFMGYMTKDN-LAIVTQWCEGS 346
Cdd:cd13997     6 EQIGSGSFSEVFKVRSKVDgclYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGhLYIQMELCENG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLH--VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQp 424
Cdd:cd13997    86 SLQDALEelSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAT---RLETSGDVEE- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 tGSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYElMAGELPYAHINNRDQIIFMvgrGYASPDLSRLYKncpKAMKRLV 504
Cdd:cd13997   162 -GDSRYLAPEL--LNENYTHLPKADIFSLGVTVYE-AATGEPLPRNGQQWQQLRQ---GKLPLPPGLVLS---QELTRLL 231
                         250
                  ....*....|....*...
gi 1720416759 505 ADCVKKVKEERPLFPQIL 522
Cdd:cd13997   232 KVMLDPDPTRRPTADQLL 249
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
273-522 9.10e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 120.69  E-value: 9.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGT--VYKGKWHGD-VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSSL 348
Cdd:cd08218     7 KIGEGSFGKalLVKSKEDGKqYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQeSFEENGNLYIVMDYCDGGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGS 427
Cdd:cd08218    87 YKRINAQRgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLN--STVELARTCIGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRGYASPDLSRLYKNcpkaMKRLVADC 507
Cdd:cd08218   165 PYYLSPEIC---ENKPYNNKSDIWALGCVLYEMCTLKHAF-EAGNMKNLVLKIIRGSYPPVPSRYSYD----LRSLVSQL 236
                         250
                  ....*....|....*
gi 1720416759 508 VKKVKEERPLFPQIL 522
Cdd:cd08218   237 FKRNPRDRPSINSIL 251
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
274-528 1.12e-30

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 120.66  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD------VAVKILKVVDPTpEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN---LAIVTQWCE 344
Cdd:cd05058     3 IGKGHFGCVYHGTLIDSdgqkihCAVKSLNRITDI-EEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEgspLVVLPYMKH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSsLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT---VKSRWSgsqqV 421
Cdd:cd05058    82 GD-LRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARdiyDKEYYS----V 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGS---VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMV-GRGYASPDLsrlyknC 496
Cdd:cd05058   157 HNHTGAklpVKWMALESLQTQK---FTTKSDVWSFGVLLWELMTrGAPPYPDVDSFDITVYLLqGRRLLQPEY------C 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05058   228 PDPLYEVMLSCWHPKPEMRPTFSELVSRISQI 259
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
260-530 1.30e-30

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 120.90  E-value: 1.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 260 YWEIEAsevmlstRIGSGSFGTVYKGKWHGDVAVKILKVVD-PTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLA 337
Cdd:cd06643     6 FWEIVG-------ELGDGAFGKVYKAQNKETGILAAAKVIDtKSEEELEDYMVEIDILASCDHPNIVkLLDAFYYENNLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsG 417
Cdd:cd06643    79 ILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTR--T 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVLWMAPEVI--RMQDDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRGyASPDLSRLYKN 495
Cdd:cd06643   157 LQRRDSFIGTPYWMAPEVVmcETSKDRPYDYKADVWSLGVTLIEMAQIEPPH-HELNPMRVLLKIAKS-EPPTLAQPSRW 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 496 CPKaMKRLVADCVKKVKEERplfpqiLSSIELLQH 530
Cdd:cd06643   235 SPE-FKDFLRKCLEKNVDAR------WTTSQLLQH 262
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
274-529 1.72e-30

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 120.27  E-value: 1.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVD-PTPE-QLQAFRNEVAVLRKTRHV---NILLFMG-YMTKDNLAIVTQWCEGSS 347
Cdd:cd06917     9 VGRGSYGAVYRGYHVKTGRVVALKVLNlDTDDdDVSDIQKEVALLSQLKLGqpkNIIKYYGsYLKGPSLWIIMDYCEGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQMFQLIdiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvkSRWSGSQQVEQPTGS 427
Cdd:cd06917    89 IRTLMRAGPIAERYIAVI--MREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAA--SLNQNSSKRSTFVGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRmqDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGyASPdlsRLYKNC-PKAMKRLVAD 506
Cdd:cd06917   165 PYWMAPEVIT--EGKYYDTKADIWSLGITTYEMATGNPPYSDVDAL-RAVMLIPKS-KPP---RLEGNGySPLLKEFVAA 237
                         250       260
                  ....*....|....*....|...
gi 1720416759 507 CVKKVKEERplfpqiLSSIELLQ 529
Cdd:cd06917   238 CLDEEPKDR------LSADELLK 254
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
274-531 1.97e-30

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 119.85  E-value: 1.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG--KWHGDVAVK--ILKVVDP--TPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGS 346
Cdd:cd06631     9 LGKGAYGTVYCGltSTGQLIAVKqvELDTSDKekAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNvVSIFMEFVPGG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG----LATVKSRWSGS 418
Cdd:cd06631    89 SIASILArfgaLEEPVFCRY-----TKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrLCINLSSGSQS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHInNRDQIIFMVGRGYASPdlSRLYKNCPK 498
Cdd:cd06631   164 QLLKSMRGTPYWMAPEVIN---ETGHGRKSDIWSIGCTVFEMATGKPPWADM-NPMAAIFAIGSGRKPV--PRLPDKFSP 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 499 AMKRLVADCVKKVKEERPlfpqilSSIELLQHS 531
Cdd:cd06631   238 EARDFVHACLTRDQDERP------SAEQLLKHP 264
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
274-530 3.33e-30

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 119.09  E-value: 3.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK-WHGDVAVKILKVV---DPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLA-IVTQWCEGSSl 348
Cdd:cd06607     9 IGHGSFGAVYYARnKRTSEVVAIKKMSysgKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAwLVMEYCLGSA- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqQVEQPTGSV 428
Cdd:cd06607    88 SDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVC------PANSFVGTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNrdqiifmvgrgyaspdLSRLY---KNCPKAMK---- 501
Cdd:cd06607   162 YWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNA----------------MSALYhiaQNDSPTLSsgew 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 502 -----RLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06607   226 sddfrNFVDSCLQKIPQDRP------SAEDLLKH 253
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
273-534 4.70e-30

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 118.88  E-value: 4.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLqaFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSSL 348
Cdd:cd06647    14 KIGQGASGTVYTAidvATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGGSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQPT--G 426
Cdd:cd06647    92 TDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT----PEQSKRSTmvG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyaSPDLSRLYKNCPkAMKRLVAD 506
Cdd:cd06647   166 TPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPEKLSA-IFRDFLNR 239
                         250       260
                  ....*....|....*....|....*...
gi 1720416759 507 CVKKVKEERplfpqiLSSIELLQHSLPK 534
Cdd:cd06647   240 CLEMDVEKR------GSAKELLQHPFLK 261
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
272-530 5.13e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 118.56  E-value: 5.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKG--KWHGDV-AVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSS 347
Cdd:cd06626     6 NKIGEGTFGKVYTAvnLDTGELmAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVeVHREEVYIFMEYCQEGT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGLtVKIGDFGLATVKSrwSGSQQVE 422
Cdd:cd06626    86 LEELLRhgriLDEAVIRVY-----TLQLLEGLAYLHENGIVHRDIKPANIFLdSNGL-IKLGDFGSAVKLK--NNTTTMA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QP-----TGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGY--ASPDLSRLYKN 495
Cdd:cd06626   158 PGevnslVGTPAYMAPEVITGNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVGMGHkpPIPDSLQLSPE 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 496 CPKAMKRlvadCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06626   238 GKDFLSR----CLESDPKKRP------TASELLDH 262
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
274-477 5.31e-30

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 118.35  E-value: 5.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwHGD----VAVKILKVvdptpEQLQA------FRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQW 342
Cdd:cd14007     8 LGKGKFGNVYLAR-EKKsgfiVALKVISK-----SQLQKsglehqLRREIEIQSHLRHPNILRLYGYFeDKKRIYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLHVQ-----ETKFQMFqlidiaRQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvksrWSg 417
Cdd:cd14007    82 APNGELYKELKKQkrfdeKEAAKYI------YQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG-------WS- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 418 sqqVEQPT-------GSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQII 477
Cdd:cd14007   148 ---VHAPSnrrktfcGTLDYLPPEMVEGK---EYDYKVDIWSLGVLCYELLVGKPPFES-KSHQETY 207
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
274-526 6.11e-30

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 118.67  E-value: 6.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---------KWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWC 343
Cdd:cd05044     3 LGSGAFGEVFEGtakdilgdgSGETKVAVKTLRK-GATDQEKAEFLKEAHLMSNFKHPNILKLLGVcLDNDPQYIILELM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLH------VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG----LTVKIGDFGLATVKS 413
Cdd:cd05044    82 EGGDLLSYLRaarptaFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKdyreRVVKIGDFGLARDIY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRG-YASPDlsr 491
Cdd:cd05044   162 KNDYYRKEGEGLLPVRWMAPESLV---DGVFTTQSDVWAFGVLMWEILTlGQQPYPARNNLEVLHFVRAGGrLDQPD--- 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 492 lykNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05044   236 ---NCPDDLYELMLRCWSTDPEERPSFARILEQLQ 267
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
276-521 8.11e-30

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 118.37  E-value: 8.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 276 SGSFGTVYKG--KWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSSLYKHL 352
Cdd:cd14027     3 SGGFGKVSLCfhRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEgKYSLVMEYMEKGNLMHVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 353 HVQETKFQMFQLIDIarQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVK--SRWSGSQQVEQP------ 424
Cdd:cd14027    83 KKVSVPLSVKGRIIL--EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwSKLTKEEHNEQRevdgta 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 ---TGSVLWMAPEVIRMQDDNPfSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyASPDLSRLYKNCPKAMK 501
Cdd:cd14027   161 kknAGTLYYMAPEHLNDVNAKP-TEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSG-NRPDVDDITEYCPREII 238
                         250       260
                  ....*....|....*....|
gi 1720416759 502 RLVADCVKKVKEERPLFPQI 521
Cdd:cd14027   239 DLMKLCWEANPEARPTFPGI 258
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
274-521 8.96e-30

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 117.80  E-value: 8.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQ-AFRNEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQWCEGSSLYKH 351
Cdd:cd05085     4 LGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQELKiKFLSEARILKQYDHPNIVKLIGVCTqRQPIYIVMELVPGGDFLSF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKS----RWSGSQQVeqptgS 427
Cdd:cd05085    84 LRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDdgvySSSGLKQI-----P 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGY--ASPdlsrlyKNCPKAMKRLV 504
Cdd:cd05085   159 IKWTAPEALNY---GRYSSESDVWSFGILLWETFSlGVCPYPGMTNQ-QAREQVEKGYrmSAP------QRCPEDIYKIM 228
                         250
                  ....*....|....*..
gi 1720416759 505 ADCVKKVKEERPLFPQI 521
Cdd:cd05085   229 QRCWDYNPENRPKFSEL 245
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
261-526 1.16e-29

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 117.52  E-value: 1.16e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKW---HGDVAVKILKvvdPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NL 336
Cdd:cd05052     1 WEIERTDITMKHKLGGGQYGEVYEGVWkkyNLTVAVKTLK---EDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREpPF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSSLYKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRW 415
Cdd:cd05052    78 YIITEFMPYGNLLDYLReCNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLS----RL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPTGS---VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHInNRDQIIFMVGRGYASPDLSr 491
Cdd:cd05052   154 MTGDTYTAHAGAkfpIKWTAPESLAY---NKFSIKSDVWAFGVLLWEIATyGMSPYPGI-DLSQVYELLEKGYRMERPE- 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 492 lykNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05052   229 ---GCPPKVYELMRACWQWNPSDRPSFAEIHQALE 260
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
274-467 1.95e-29

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 117.27  E-value: 1.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK------------VVDPTPEQLQAFRNEVAVLRKTRHVNIL-LF--MGYMTKDN 335
Cdd:cd14008     1 LGRGSFGKVKLALDTETgqlYAIKIFNksrlrkrregknDRGKIKNALDDVRREIAIMKKLDHPNIVrLYevIDDPESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvksr 414
Cdd:cd14008    81 LYLVLEYCEGGPVMELDSGDRVPpLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV------ 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 415 wsgSQQVEQPT-------GSVLWMAPEVIRMqDDNPFS-FQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14008   155 ---SEMFEDGNdtlqktaGTPAFLAPELCDG-DSKTYSgKAADIWALGVTLYCLVFGRLPF 211
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
262-521 2.83e-29

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 117.04  E-value: 2.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKGKWHGD--------VAVKILKVVDPTPEQlQAFRNEVAVLRKTRHVNILLFMGYMTK 333
Cdd:cd05091     2 EINLSAVRFMEELGEDRFGKVYKGHLFGTapgeqtqaVAIKTLKDKAEGPLR-EEFRHEAMLRSRLQHPNIVCLLGVVTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DN-LAIVTQWCEGSSLYKHLHVQ---------------ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE 397
Cdd:cd05091    81 EQpMSMIFSYCSHGDLHEFLVMRsphsdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 398 GLTVKIGDFGLAtvksRWSGSQQVEQPTGSVL----WMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINN 472
Cdd:cd05091   161 KLNVKISDLGLF----REVYAADYYKLMGNSLlpirWMSPEAIMY---GKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSN 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 473 RDQIIFMVGRGYAS-PDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd05091   234 QDVIEMIRNRQVLPcPD------DCPAWVYTLMLECWNEFPSRRPRFKDI 277
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
273-532 3.52e-29

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 116.49  E-value: 3.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVD---PTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDN--LAIVTQWCEG- 345
Cdd:cd08217     7 TIGKGSFGTVRKVRRKSDGKILVWKEIDygkMSEKEKQQLVSEVNILRELKHPNIVRYYDrIVDRANttLYIVMEYCEGg 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 --SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKN-----IIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGS 418
Cdd:cd08217    87 dlAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFGLA----RVLSH 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPT--GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRGyASPDLSRLYKnc 496
Cdd:cd08217   163 DSSFAKTyvGTPYYMSPELLN---EQSYDEKSDIWSLGCLIYELCALHPPF-QAANQLELAKKIKEG-KFPRIPSRYS-- 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 497 pKAMKRLVADCVKKVKEERPlfpqilSSIELLQHSL 532
Cdd:cd08217   236 -SELNEVIKSMLNVDPDKRP------SVEELLQLPL 264
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
271-521 3.86e-29

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 116.34  E-value: 3.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGsfGTVYKGKWHGD--VAVKIL-KVVDPTPEQLQafrnEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQWCEGS 346
Cdd:cd13992     8 SSHTGEP--KYVKKVGVYGGrtVAIKHItFSRTEKRTILQ----ELNQLKELVHDNLNKFIGICInPPNIAVVTEYCTRG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHVQETKFQ---MFQLI-DIARqtaqGMDYLHAKNII-HRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQV 421
Cdd:cd13992    82 SLQDVLLNREIKMDwmfKSSFIkDIVK----GMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGS-VLWMAPEVIRMQDDNP-FSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRG---YASPDLSRLYKNC 496
Cdd:cd13992   158 EDAQHKkLLWTAPELLRGSLLEVrGTQKGDVYSFAIILYEILFRSDPFALEREV-AIVEKVISGgnkPFRPELAVLLDEF 236
                         250       260
                  ....*....|....*....|....*
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd13992   237 PPRLVLLVKQCWAENPEKRPSFKQI 261
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
273-460 4.05e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 115.98  E-value: 4.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVY-----KGKWHGDVAV-KILKVVDPTP-EQLQAFRnEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCE 344
Cdd:cd08222     7 KLGSGNFGTVYlvsdlKATADEELKVlKEISVGELQPdETVDANR-EAKLLSKLDHPAIVKFHdSFVEKESFCIVTEYCE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSL---YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLtVKIGDFGLATVksrWSGSQQV 421
Cdd:cd08222    86 GGDLddkISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRI---LMGTSDL 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720416759 422 EQP-TGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYEL 460
Cdd:cd08222   162 ATTfTGTPYYMSPEVLKHEGYNS---KSDIWSLGCILYEM 198
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
273-543 4.09e-29

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 116.71  E-value: 4.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVD--PTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLY 349
Cdd:cd06641    11 KIGKGSFGEVFKGIDNRTQKVVAIKIIDleEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTkLWIIMEYLGGGSAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLH---VQETkfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQP-- 424
Cdd:cd06641    91 DLLEpgpLDET-----QIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLT----DTQIKRN*f 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 TGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGyaSPDLsrLYKNCPKAMKRLV 504
Cdd:cd06641   162 VGTPFWMAPEVIK---QSAYDSKADIWSLGITAIELARGEPPHSELHPM-KVLFLIPKN--NPPT--LEGNYSKPLKEFV 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 505 ADCVKKVKEERPlfpqilSSIELLQHSLpkINRSASEPS 543
Cdd:cd06641   234 EACLNKEPSFRP------TAKELLKHKF--ILRNAKKTS 264
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
273-530 4.60e-29

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 116.31  E-value: 4.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVD--PTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSS-- 347
Cdd:cd06642    11 RIGKGSFGEVYKGIDNRTKEVVAIKIIDleEAEDEIEDIQQEITVLSQCDSPYITRYYGsYLKGTKLWIIMEYLGGGSal 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 -LYKHLHVQETkfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQPT- 425
Cdd:cd06642    91 dLLKPGPLEET-----YIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLT----DTQIKRNTf 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 -GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGyASPDLSRLYKncpKAMKRLV 504
Cdd:cd06642   162 vGTPFWMAPEVIK---QSAYDFKADIWSLGITAIELAKGEPPNSDLHPM-RVLFLIPKN-SPPTLEGQHS---KPFKEFV 233
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 505 ADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06642   234 EACLNKDPRFRP------TAKELLKH 253
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
272-526 9.54e-29

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 115.25  E-value: 9.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKGKWHG-----DVAVKILKVVDPTPEQ--LQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWC 343
Cdd:cd05046    11 TTLGRGEFGEVFLAKAKGieeegGETLVLVKALQKTKDEnlQSEFRRELDMFRKLSHKNVVRLLGLCrEAEPHYMILEYT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHVQETKFQMF--------QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA--TVKS 413
Cdd:cd05046    91 DLGDLKQFLRATKSKDEKLkppplstkQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSkdVYNS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RWSGSQQVEQPtgsVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIFMVGRGyaspDLS-R 491
Cdd:cd05046   171 EYYKLRNALIP---LRWLAPEAVQ---EDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSD-EEVLNRLQAG----KLElP 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 492 LYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05046   240 VPEGCPSRLYKLMTRCWAVNPKDRPSFSELVSALG 274
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
261-532 1.40e-28

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 115.45  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVY--------KGKWHGDVAVKILKVVDPTPEQLQaFRNEVAVLRKTRHVNILLFMGYMT 332
Cdd:cd05061     1 WEVSREKITLLRELGQGSFGMVYegnardiiKGEAETRVAVKTVNESASLRERIE-FLNEASVMKGFTCHHVVRLLGVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 333 KDN--LAIVTQWCEG--SSLYKHLHVQETKFQ------MFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK 402
Cdd:cd05061    80 KGQptLVVMELMAHGdlKSYLRSLRPEAENNPgrppptLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 403 IGDFGLA-----TVKSRWSGSQQVeqptgSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQI 476
Cdd:cd05061   160 IGDFGMTrdiyeTDYYRKGGKGLL-----PVRWMAPESLK---DGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVL 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 477 IFMVGRGYAS-PDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQIlssIELLQHSL 532
Cdd:cd05061   232 KFVMDGGYLDqPD------NCPERVTDLMRMCWQFNPKMRPTFLEI---VNLLKDDL 279
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
274-532 2.27e-28

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 113.72  E-value: 2.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSSLYKHL 352
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANMLR-EVQLMNRLSHPNILRFMGVCVHQgQLHALTEYINGGNLEQLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 353 HVQETkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLAT-VKSRWSGSQQVEQpTGSV 428
Cdd:cd14155    80 DSNEP-LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEkIPDYSDGKEKLAV-VGSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAgelpyahinnrdqiifmvgRGYASPD-LSR-------------LYK 494
Cdd:cd14155   158 YWMAPEVLR---GEPYNEKADVFSYGIILCEIIA-------------------RIQADPDyLPRtedfgldydafqhMVG 215
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSL 532
Cdd:cd14155   216 DCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLEEILEKL 253
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
274-532 3.52e-28

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 113.38  E-value: 3.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKHL 352
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIVR-EISLLQKLSHPNIVRYLGICVKDEkLHPILEYVSGGCLEELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 353 HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLTVKIGDFGLAtvksRWSGSQQVEQPT---- 425
Cdd:cd14156    80 AREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRvtpRGREAVVTDFGLA----REVGEMPANDPErkls 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 --GSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMagelpyAHINNRDQIIFMVGR-GYASPDLSRLYKNCPKAMKR 502
Cdd:cd14156   156 lvGSAFWMAPEMLRGE---PYDRKVDVFSFGIVLCEIL------ARIPADPEVLPRTGDfGLDVQAFKEMVPGCPEPFLD 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1720416759 503 LVADCVKKVKEERPLFPQILSSIELLQHSL 532
Cdd:cd14156   227 LAASCCRMDAFKRPSFAELLDELEDIAETL 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
274-530 3.84e-28

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 113.63  E-value: 3.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG--KWHGDV-AVK---------------ILKVVDptpeqlqAFRNEVAVLRKTRHVNILLFMGYMTKDN 335
Cdd:cd06629     9 IGKGTYGRVYLAmnATTGEMlAVKqvelpktssdradsrQKTVVD-------ALKSEIDTLKDLDHPNIVQYLGFEETED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 -LAIVTQWCEGSS----LYKHLHVQE--TKFqmfqlidIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL 408
Cdd:cd06629    82 yFSIFLEYVPGGSigscLRKYGKFEEdlVRF-------FTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 409 ATVKSRWSGSQQVEQPTGSVLWMAPEVIrMQDDNPFSFQSDVYSYGIVLYELMAGELPYAhinnRD---QIIFMVGRGYA 485
Cdd:cd06629   155 SKKSDDIYGNNGATSMQGSVFWMAPEVI-HSQGQGYSAKVDIWSLGCVVLEMLAGRRPWS----DDeaiAAMFKLGNKRS 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 486 SPDLSRLYKNCPKAMKRLVAdCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06629   230 APPVPEDVNLSPEALDFLNA-CFAIDPRDRP------TAAELLSH 267
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
262-521 5.79e-28

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 113.33  E-value: 5.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKGKWH-----GD---VAVKILKvvDPTPEQL-QAFRNEVAVLRKTRHVNILLFMGYMT 332
Cdd:cd05049     1 HIKRDTIVLKRELGEGAFGKVFLGECYnlepeQDkmlVAVKTLK--DASSPDArKDFEREAELLTNLQHENIVKFYGVCT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 333 K-DNLAIVTQWCEGSSLYKHLH-------------VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG 398
Cdd:cd05049    79 EgDPLLMVFEYMEHGDLNKFLRshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 399 LTVKIGDFGLA-----TVKSRWSGSQQVeqptgSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINN 472
Cdd:cd05049   159 LVVKIGDFGMSrdiysTDYYRVGGHTML-----PIRWMPPESILYRK---FTTESDVWSFGVVLWEIFTyGKQPWFQLSN 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 473 RDQIIFMV-GRGYASPdlsrlyKNCPKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd05049   231 TEVIECITqGRLLQRP------RTCPSEVYAVMLGCWKREPQQRLNIKDI 274
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
274-521 6.23e-28

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 113.59  E-value: 6.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---------------YKGKWHGD----VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd05051    13 LGEGQFGEVhlceanglsdltsddFIGNDNKDepvlVAVKMLRP-DASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 N-LAIVTQWCEGSSLYKHL--HVQETKFQM--------FQ-LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK 402
Cdd:cd05051    92 EpLCMIVEYMENGDLNQFLqkHEAETQGASatnsktlsYGtLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 403 IGDFGLAtvKSRWSGSQ-QVEqptGSVL----WMAPEVIRMqddNPFSFQSDVYSYGIVLYELM--AGELPYAHINNrDQ 475
Cdd:cd05051   172 IADFGMS--RNLYSGDYyRIE---GRAVlpirWMAWESILL---GKFTTKSDVWAFGVTLWEILtlCKEQPYEHLTD-EQ 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 476 IIFMVGRGYASpDLSRLY----KNCPKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd05051   243 VIENAGEFFRD-DGMEVYlsrpPNCPKEIYELMLECWRRDEEDRPTFREI 291
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
274-532 6.74e-28

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 113.18  E-value: 6.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRK-TRHVNILLFMGYMTK-------DNLAIVTQWCEG 345
Cdd:cd06636    24 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKySHHRNIATYYGAFIKksppghdDQLWLVMEFCGA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHlhVQETKFQMFQ---LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVE 422
Cdd:cd06636   104 GSVTDL--VKNTKGNALKedwIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTF 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 qpTGSVLWMAPEVIRMqDDNP---FSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGyASPDLSRlyKNCPKA 499
Cdd:cd06636   182 --IGTPYWMAPEVIAC-DENPdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPM-RALFLIPRN-PPPKLKS--KKWSKK 254
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 500 MKRLVADCVKKVKEERPlfpqilSSIELLQHSL 532
Cdd:cd06636   255 FIDFIEGCLVKNYLSRP------STEQLLKHPF 281
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
256-530 6.79e-28

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 113.59  E-value: 6.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 256 DSSYYWEIEAsevmlstRIGSGSFGTVYKGKWHGDVAVKILKVVD-PTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd06644     9 DPNEVWEIIG-------ELGDGAFGKVYKAKNKETGALAAAKVIEtKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 N-LAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKS 413
Cdd:cd06644    82 GkLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RwsGSQQVEQPTGSVLWMAPEVIRMQ--DDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGyASPDLSR 491
Cdd:cd06644   162 K--TLQRRDSFIGTPYWMAPEVVMCEtmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPM-RVLLKIAKS-EPPTLSQ 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 492 LYKNCPKaMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06644   238 PSKWSME-FRDFLKTALDKHPETRP------SAAQLLEH 269
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
261-526 6.87e-28

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 113.57  E-value: 6.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG----------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMG 329
Cdd:cd05098     8 WELPRDRLVLGKPLGEGCFGQVVLAEAIGldkdkpnrvtKVAVKMLKS-DATEKDLSDLISEMEMMKMIgKHKNIINLLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 YMTKDN-LAIVTQWCEGSSLYKHL---------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 393
Cdd:cd05098    87 ACTQDGpLYVIVEYASKGNLREYLqarrppgmeycynpsHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 394 FLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHInN 472
Cdd:cd05098   167 LVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALF---DRIYTHQSDVWSFGVLLWEIFTlGGSPYPGV-P 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 473 RDQIIFMVGRGYaspdlsRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05098   243 VEELFKLLKEGH------RMDKpsNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD 292
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
274-532 7.25e-28

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 112.74  E-value: 7.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQ-AFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKH 351
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQrTFLKEVKVMRCLEHPNVLKFIGVLYKDKrLNFITEYIKGGTLRGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV----KSRWSGSQQVEQP--- 424
Cdd:cd14221    81 IKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLmvdeKTQPEGLRSLKKPdrk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 -----TGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELmagelpyahinnrdqiifmVGRGYASPD-LSRLYK---- 494
Cdd:cd14221   161 krytvVGNPYWMAPEMI---NGRSYDEKVDVFSFGIVLCEI-------------------IGRVNADPDyLPRTMDfgln 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 495 -----------NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSL 532
Cdd:cd14221   219 vrgfldrycppNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLRMHL 267
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
274-466 1.01e-27

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 112.20  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKW--HGDVAVKILKVVDPTPEQLQaFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSSLYK 350
Cdd:cd14664     1 IGRGGAGTVYKGVMpnGTLVAVKRLKGEGTQGGDHG-FQAEIQTLGMIRHRNIVRLRGYcSNPTTNLLVYEYMPNGSLGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLHVQETKFQMFQLI---DIARQTAQGMDYLH---AKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrWSGSQQVEQP 424
Cdd:cd14664    80 LLHSRPESQPPLDWEtrqRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMD-DKDSHVMSSV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 425 TGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELP 466
Cdd:cd14664   159 AGSYGYIAPEYAYTGKVSE---KSDVYSYGVVLLELITGKRP 197
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
261-544 1.05e-27

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 113.52  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG----------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMG 329
Cdd:cd05099     7 WEFPRDRLVLGKPLGEGCFGQVVRAEAYGidksrpdqtvTVAVKMLKD-NATDKDLADLISEMELMKLIgKHKNIINLLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 YMTKDN-LAIVTQWCEGSSLYKHLH---------------VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 393
Cdd:cd05099    86 VCTQEGpLYVIVEYAAKGNLREFLRarrppgpdytfditkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 394 FLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHInN 472
Cdd:cd05099   166 LVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALF---DRVYTHQSDVWSFGILMWEIFTlGGSPYPGI-P 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 473 RDQIIFMVGRGYaspdlsRLYK--NCPKAMKRLVADCVKKVKEERPLFPQilssielLQHSLPKINRSASEPSL 544
Cdd:cd05099   242 VEELFKLLREGH------RMDKpsNCTHELYMLMRECWHAVPTQRPTFKQ-------LVEALDKVLAAVSEEYL 302
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
270-523 1.76e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 111.66  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGK--WHGDVA-VKILKVvDPTpEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEG 345
Cdd:cd06646    13 LIQRVGSGTYGDVYKARnlHTGELAaVKIIKL-EPG-DDFSLIQQEIFMVKECKHCNIVAYFGsYLSREKLWICMEYCGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQeTKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL-----ATVKSRWSGsqq 420
Cdd:cd06646    91 GSLQDIYHVT-GPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVaakitATIAKRKSF--- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 veqpTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKNCPkAM 500
Cdd:cd06646   167 ----IGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPPKLKDKTKWSS-TF 241
                         250       260
                  ....*....|....*....|...
gi 1720416759 501 KRLVADCVKKVKEERPLFPQILS 523
Cdd:cd06646   242 HNFVKISLTKNPKKRPTAERLLT 264
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
274-528 1.76e-27

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 111.94  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKW--HGD-----VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD---NLAIVTQWC 343
Cdd:cd05079    12 LGEGHFGKVELCRYdpEGDntgeqVAVKSLKP-ESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggnGIKLIMEFL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA----TVKSRWSGSQ 419
Cdd:cd05079    91 PSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTkaieTDKEYYTVKD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPtgsVLWMAPEVIrMQddNPFSFQSDVYSYGIVLYELmageLPYAHINNRDQIIF--MVGRGYASPDLSRLYK--- 494
Cdd:cd05079   171 DLDSP---VFWYAPECL-IQ--SKFYIASDVWSFGVTLYEL----LTYCDSESSPMTLFlkMIGPTHGQMTVTRLVRvle 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 495 ---------NCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05079   241 egkrlprppNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAI 283
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
273-524 2.01e-27

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 111.12  E-value: 2.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKW-----HGDVAVKILKVVDPTPEQLQAF--RnEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCE 344
Cdd:cd14080     7 TIGEGSYSKVKLAEYtksglKEKVACKIIDKKKAPKDFLEKFlpR-ELEILRKLRHPNIIQVYSIFeRGSKVFIFMEYAE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKH------LHVQETKfQMFqlidiaRQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGS 418
Cdd:cd14080    86 HGDLLEYiqkrgaLSESQAR-IWF------RQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFA----RLCPD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPT----GSVLWMAPEVIRMQDDNPFSfqSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPdlsRLYK 494
Cdd:cd14080   155 DDGDVLSktfcGSAAYAAPEILQGIPYDPKK--YDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFP---SSVK 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILSS 524
Cdd:cd14080   230 KLSPECKDLIDQLLEPDPTKRATIEEILNH 259
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
273-528 2.20e-27

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 111.43  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGK---WHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGyMTKDNLAIVTQWCEGSSLY 349
Cdd:cd14025     3 KVGSGGFGQVYKVRhkhWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYG-ICSEPVGLVMEYMETGSLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQ----ETKFQMFQlidiarQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSG---SQQ 420
Cdd:cd14025    82 KLLASEplpwELRFRIIH------ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLA----KWNGlshSHD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQPT--GSVLWMAPEVIrMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYaSPDLSRLYKNCPK 498
Cdd:cd14025   152 LSRDGlrGTIAYLPPERF-KEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGH-RPSLSPIPRQRPS 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 499 A---MKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd14025   230 EcqqMICLMKRCWDQDPRKRPTFQDITSETENL 262
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
274-529 2.58e-27

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 111.52  E-value: 2.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWH--GD-----VAVKILKvvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM---TKDNLAIVTQWC 343
Cdd:cd05081    12 LGKGNFGSVELCRYDplGDntgalVAVKQLQ--HSGPDQQRDFQREIQILKALHSDFIVKYRGVSygpGRRSLRLVMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd05081    90 PSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVRE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGS-VLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAgelpYAH--INNRDQIIFMVGRGYASPDLSRLYK------ 494
Cdd:cd05081   170 PGQSpIFWYAPESL---SDNIFSRQSDVWSFGVVLYELFT----YCDksCSPSAEFLRMMGCERDVPALCRLLElleegq 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 495 ------NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQ 529
Cdd:cd05081   243 rlpappACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLW 283
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
274-532 3.87e-27

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 110.81  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG-----KWHGDVAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSL 348
Cdd:cd05115    12 LGSGNFGCVKKGvykmrKKQIDVAIKVLKQGNEKAVRDEMMR-EAQIMHQLDNPYIVRMIGVCEAEALMLVMEMASGGPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV--------KSRWSGSQQ 420
Cdd:cd05115    91 NKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKAlgaddsyyKARSAGKWP 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEqptgsvlWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMV-GRGYASPdlsrlyKNCPK 498
Cdd:cd05115   171 LK-------WYAPECINFRK---FSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEVMSFIEqGKRMDCP------AECPP 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 499 AMKRLVADCVKKVKEERPLFPQILSSIELLQHSL 532
Cdd:cd05115   235 EMYALMSDCWIYKWEDRPNFLTVEQRMRTYYYSI 268
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
274-522 4.08e-27

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 111.35  E-value: 4.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRK-TRHVNILLFMGYMTK-------DNLAIVTQWCEG 345
Cdd:cd06637    14 VGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKySHHRNIATYYGAFIKknppgmdDQLWLVMEFCGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHlhVQETKFQMFQ---LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVE 422
Cdd:cd06637    94 GSVTDL--IKNTKGNTLKeewIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTF 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 qpTGSVLWMAPEVIRMqDDNP---FSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGYAsPDLSRlyKNCPKA 499
Cdd:cd06637   172 --IGTPYWMAPEVIAC-DENPdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPM-RALFLIPRNPA-PRLKS--KKWSKK 244
                         250       260
                  ....*....|....*....|...
gi 1720416759 500 MKRLVADCVKKVKEERPLFPQIL 522
Cdd:cd06637   245 FQSFIESCLVKNHSQRPSTEQLM 267
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
274-530 6.67e-27

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 110.88  E-value: 6.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK-WHGDVAVKILKVV---DPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLA-IVTQWCEGSSl 348
Cdd:cd06634    23 IGHGSFGAVYFARdVRNNEVVAIKKMSysgKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAwLVMEYCLGSA- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqQVEQPTGSV 428
Cdd:cd06634   102 SDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMA------PANSFVGTP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRgyASPDLSRlyKNCPKAMKRLVADCV 508
Cdd:cd06634   176 YWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQN--ESPALQS--GHWSEYFRNFVDSCL 251
                         250       260
                  ....*....|....*....|..
gi 1720416759 509 KKVKEERPlfpqilSSIELLQH 530
Cdd:cd06634   252 QKIPQDRP------TSDVLLKH 267
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
263-525 6.92e-27

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 109.57  E-value: 6.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKIlKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQ 341
Cdd:cd05114     1 INPSELTFMKELGSGLFGVVRLGKWRAQYKVAI-KAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKpIYIVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGSQQV 421
Cdd:cd05114    80 FMENGCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMT----RYVLDDQY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGS---VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYaspdlsRLY--KN 495
Cdd:cd05114   156 TSSSGAkfpVKWSPPEVFNY---SKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNY-EVVEMVSRGH------RLYrpKL 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 1720416759 496 CPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd05114   226 ASKSVYEVMYSCWHEKPEGRPTFADLLRTI 255
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
270-462 6.97e-27

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 109.67  E-value: 6.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHGD---VAVKILKVVDPT-PEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCE 344
Cdd:cd08224     4 IEKKIGKGQFSVVYRARCLLDgrlVALKKVQIFEMMdAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNeLNIVLELAD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 G---SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGSQQV 421
Cdd:cd08224    84 AgdlSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL----GRFFSSKTT 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 422 EQPT--GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA 462
Cdd:cd08224   160 AAHSlvGTPYYMSPERIR---EQGYDFKSDIWSLGCLLYEMAA 199
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
274-528 7.69e-27

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 110.03  E-value: 7.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQ-AFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKH 351
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQkTFLTEVKVMRSLDHPNVLKFIGVLYKDKrLNLLTEFIEGGTLKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LHVQETkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPT------ 425
Cdd:cd14222    81 LRADDP-FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPPDKPTtkkrtl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 ------------GSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELmagelpyahinnrdqiifmVGRGYASPD-LSR- 491
Cdd:cd14222   160 rkndrkkrytvvGNPYWMAPEMLNGKS---YDEKVDIFSFGIVLCEI-------------------IGQVYADPDcLPRt 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 492 --------------LYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd14222   218 ldfglnvrlfwekfVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEAL 268
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
268-528 9.52e-27

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 110.05  E-value: 9.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 268 VMLSTRIGSGSFGTVYKG--------KWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAI 338
Cdd:cd05045     2 LVLGKTLGEGEFGKVVKAtafrlkgrAGYTTVAVKMLKE-NASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGpLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHL-----------------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL 395
Cdd:cd05045    81 IVEYAKYGSLRSFLresrkvgpsylgsdgnrnssyldNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 396 HEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINN 472
Cdd:cd05045   161 AEGRKMKISDFGLS--RDVYEEDSYVKRSKGRipVKWMAIESLF---DHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 473 rDQIIFMVGRGY--ASPDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05045   236 -ERLFNLLKTGYrmERPE------NCSEEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
261-526 9.84e-27

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 109.74  E-value: 9.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVDPTPEQLQaFRNEVAVLRK--TRHVNILLFMGY 330
Cdd:cd05062     1 WEVAREKITMSRELGQGSFGMVYEGIAKGvvkdepetRVAIKTVNEAASMRERIE-FLNEASVMKEfnCHHVVRLLGVVS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 331 MTKDNLAIVTQWCEGSsLYKHLHVQETKFQ---------MFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTV 401
Cdd:cd05062    80 QGQPTLVIMELMTRGD-LKSYLRSLRPEMEnnpvqappsLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 402 KIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIF-M 479
Cdd:cd05062   159 KIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLK---DGVFTTYSDVWSFGVVLWEIATlAEQPYQGMSNEQVLRFvM 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 480 VGRGYASPDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05062   236 EGGLLDKPD------NCPDMLFELMRMCWQYNPKMRPSFLEIISSIK 276
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
274-530 1.23e-26

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 109.60  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV--YKGKWHGD-----VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN---LAIVTQWC 343
Cdd:cd05080    12 LGEGHFGKVslYCYDPTNDgtgemVAVKALKA-DCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGgksLQLIMEYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLhvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA----TVKSRWSGSQ 419
Cdd:cd05080    91 PLGSLRDYL--PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAkavpEGHEYYRVRE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPtgsVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYahINNRDQIIFMVGRGYASPDLSRLY------ 493
Cdd:cd05080   169 DGDSP---VFWYAPECLK---EYKFYYASDVWSFGVTLYELLTHCDSS--QSPPTKFLEMIGIAQGQMTVVRLIellerg 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 494 ------KNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQH 530
Cdd:cd05080   241 erlpcpDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTVHE 283
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
270-530 1.43e-26

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 109.36  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTP-EQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSS 347
Cdd:cd06645    15 LIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPgEDFAVVQQEIIMMKDCKHSNIVAYFGsYLRRDKLWICMEFCGGGS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQeTKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL-----ATVKSRWSGsqqve 422
Cdd:cd06645    95 LQDIYHVT-GPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVsaqitATIAKRKSF----- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 qpTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKnCPKAMKR 502
Cdd:cd06645   169 --IGTPYWMAPEVAAVERKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKMK-WSNSFHH 245
                         250       260
                  ....*....|....*....|....*...
gi 1720416759 503 LVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06645   246 FVKMALTKNPKKRP------TAEKLLQH 267
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
274-469 1.44e-26

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 108.92  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPT--PEQLqafrNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLYK 350
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSkrPEVL----NEVRLTHELKHPNVLKFYEwYETSNHLWLVVEYCTGGDLET 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HL----HVQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA-------------TVKS 413
Cdd:cd14010    84 LLrqdgNLPESSVRKF-----GRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeilkelfgqFSDE 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 414 RWSGSQQVEQPT-GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAH 469
Cdd:cd14010   159 GNVNKVSKKQAKrGTPYYMAPELFQ---GGVHSFASDLWALGCVLYEMFTGKPPFVA 212
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
274-531 1.45e-26

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 108.60  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKwhgDVAVKILKVVDPTPE---QLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWC 343
Cdd:cd06625     8 LGQGAFGQVYlcydadTGR---ELAVKQVEIDPINTEaskEVKALECEIQLLKNLQHERIVQYYGCLQDEKsLSIFMEYM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG----LATVKSRw 415
Cdd:cd06625    85 PGGSVKDEIKaygaLTENVTRKY-----TRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGaskrLQTICSS- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVeqpTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGYASPDLSrlyKN 495
Cdd:cd06625   159 TGMKSV---TGTPYWMSPEVINGEG---YGRKADIWSVGCTVVEMLTTKPPWAEFEPM-AAIFKIATQPTNPQLP---PH 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 496 CPKAMKRLVADCVKKVKEERPlfpqilSSIELLQHS 531
Cdd:cd06625   229 VSEDARDFLSLIFVRNKKQRP------SAEELLSHS 258
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
261-525 2.32e-26

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 109.12  E-value: 2.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMGYM 331
Cdd:cd05054     2 WEFPRDRLKLGKPLGRGAFGKVIQASAFGidksatcrTVAVKMLKE-GATASEHKALMTELKILIHIgHHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDN--LAIVTQWCEGSSLYKHL------------------HVQETKFQMFQ-------LIDIARQTAQGMDYLHAKNII 384
Cdd:cd05054    81 TKPGgpLMVIVEFCKFGNLSNYLrskreefvpyrdkgardvEEEEDDDELYKepltledLICYSFQVARGMEFLASRKCI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 385 HRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA 462
Cdd:cd05054   161 HRDLAARNILLSENNVVKICDFGLA--RDIYKDPDYVRKGDARlpLKWMAPESIF---DKVYTTQSDVWSFGVLLWEIFS 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 463 -GELPYAHINNRDQIIFMVGRGY--ASPDLSrlykncPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd05054   236 lGASPYPGVQMDEEFCRRLKEGTrmRAPEYT------TPEIYQIMLDCWHGEPKERPTFSELVEKL 295
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
274-466 2.45e-26

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 109.14  E-value: 2.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDV-AVKILK--------VVDptpeqlQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWC 343
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTEyAVKRLKedseldwsVVK------NSFLTEVEKLSRFRHPNIVDLAGYsAQQGNYCLIYVYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHVQET--KFQMFQLIDIARQTAQGMDYLH--AKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV-------- 411
Cdd:cd14159    75 PNGSLEDRLHCQVScpCLSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGLARFsrrpkqpg 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 412 KSRWSGSQQVEQptGSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMAGELP 466
Cdd:cd14159   155 MSSTLARTQTVR--GTLAYLPEEYVKT---GTLSVEIDVYSFGVVLLELLTGRRA 204
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
273-467 2.53e-26

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 108.40  E-value: 2.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG-------KWhgdvAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCE 344
Cdd:cd14097     8 KLGQGSFGVVIEAthketqtKW----AIKKINREKAGSSAVKLLEREVDILKHVNHAHIIhLEEVFETPKRMYLVMELCE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLyKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG-------LTVKIGDFGLAtVKSRWSG 417
Cdd:cd14097    84 DGEL-KELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndkLNIKVTDFGLS-VQKYGLG 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14097   162 EDMLQETCGTPIYMAPEVISAHG---YSQQCDIWSIGVIMYMLLCGEPPF 208
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
56-104 2.55e-26

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410361  Cd Length: 49  Bit Score: 101.22  E-value: 2.55e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759  56 TTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCV 104
Cdd:cd20811     1 ISHNFVRKTFFTLAFCDVCRKLLFQGFRCQTCGFKFHQRCSDQVPALCE 49
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
274-523 2.80e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 107.90  E-value: 2.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILK---VVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLY 349
Cdd:cd08220     8 VGRGAYGTVYLCRRKDDNKLVIIKqipVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKaLMIVMEYAPGGTLF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKF-QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT-VKIGDFGLATVKSRWSGSQQVeqpTGS 427
Cdd:cd08220    88 EYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTvVKIGDFGISKILSSKSKAYTV---VGT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMagELPYA-HINNRDQIIFMVGRGYASPDLSRLYKNcpkaMKRLVAD 506
Cdd:cd08220   165 PCYISPELC---EGKPYNQKSDIWALGCVLYELA--SLKRAfEAANLPALVLKIMRGTFAPISDRYSEE----LRHLILS 235
                         250
                  ....*....|....*..
gi 1720416759 507 CVKKVKEERPLFPQILS 523
Cdd:cd08220   236 MLHLDPNKRPTLSEIMA 252
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
274-530 3.06e-26

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 109.37  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY---KGKWHGDVAVKILKVV-DPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSl 348
Cdd:cd06635    33 IGHGSFGAVYfarDVRTSEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGcYLREHTAWLVMEYCLGSA- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqQVEQPTGSV 428
Cdd:cd06635   112 SDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS------PANSFVGTP 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRgyASPDLSRlyKNCPKAMKRLVADCV 508
Cdd:cd06635   186 YWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQN--ESPTLQS--NEWSDYFRNFVDSCL 261
                         250       260
                  ....*....|....*....|..
gi 1720416759 509 KKVKEERPlfpqilSSIELLQH 530
Cdd:cd06635   262 QKIPQDRP------TSEELLKH 277
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
261-526 3.29e-26

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 110.32  E-value: 3.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVDPTPEQlQAFRNEVAVLRKT-RHVNILLFMGYM 331
Cdd:cd05106    33 WEFPRDNLQFGKTLGAGAFGKVVEATAFGlgkednvlRVAVKMLKASAHTDER-EALMSELKILSHLgQHKNIVNLLGAC 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDN-LAIVTQWC---------------------------EGSSLYKHLHVqETKF------------------------ 359
Cdd:cd05106   112 THGGpVLVITEYCcygdllnflrkkaetflnfvmalpeisETSSDYKNITL-EKKYirsdsgfssqgsdtyvemrpvsss 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 360 -------------------QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQ 420
Cdd:cd05106   191 ssqssdskdeedtedswplDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLA--RDIMNDSNY 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQPTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRGY--ASPDLSrlykn 495
Cdd:cd05106   269 VVKGNARlpVKWMAPESIF---DCVYTVQSDVWSYGILLWEIFSlGKSPYPGILVNSKFYKMVKRGYqmSRPDFA----- 340
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1720416759 496 cPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05106   341 -PPEIYSIMKMCWNLEPTERPTFSQISQLIQ 370
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
273-531 3.41e-26

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 108.22  E-value: 3.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSL 348
Cdd:cd06640    11 RIGKGSFGEVFKGidnRTQQVVAIKIIDL-EEAEDEIEDIQQEITVLSQCDSPYVTKYYGsYLKGTKLWIIMEYLGGGSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLhvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQPT--G 426
Cdd:cd06640    90 LDLL--RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLT----DTQIKRNTfvG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRgYASPDLSRLYKncpKAMKRLVAD 506
Cdd:cd06640   164 TPFWMAPEVIQ---QSAYDSKADIWSLGITAIELAKGEPPNSDMHPM-RVLFLIPK-NNPPTLVGDFS---KPFKEFIDA 235
                         250       260
                  ....*....|....*....|....*
gi 1720416759 507 CVKKVKEERPLFPQILSSIELLQHS 531
Cdd:cd06640   236 CLNKDPSFRPTAKELLKHKFIVKNA 260
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
273-460 4.38e-26

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 108.30  E-value: 4.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG-DVAVKILKvvdpTPEQLQAFRN-EVAVLRKTRHVNILLFMGYMTKDN-----LAIVTQWCEG 345
Cdd:cd14143     2 SIGKGRFGEVWRGRWRGeDVAVKIFS----SREERSWFREaEIYQTVMLRHENILGFIAADNKDNgtwtqLWLVSDYHEH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLhvQETKFQMFQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVKIGDFGLAtVKSRwSG 417
Cdd:cd14143    78 GSLFDYL--NRYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGLA-VRHD-SA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQP----TGSVLWMAPEVI--RMQDDNPFSF-QSDVYSYGIVLYEL 460
Cdd:cd14143   154 TDTIDIApnhrVGTKRYMAPEVLddTINMKHFESFkRADIYALGLVFWEI 203
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
272-467 5.33e-26

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 107.69  E-value: 5.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAF-RNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05581     7 KPLGEGSYSTVVLAKEKETgkeYAIKVLDKRHIIKEKKVKYvTIEKEVLSRLAHPGIVkLYYTFQDESKLYFVLEYAPNG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLH------VQETKFQMFQLIDIarqtaqgMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQ 420
Cdd:cd05581    87 DLLEYIRkygsldEKCTRFYTAEIVLA-------LEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDSSPES 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 421 VEQP---------------TGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05581   160 TKGDadsqiaynqaraasfVGTAEYVSPELL---NEKPAGKSSDLWALGCIIYQMLTGKPPF 218
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
273-540 5.81e-26

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 107.89  E-value: 5.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGK---WHGDVAVKILKVVDPTPEQLqaFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSSL 348
Cdd:cd06655    26 KIGQGASGTVFTAIdvaTGQEVAIKQINLQKQPKKEL--IINEILVMKELKNPNIVNFLdSFLVGDELFVVMEYLAGGSL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQPT--G 426
Cdd:cd06655   104 TDV--VTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQIT----PEQSKRSTmvG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyaSPDLSRLYKNCPkAMKRLVAD 506
Cdd:cd06655   178 TPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQNPEKLSP-IFRDFLNR 251
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 507 CVKKVKEERPlfpqilSSIELLQHSLPKINRSAS 540
Cdd:cd06655   252 CLEMDVEKRG------SAKELLQHPFLKLAKPLS 279
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
273-551 7.54e-26

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 107.89  E-value: 7.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLqaFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSSL 348
Cdd:cd06654    27 KIGQGASGTVYTAmdvATGQEVAIRQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGGSL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQPT--G 426
Cdd:cd06654   105 TDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT----PEQSKRSTmvG 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyaSPDLSRlykncPKAMKRLVAD 506
Cdd:cd06654   179 TPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNG--TPELQN-----PEKLSAIFRD 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 507 ----CVKKVKEERPlfpqilSSIELLQHSLPKINRSASEPSLHRAAHTE 551
Cdd:cd06654   249 flnrCLEMDVEKRG------SAKELLQHQFLKIAKPLSSLTPLIAAAKE 291
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
274-488 7.92e-26

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 106.57  E-value: 7.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwHGD----VAVKIL-KVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd14081     9 LGKGQTGLVKLAK-HCVtgqkVAIKIVnKEKLSKESVLMKVEREIAIMKLIEHPNVLkLYDVYENKKYLYLVLEYVSGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKsrwSGSQQVEQPTGS 427
Cdd:cd14081    88 LFDYL-VKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQ---PEGSLLETSCGS 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 428 VLWMAPEVIRMQ--DDNPfsfqSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRG-YASPD 488
Cdd:cd14081   164 PHYACPEVIKGEkyDGRK----ADIWSCGVILYALLVGALPFDDDNLR-QLLEKVKRGvFHIPH 222
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
272-541 1.43e-25

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 105.99  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTV---YKGKWHGDVAVKILKVVDPTPEQLqaFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd06648    13 VKIGEGSTGIVciaTDKSTGRQVAVKKMDLRKQQRREL--LFNEVVIMRDYQHPNIVeMYSSYLVGDELWVVMEFLEGGA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvksrWSGSQQVEQP--- 424
Cdd:cd06648    91 LTDI--VTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFG-------FCAQVSKEVPrrk 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 --TGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYahinnrdqiifmvgrgYASPDLsrlykncpKAMKR 502
Cdd:cd06648   162 slVGTPYWMAPEVISRL---PYGTEVDIWSLGIMVIEMVDGEPPY----------------FNEPPL--------QAMKR 214
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 503 LVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASE 541
Cdd:cd06648   215 IRDNEPPKLKNLHKVSPRLRSFLDRMLVRDPAQRATAAE 253
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
262-521 1.43e-25

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 106.63  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKGKWHGD-------VAVKILKVVDpTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd05090     1 ELPLSAVRFMEELGECAFGKIYKGHLYLPgmdhaqlVAIKTLKDYN-NPQQWNEFQQEASLMTELHHPNIVCLLGVVTQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 N-LAIVTQWCEGSSLYKHLHVQ----------------ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE 397
Cdd:cd05090    80 QpVCMLFEFMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 398 GLTVKIGDFGLAtvKSRWSGSQQVEQPTG--SVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRd 474
Cdd:cd05090   160 QLHVKISDLGLS--REIYSSDYYRVQNKSllPIRWMPPEAIMY---GKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQ- 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 475 QIIFMVGRGYASPdlsrLYKNCPKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd05090   234 EVIEMVRKRQLLP----CSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
273-540 1.47e-25

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 106.73  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLqaFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCEGSSL 348
Cdd:cd06656    26 KIGQGASGTVYTAidiATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLdSYLVGDELWVVMEYLAGGSL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgSQQVEQPT--G 426
Cdd:cd06656   104 TDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT----PEQSKRSTmvG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyaSPDLSRlykncPKAMKRLVAD 506
Cdd:cd06656   178 TPYWMAPEVVTRKAYGP---KVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNG--TPELQN-----PERLSAVFRD 247
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720416759 507 ----CVKKVKEERPlfpqilSSIELLQHSLPKINRSAS 540
Cdd:cd06656   248 flnrCLEMDVDRRG------SAKELLQHPFLKLAKPLS 279
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
256-534 1.47e-25

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 106.62  E-value: 1.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 256 DSSYYWEIEASevmlstrIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRK-TRHVNILLFMGYMTKD 334
Cdd:cd06639    19 DPSDTWDIIET-------IGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSlPNHPNVVKFYGMFYKA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 N------LAIVTQWCEGSS---LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGD 405
Cdd:cd06639    92 DqyvggqLWLVLELCNGGSvteLVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 406 FGLATVKSrwSGSQQVEQPTGSVLWMAPEVI--RMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRG 483
Cdd:cd06639   172 FGVSAQLT--SARLRRNTSVGTPFWMAPEVIacEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPV-KALFKIPRN 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 484 yASPDLSRLYKNCpKAMKRLVADCVKKVKEERPlfpqilSSIELLQHSLPK 534
Cdd:cd06639   249 -PPPTLLNPEKWC-RGFSHFISQCLIKDFEKRP------SVTHLLEHPFIK 291
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
261-526 1.61e-25

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 107.02  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG----------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMG 329
Cdd:cd05101    19 WEFPRDKLTLGKPLGEGCFGQVVMAEAVGidkdkpkeavTVAVKMLKD-DATEKDLSDLVSEMEMMKMIgKHKNIINLLG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 YMTKDN-LAIVTQWCEGSSLYKHLH---------------VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 393
Cdd:cd05101    98 ACTQDGpLYVIVEYASKGNLREYLRarrppgmeysydinrVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 394 FLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHInN 472
Cdd:cd05101   178 LVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALF---DRVYTHQSDVWSFGVLMWEIFTlGGSPYPGI-P 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 473 RDQIIFMVGRGYaspdlsRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05101   254 VEELFKLLKEGH------RMDKpaNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLD 303
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
268-530 1.61e-25

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 106.35  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 268 VMLStRIGSGSFGTVYKGKWHGDVAVKILKVV--DPTPE-QLQAFRnEVAVLRKTRHVNILLFMGYMTKD---NLAIVTQ 341
Cdd:cd06621     4 VELS-SLGEGAGGSVTKCRLRNTKTIFALKTIttDPNPDvQKQILR-ELEINKSCASPYIVKYYGAFLDEqdsSIGIAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSL---YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGS 418
Cdd:cd06621    82 YCEGGSLdsiYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGV----SGELVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY--------AHINNRDQIIFMvgrgyASPDLs 490
Cdd:cd06621   158 SLAGTFTGTSYYMAPERIQGG---PYSITSDVWSLGLTLLEVAQNRFPFppegepplGPIELLSYIVNM-----PNPEL- 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 491 rlyKNCP-------KAMKRLVADCVKKVKEERPlFPQilssiELLQH 530
Cdd:cd06621   229 ---KDEPengikwsESFKDFIEKCLEKDGTRRP-GPW-----QMLAH 266
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
274-475 1.87e-25

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 105.49  E-value: 1.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---YKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSSLY 349
Cdd:cd14069     9 LGEGAFGEVflaVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHrREGEFQYLFLEYASGGELF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLH------VQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd14069    89 DKIEpdvgmpEDVAQFYFQQLM-------AGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKERLLNK 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 424 PTGSVLWMAPEVIRMQddnPFSFQ-SDVYSYGIVLYELMAGELPYAHINNRDQ 475
Cdd:cd14069   162 MCGTLPYVAPELLAKK---KYRAEpVDVWSCGIVLFAMLAGELPWDQPSDSCQ 211
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
274-522 1.89e-25

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 105.46  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKW--HG-DVAVKILKVVDPTPEQLQAF--RnEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEGSS 347
Cdd:cd14162     8 LGHGSYAVVKKAYStkHKcKVAIKIVSKKKAPEDYLQKFlpR-EIEVIKGLKHPNLICFYEAIeTTSRVYIIMELAENGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 L------YKHLHVQETKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA-----TVKSRWS 416
Cdd:cd14162    87 LldyirkNGALPEPQARRWFRQLVA-------GVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFArgvmkTKDGKPK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 GSQQVeqpTGSVLWMAPEVIRMQDDNPfsFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGYASPDLSRLYKNC 496
Cdd:cd14162   160 LSETY---CGSYAYASPEILRGIPYDP--FLSDIWSMGVVLYTMVYGRLPFDDSNLK-VLLKQVQRRVVFPKNPTVSEEC 233
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 497 PKAMKRLVAdcvkKVKeERPLFPQIL 522
Cdd:cd14162   234 KDLILRMLS----PVK-KRITIEEIK 254
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
261-552 2.17e-25

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 107.41  E-value: 2.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG----------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMG 329
Cdd:cd05100     7 WELSRTRLTLGKPLGEGCFGQVVMAEAIGidkdkpnkpvTVAVKMLKD-DATDKDLSDLVSEMEMMKMIgKHKNIINLLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 YMTKDN-LAIVTQWCEGSSLYKHLHVQ---------------ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 393
Cdd:cd05100    86 ACTQDGpLYVLVEYASKGNLREYLRARrppgmdysfdtcklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 394 FLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHInN 472
Cdd:cd05100   166 LVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALF---DRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI-P 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 473 RDQIIFMVGRGYaspdlsRLYK--NCPKAMKRLVADCVKKVKEERPLFPQIL----------SSIELLQHSLPKINRSAS 540
Cdd:cd05100   242 VEELFKLLKEGH------RMDKpaNCTHELYMIMRECWHAVPSQRPTFKQLVedldrvltvtSTDEYLDLSVPFEQYSPG 315
                         330
                  ....*....|..
gi 1720416759 541 EPSLHRAAHTED 552
Cdd:cd05100   316 CPDSPSSCSSGD 327
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
270-530 2.21e-25

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 105.64  E-value: 2.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYK------GKWHgdvAVKIL--KVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVT 340
Cdd:cd14098     4 IIDRLGSGTFAEVKKavevetGKMR---AIKQIvkRKVAGNDKNLQLFQREINILKSLEHPGIVRLIDwYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLATVKsrwSGS 418
Cdd:cd14098    81 EYVEGGDLMDFI-MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLAKVI---HTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPTGSVLWMAPEVIR---MQDDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRG-YASPDLSRLyk 494
Cdd:cd14098   157 TFLVTFCGTMAYLAPEILMskeQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDG-SSQLPVEKRIRKGrYTQPPLVDF-- 233
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd14098   234 NISEEAIDFILRLLDVDPEKRM------TAAQALDH 263
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
274-526 2.70e-25

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 105.77  E-value: 2.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK---WHGDVAVKILKVVDPTPE-QLQAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSSL 348
Cdd:cd14026     5 LSRGAFGTVSRARhadWRVTVAIKCLKLDSPVGDsERNCLLKEAEILHKARFSYILPILGICNEpEFLGIVTEYMTNGSL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQEtkfqMFQLI------DIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLTVKIGDFGLATVK----SRWS 416
Cdd:cd14026    85 NELLHEKD----IYPDVawplrlRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRqlsiSQSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 GSQQVEQpTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyASPDLSR--LYK 494
Cdd:cd14026   161 SSKSAPE-GGTIIYMPPEEYEPSQKRRASVKHDIYSYAIIMWEVLSRKIPFEEVTNPLQIMYSVSQG-HRPDTGEdsLPV 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 495 NCP--KAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd14026   239 DIPhrATLINLIESGWAQNPDERPSFLKCLIELE 272
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
274-524 2.82e-25

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 105.18  E-value: 2.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK--WHGD-VAVKIL---KVVDPT-PEQLqafRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd14663     8 LGEGTFAKVKFARntKTGEsVAIKIIdkeQVAREGmVEQI---KREIAIMKLLRHPNIVeLHEVMATKTKIFFVMELVTG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLY----KHLHVQETK----FQmfQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSG 417
Cdd:cd14663    85 GELFskiaKNGRLKEDKarkyFQ--QLID-------AVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVLWMAPEVIRmqDDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRG------YASPDLSR 491
Cdd:cd14663   156 DGLLHTTCGTPNYVAPEVLA--RRGYDGAKADIWSCGVILFVLLAGYLPF-DDENLMALYRKIMKGefeyprWFSPGAKS 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 492 LYKncpkamKRLVADCVKKVKeerplFPQILSS 524
Cdd:cd14663   233 LIK------RILDPNPSTRIT-----VEQIMAS 254
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
274-532 3.04e-25

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 105.20  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwhgDV------AVKILKVVDPTP-EQ---LQAFRNEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQW 342
Cdd:cd06630     8 LGTGAFSSCYQAR---DVktgtlmAVKQVSFCRNSSsEQeevVEAIREEIRMMARLNHPNIVRMLGATQhKSHFNIFVEW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLHvqetKFQMFQ---LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE-GLTVKIGDFGLAT-VKSRWSG 417
Cdd:cd06630    85 MAGGSVASLLS----KYGAFSenvIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDStGQRLRIADFGAAArLASKGTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVE-QPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY-AH-INNRDQIIFMVGRGYASPDLSrlyK 494
Cdd:cd06630   161 AGEFQgQLLGTIAFMAPEVLRGE---QYGRSCDVWSVGCVIIEMATAKPPWnAEkISNHLALIFKIASATTPPPIP---E 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPlfpqilSSIELLQHSL 532
Cdd:cd06630   235 HLSPGLRDVTLRCLELQPEDRP------PARELLKHPV 266
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
268-523 3.12e-25

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 105.61  E-value: 3.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 268 VMLSTRIGSGSFGTVYKGKWH----GDVAVKILKVVD-PTPEQLQAFRNEVAVLRKTRHVNIL--------------LFM 328
Cdd:cd05043     8 VTLSDLLQEGTFGRIFHGILRdekgKEEEVLVKTVKDhASEIQVTMLLQESSLLYGLSHQNLLpilhvciedgekpmVLY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 329 GYMTKDNLAIVTQWCEgsslykhlHVQETKFQMF---QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGD 405
Cdd:cd05043    88 PYMNWGNLKLFLQQCR--------LSEANNPQALstqQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 406 FGLatvkSR--------WSGSQQvEQPtgsVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQI 476
Cdd:cd05043   160 NAL----SRdlfpmdyhCLGDNE-NRP---IKWMSLESLV---NKEYSSASDVWSFGVLLWELMTlGQTPYVEIDP-FEM 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 477 IFMVGRGYaspdlsRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd05043   228 AAYLKDGY------RLAQpiNCPDELFAVMACCWALDPEERPSFQQLVQ 270
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
274-460 4.92e-25

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 105.21  E-value: 4.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-VAVKILKVVDPtpeqlQAFRNEVAVLRKT--RHVNILLFMGYMTKDN-----LAIVTQWCEG 345
Cdd:cd13998     3 IGKGRFGEVWKASLKNEpVAVKIFSSRDK-----QSWFREKEIYRTPmlKHENILQFIAADERDTalrteLWLVTAFHPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHL--HVQETKfqmfQLIDIARQTAQGMDYLHAK---------NIIHRDMKSNNIFLHEGLTVKIGDFGLATvksR 414
Cdd:cd13998    78 GSL*DYLslHTIDWV----SLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLAV---R 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 415 WSGSQQVEQ-----PTGSVLWMAPEVI--RMQDDNPFSF-QSDVYSYGIVLYEL 460
Cdd:cd13998   151 LSPSTGEEDnanngQVGTKRYMAPEVLegAINLRDFESFkRVDIYAMGLVLWEM 204
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
273-478 4.93e-25

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 104.87  E-value: 4.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKwhgD------VAVKILKVvDPTPEQLQ--AFRnEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWC 343
Cdd:cd07829     6 KLGEGTYGVVYKAK---DkktgeiVALKKIRL-DNEEEGIPstALR-EISLLKELKHPNIVKLLDVIhTENKLYLVFEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EgSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA---TVKSRwsgsqq 420
Cdd:cd07829    81 D-QDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLArafGIPLR------ 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 421 veQPTGSV--LWM-APEVIrMQDDNpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI--IF 478
Cdd:cd07829   154 --TYTHEVvtLWYrAPEIL-LGSKH-YSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLfkIF 212
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
256-530 5.45e-25

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 105.09  E-value: 5.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 256 DSSYYWEIEASevmlstrIGSGSFGTVYK--GKWHGD-VAVKILKVVDPTPEQLQAFRNEVAVLrkTRHVNILLFMGYMT 332
Cdd:cd06638    15 DPSDTWEIIET-------IGKGTYGKVFKvlNKKNGSkAAVKILDPIHDIDEEIEAEYNILKAL--SDHPNVVKFYGMYY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 333 K------DNLAIVTQWCEGSS---LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI 403
Cdd:cd06638    86 KkdvkngDQLWLVLELCNGGSvtdLVKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 404 GDFG----LATVKSRWSGSqqveqpTGSVLWMAPEVI--RMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRdQII 477
Cdd:cd06638   166 VDFGvsaqLTSTRLRRNTS------VGTPFWMAPEVIacEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPM-RAL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 478 FMVGRGyASPDLSR--LYKNcpkAMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd06638   239 FKIPRN-PPPTLHQpeLWSN---EFNDFIRKCLTKDYEKRP------TVSDLLQH 283
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
274-532 5.67e-25

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 104.31  E-value: 5.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGkWHGDVAVKI----LKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMT-----KDNLAIVTQWCE 344
Cdd:cd14033     9 IGRGSFKTVYRG-LDTETTVEVawceLQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKstvrgHKCIILVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHL-HVQETKFQMFQliDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLhEGLT--VKIGDFGLATVKSrwsgSQ 419
Cdd:cd14033    88 SGTLKTYLkRFREMKLKLLQ--RWSRQILKGLHFLHSRCppILHRDLKCDNIFI-TGPTgsVKIGDLGLATLKR----AS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPTGSVLWMAPEVIRMQDDNPFsfqsDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyASPDlsRLYKNCPKA 499
Cdd:cd14033   161 FAKSVIGTPEFMAPEMYEEKYDEAV----DVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSG-IKPD--SFYKVKVPE 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 500 MKRLVADCVKKVKEERplfpqiLSSIELLQHSL 532
Cdd:cd14033   234 LKEIIEGCIRTDKDER------FTIQDLLEHRF 260
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
274-530 5.78e-25

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 104.33  E-value: 5.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPT----PEQLqaFRNEVAVLRKTRHVNI-LLFMGYMTKDNLAIVTQWCEGSSL 348
Cdd:cd14095     8 IGDGNFAVVKECRDKATDKEYALKIIDKAkckgKEHM--IENEVAILRRVKHPNIvQLIEEYDTDTELYLVMELVKGGDL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE----GLTVKIGDFGLATVksrwsgsqqVEQP 424
Cdd:cd14095    86 FDAI-TSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEhedgSKSLKLADFGLATE---------VKEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 ----TGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIF---MVGR-GYASPdlsrLYKNC 496
Cdd:cd14095   156 lftvCGTPTYVAPEIL---AETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDQEELFdliLAGEfEFLSP----YWDNI 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 497 PKAMKRLVADCVKKVKEERplfpqiLSSIELLQH 530
Cdd:cd14095   229 SDSAKDLISRMLVVDPEKR------YSAGQVLDH 256
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
263-526 6.12e-25

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 104.66  E-value: 6.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHGD--------VAVKILKvvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTK- 333
Cdd:cd05092     2 IKRRDIVLKWELGEGAFGKVFLAECHNLlpeqdkmlVAVKALK--EATESARQDFQREAELLTVLQHQHIVRFYGVCTEg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DNLAIVTQWCEGSSLYKHL--HVQETK------------FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL 399
Cdd:cd05092    80 EPLIMVFEYMRHGDLNRFLrsHGPDAKildggegqapgqLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 400 TVKIGDFGLatvkSRWSGSQQVEQPTGSVL----WMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRD 474
Cdd:cd05092   160 VVKIGDFGM----SRDIYSTDYYRVGGRTMlpirWMPPESILYRK---FTTESDIWSFGVVLWEIFTyGKQPWYQLSNTE 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 475 QI-IFMVGRGYASPdlsrlyKNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05092   233 AIeCITQGRELERP------RTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
257-460 6.28e-25

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 104.37  E-value: 6.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 257 SSYYWEIEasEVMLstrIGSGSFGTVYKGKWHGD---VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMT 332
Cdd:cd14046     2 SRYLTDFE--ELQV---LGKGAFGQVVKVRNKLDgryYAIKKIKL-RSESKNNSRILREVMLLSRLNHQHVVRYYQaWIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 333 KDNLAIVTQWCEGSSLY---KHLHVQETKfQMFQLIdiaRQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd14046    76 RANLYIQMEYCEKSTLRdliDSGLFQDTD-RLWRLF---RQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 410 T------------VKSRWSGSQQVEQP-TGSV---LWMAPEVirmQDDNPFSF--QSDVYSYGIVLYEL 460
Cdd:cd14046   152 TsnklnvelatqdINKSTSAALGSSGDlTGNVgtaLYVAPEV---QSGTKSTYneKVDMYSLGIIFFEM 217
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
274-526 7.85e-25

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 104.53  E-value: 7.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG--------DVAVKILKvvDPTPEQLQA-FRNEVAVLRKTRHVNILLFMG-------------YM 331
Cdd:cd05050    13 IGQGAFGRVFQARAPGllpyepftMVAVKMLK--EEASADMQAdFQREAALMAEFDHPNIVKLLGvcavgkpmcllfeYM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDNL-----AIVTQWCEGSSLYKHLHVQET----KFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK 402
Cdd:cd05050    91 AYGDLneflrHRSPRAQCSLSHSTSSARKCGlnplPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMVVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 403 IGDFGLAT---VKSRWSGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIF 478
Cdd:cd05050   171 IADFGLSRniySADYYKASENDAIP---IRWMPPESIFY---NRYTTESDVWAYGVVLWEIFSyGMQPYYGMAH-EEVIY 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 479 MVGRG--YASPDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05050   244 YVRDGnvLSCPD------NCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
262-543 7.99e-25

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 104.34  E-value: 7.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLstrIGSGSFGTVYKGKWHGD-------VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD 334
Cdd:cd05109     6 ETELKKVKV---LGSGAFGTVYKGIWIPDgenvkipVAIKVLRE-NTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 414
Cdd:cd05109    82 TVQLVTQLMPYGCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDqiifmvgrgyaSPDL---- 489
Cdd:cd05109   162 DETEYHADGGKVPIKWMALESILHRR---FTHQSDVWSYGVTVWELMTfGAKPYDGIPARE-----------IPDLlekg 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 490 SRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSsiellqhslpKINRSASEPS 543
Cdd:cd05109   228 ERLPQppICTIDVYMIMVKCWMIDSECRPRFRELVD----------EFSRMARDPS 273
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
274-538 8.17e-25

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 103.96  E-value: 8.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK--GKWHGDV-AVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd06605     9 LGEGNGGVVSKvrHRPSGQImAVKVIRLEIDEALQKQILR-ELDVLHKCNSPYIVGFYGaFYSEGDISICMEYMDGGSLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHL-HVQETKFQmfQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLAT--VKSRWSGSqqveqpT 425
Cdd:cd06605    88 KILkEVGRIPER--ILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGqlVDSLAKTF------V 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 GSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNR---------DQIIFMvgrgyASPDLSRlyKNC 496
Cdd:cd06605   160 GTRSYMAPERI---SGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifellSYIVDE-----PPPLLPS--GKF 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPqilssiELLQHslPKINRS 538
Cdd:cd06605   230 SPDFQDFVSQCLQKDPTERPSYK------ELMEH--PFIKRY 263
C1_B-Raf cd20871
protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated ...
53-115 8.85e-25

protein kinase C conserved region 1 (C1 domain) found in B-Raf (Rapidly Accelerated Fibrosarcoma) kinase and similar proteins; Serine/threonine-protein kinase B-Raf, also called proto-oncogene B-Raf, p94, or v-Raf murine sarcoma viral oncogene homolog B1, activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410421  Cd Length: 60  Bit Score: 97.41  E-value: 8.85e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759  53 VPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVdwsNIRQLLLF 115
Cdd:cd20871     1 VPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCV---NYDQLDLL 60
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
274-474 1.05e-24

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 103.12  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG---DVAVKILKVVDPTPEQLqafRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG---- 345
Cdd:cd14006     1 LGRGRFGVVKRCIEKAtgrEFAAKFIPKRDKKKEAV---LREISILNQLQHPRIIqLHEAYESPTELVLILELCSGgell 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKfqmfqLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL--TVKIGDFGLATvksRWSGSQQVEQ 423
Cdd:cd14006    78 DRLAERGSLSEEE-----VRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLAR---KLNPGEELKE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 424 PTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRD 474
Cdd:cd14006   150 IFGTPEFVAPEIVN---GEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQE 197
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
273-461 1.19e-24

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 103.95  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHG-DVAVKILkvvdptPEQ-LQAFRNEVAV--LRKTRHVNILLFMG-----YMTKDNLAIVTQWC 343
Cdd:cd14053     2 IKARGRFGAVWKAQYLNrLVAVKIF------PLQeKQSWLTEREIysLPGMKHENILQFIGaekhgESLEAEYWLITEFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHVQETKFQmfQLIDIARQTAQGMDYLHA----------KNIIHRDMKSNNIFLHEGLTVKIGDFGLATV-- 411
Cdd:cd14053    76 ERGSLCDYLKGNVISWN--ELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLKSDLTACIADFGLALKfe 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 412 KSRWSGSQ--QVeqptGSVLWMAPEVIrmqdDNPFSFQS------DVYSYGIVLYELM 461
Cdd:cd14053   154 PGKSCGDThgQV----GTRRYMAPEVL----EGAINFTRdaflriDMYAMGLVLWELL 203
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
272-518 1.30e-24

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 103.12  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKG-----KWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05116     1 GELGSGNFGTVKKGyyqmkKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHL----HVQETkfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVe 422
Cdd:cd05116    81 PLNKFLqknrHVTEK-----NITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKA- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTGS--VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFM-VGRGYASPdlsrlyKNCPK 498
Cdd:cd05116   155 QTHGKwpVKWYAPECMNYYK---FSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIeKGERMECP------AGCPP 225
                         250       260
                  ....*....|....*....|
gi 1720416759 499 AMKRLVADCVKKVKEERPLF 518
Cdd:cd05116   226 EMYDLMKLCWTYDVDERPGF 245
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
263-528 1.61e-24

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 103.46  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHGD------VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY----MT 332
Cdd:cd05074     6 IQEQQFTLGRMLGKGEFGSVREAQLKSEdgsfqkVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVslrsRA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 333 KDNLAI---VTQWCEGSSLYKHL---HVQETKFQMFQ------LIDIARqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLT 400
Cdd:cd05074    86 KGRLPIpmvILPFMKHGDLHTFLlmsRIGEEPFTLPLqtlvrfMIDIAS----GMEYLSSKNFIHRDLAARNCMLNENMT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 401 VKIGDFGLAtvKSRWSGS--QQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQII 477
Cdd:cd05074   162 VCVADFGLS--KKIYSGDyyRQGCASKLPVKWLALESLA---DNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYN 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 478 FMVG--RGYASPDlsrlyknCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05074   237 YLIKgnRLKQPPD-------CLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
272-526 1.73e-24

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 102.57  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKGKWHG-DVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSSLY 349
Cdd:cd14057     1 TKINETHSGELWKGRWQGnDIVAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSpPNLVVISQYMPYGSLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLH------VQETKFQMFQLiDIARqtaqGMDYLHA-KNIIHR-DMKSNNIFLHEGLTVKIGdfgLATVKSRWSGSQQV 421
Cdd:cd14057    81 NVLHegtgvvVDQSQAVKFAL-DIAR----GMAFLHTlEPLIPRhHLNSKHVMIDEDMTARIN---MADVKFSFQEPGKM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTgsvlWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRD---QIIFMVGRGYASPDLSRlykncpk 498
Cdd:cd14057   153 YNPA----WMAPEALQKKPEDINRRSADMWSFAILLWELVTREVPFADLSNMEigmKIALEGLRVTIPPGISP------- 221
                         250       260
                  ....*....|....*....|....*...
gi 1720416759 499 AMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd14057   222 HMCKLMKICMNEDPGKRPKFDMIVPILE 249
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
273-461 2.00e-24

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 102.95  E-value: 2.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQafrNEVAVLRKTRHVNILLFMGYMT-KDN---------------- 335
Cdd:cd14047    13 LIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAE---REVKALAKLDHPNIVRYNGCWDgFDYdpetsssnssrsktkc 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHL-HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKsr 414
Cdd:cd14047    90 LFIQMEFCEKGTLESWIeKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTSL-- 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 415 wSGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELM 461
Cdd:cd14047   168 -KNDGKRTKSKGTLSYMSPEQISSQD---YGKEVDIYALGLILFELL 210
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
265-460 2.25e-24

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 103.29  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 265 ASEVMLSTRIGSGSFGTVYKGKWHGD-VAVKILkvvdptpeqlqAFRNEVAVLRKT--------RHVNILLFMGY-MTKD 334
Cdd:cd14142     4 ARQITLVECIGKGRYGEVWRGQWQGEsVAVKIF-----------SSRDEKSWFRETeiyntvllRHENILGFIASdMTSR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 N----LAIVTQWCEGSSLYKHLhvQETKFQMFQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVK 402
Cdd:cd14142    73 NsctqLWLITHYHENGSLYDYL--QRTTLDHQEMLRLALSAASGLVHLHTEifgtqgkpAIAHRDLKSKNILVKSNGQCC 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 403 IGDFGLATVKSRWSGSQQVEQPT--GSVLWMAPEVIRmQDDNPFSFQS----DVYSYGIVLYEL 460
Cdd:cd14142   151 IADLGLAVTHSQETNQLDVGNNPrvGTKRYMAPEVLD-ETINTDCFESykrvDIYAFGLVLWEV 213
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
274-523 3.04e-24

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 102.69  E-value: 3.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-DVAVKILKVV----------------DPTPEQLQAF---RNEVAVLRKTRHVNILLFMGYMTK 333
Cdd:cd14000     2 LGDGGFGSVYRASYKGePVAVKIFNKHtssnfanvpadtmlrhLRATDAMKNFrllRQELTVLSHLHHPSIVYLLGIGIH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DnLAIVTQWCEGSSLYKHL--------HVQETKFQMfqlidIARQTAQGMDYLHAKNIIHRDMKSNNIFL-----HEGLT 400
Cdd:cd14000    82 P-LMLVLELAPLGSLDHLLqqdsrsfaSLGRTLQQR-----IALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAII 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 401 VKIGDFGLATVKSRwSGSQQVEQPTGsvlWMAPEVIRMQDDnpFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMV 480
Cdd:cd14000   156 IKIADYGISRQCCR-MGAKGSEGTPG---FRAPEIARGNVI--YNEKVDVFSFGMLLYEILSGGAPMVG-HLKFPNEFDI 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 481 GRGyASPDLSRLYKNCPKAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd14000   229 HGG-LRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVS 270
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
274-470 3.11e-24

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 103.56  E-value: 3.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-------VAVKILKVVDpTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05108    15 LGSGAFGTVYKGLWIPEgekvkipVAIKELREAT-SPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTG 426
Cdd:cd05108    94 CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKV 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 427 SVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMA-GELPYAHI 470
Cdd:cd05108   174 PIKWMALESILHR---IYTHQSDVWSYGVTVWELMTfGSKPYDGI 215
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
274-467 5.19e-24

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 101.15  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK------GKwhgDVAVKILKVvdPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd14103     1 LGRGKFGTVYRcvekatGK---ELAAKFIKC--RKAKDREDVRNEIEIMNQLRHPRLLqLYDAFETPREMVLVMEYVAGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHlhVQETKFQMFQL--IDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH--EGLTVKIGDFGLAtvkSRWSGSQQVE 422
Cdd:cd14103    76 ELFER--VVDDDFELTERdcILFMRQICEGVQYMHKQGILHLDLKPENILCVsrTGNQIKIIDFGLA---RKYDPDKKLK 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 423 QPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14103   151 VLFGTPEFVAPEVVNYE---PISYATDMWSVGVICYVLLSGLSPF 192
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
274-521 8.13e-24

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 100.79  E-value: 8.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVykgKWHGD------VAVKILKV--VDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMT---KDNLAIVTQW 342
Cdd:cd14119     1 LGEGSYGKV---KEVLDtetlcrRAVKILKKrkLRRIPNGEANVKREIQILRRLNHRNVIKLVDVLYneeKQKLYMVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVE 422
Cdd:cd14119    78 CVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAEDDTCT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTGSVLWMAPEVIRMQDDnpFS-FQSDVYSYGIVLYELMAGELPYahinnRDQIIFM----VGRG-YASPDlsrlykNC 496
Cdd:cd14119   158 TSQGSPAFQPPEIANGQDS--FSgFKVDIWSAGVTLYNMTTGKYPF-----EGDNIYKlfenIGKGeYTIPD------DV 224
                         250       260
                  ....*....|....*....|....*
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd14119   225 DPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
274-516 8.15e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 101.04  E-value: 8.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD----VAVKILKVVDP-----TPEQLQAFRN---EVAVLRKT-RHVNILLFMG-YMTKDNLAIV 339
Cdd:cd08528     8 LGSGAFGCVYKVRKKSNgqtlLALKEINMTNPafgrtEQERDKSVGDiisEVNIIKEQlRHPNIVRYYKtFLENDRLYIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHLHVQETKFQMF---QLIDIARQTAQGMDYLH-AKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRw 415
Cdd:cd08528    88 MELIEGAPLGEHFSSLKEKNEHFtedRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQKGP- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 sGSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYaSPDLSRLYKN 495
Cdd:cd08528   167 -ESSKMTSVVGTILYSCPEIVQNE---PYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEY-EPLPEGMYSD 241
                         250       260
                  ....*....|....*....|.
gi 1720416759 496 cpkAMKRLVADCVKKVKEERP 516
Cdd:cd08528   242 ---DITFVIRSCLTPDPEARP 259
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
263-474 9.34e-24

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 101.68  E-value: 9.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKW--HGD-----VAVKILKVVDpTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN 335
Cdd:cd05110     4 LKETELKRVKVLGSGAFGTVYKGIWvpEGEtvkipVAIKILNETT-GPKANVEFMDEALIMASMDHPHLVRLLGVCLSPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRW 415
Cdd:cd05110    83 IQLVTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRD 474
Cdd:cd05110   163 EKEYNADGGKMPIKWMALECIHYRK---FTHQSDVWSYGVTIWELMTfGGKPYDGIPTRE 219
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
273-468 1.03e-23

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 100.44  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD----VAVKilkVVDPTPEQLQAFRN---EVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCE 344
Cdd:cd14121     2 KLGSGTYATVYKAYRKSGarevVAVK---CVSKSSLNKASTENlltEIELLKKLKHPHIVeLKDFQWDEEHIYLIMEYCS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTV--KIGDFGLATVKSRWSGS 418
Cdd:cd14121    79 GGDLSRFIRsrrtLPESTVRRF-----LQQLASALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFAQHLKPNDEA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEqptGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYA 468
Cdd:cd14121   154 HSLR---GSPLYMAPEMILKKKYDA---RVDLWSVGVILYECLFGRAPFA 197
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
274-518 1.76e-23

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 100.09  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG----KWHGDVAVKILKVVDPTPEQlQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSL 348
Cdd:cd14202    10 IGHGAFAVVFKGrhkeKHDLEVAVKCINKKNLAKSQ-TLLGKEIKILKELKHENIVALYDFQEIANsVYLVMEYCNGGDL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLH---------EGLTVKIGDFGLAtvksRW 415
Cdd:cd14202    89 ADYLHtmrtLSEDTIRLF-----LQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFA----RY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 -SGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRlYK 494
Cdd:cd14202   160 lQNNMMAATLCGSPMYMAPEVIMSQH---YDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPR-ET 235
                         250       260
                  ....*....|....*....|....
gi 1720416759 495 NCPkaMKRLVADCVKKVKEERPLF 518
Cdd:cd14202   236 SSH--LRQLLLGLLQRNQKDRMDF 257
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
283-530 2.01e-23

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 100.36  E-value: 2.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 283 YKGKWhgdVAVKIL--KVVDPTPEQLQafrnEVAVLRKTRHVNILLFMGYMTkD--NLAIVTQWCEGSSLYKHLHVQETK 358
Cdd:cd14042    28 YKGNL---VAIKKVnkKRIDLTREVLK----ELKHMRDLQHDNLTRFIGACV-DppNICILTEYCPKGSLQDILENEDIK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 359 F-QMFQ--LI-DIARqtaqGMDYLHAKNII-HRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAP 433
Cdd:cd14042   100 LdWMFRysLIhDIVK----GMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPPDDSHAYYAKLLWTAP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 434 EVIRMQDDNPFSFQ-SDVYSYGIVLYELMAGELPYaHINNRD----QIIF----MVGRGYASPDLSRLykNCPKAMKRLV 504
Cdd:cd14042   176 ELLRDPNPPPPGTQkGDVYSFGIILQEIATRQGPF-YEEGPDlspkEIIKkkvrNGEKPPFRPSLDEL--ECPDEVLSLM 252
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 505 ADCVKKVKEERPLFPQILSSIELLQH 530
Cdd:cd14042   253 QRCWAEDPEERPDFSTLRNKLKKLNK 278
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
274-518 2.67e-23

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 99.60  E-value: 2.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGDV-AVKILK--------VVDptpeQLQAFRNevaVLRKTRHVNIL-LFMGYMTKDNLAIVTQ 341
Cdd:cd05579     1 ISRGAYGRVYlaKKKSTGDLyAIKVIKkrdmirknQVD----SVLAERN---ILSQAQNPFVVkLYYSFQGKKNLYLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHvqetkfqMFQLID--IAR----QTAQGMDYLHAKNIIHRDMKSNNIFL-HEGlTVKIGDFGLATV--- 411
Cdd:cd05579    74 YLPGGDLYSLLE-------NVGALDedVARiyiaEIVLALEYLHSHGIIHRDLKPDNILIdANG-HLKLTDFGLSKVglv 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 412 -KSRWSGSQQVEQPTGSVL---------WMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYahinNRD--QIIFM 479
Cdd:cd05579   146 rRQIKLSIQKKSNGAPEKEdrrivgtpdYLAPEILLGQ---GHGKTVDWWSLGVILYEFLVGIPPF----HAEtpEEIFQ 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 480 --VGRGYASPDLSRLYKNC---------PKAMKRLVADCVKKVKEErPLF 518
Cdd:cd05579   219 niLNGKIEWPEDPEVSDEAkdlisklltPDPEKRLGAKGIEEIKNH-PFF 267
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
258-531 2.89e-23

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 99.27  E-value: 2.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 258 SYYWEIEASEVMlstriGSGSFGTVYK--GKWHG-DVAVKILKVvdPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTK 333
Cdd:cd14192     1 NSYYAVCPHEVL-----GGGRFGQVHKctELSTGlTLAAKIIKV--KGAKEREEVKNEINIMNQLNHVNLIqLYDAFESK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DNLAIVTQWCEGSSLYKHlhVQETKFQMFQL--IDIARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLA 409
Cdd:cd14192    74 TNLTLIMEYVDGGELFDR--ITDESYQLTELdaILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 tvkSRWSGSQQVEQPTGSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVgrgYASPDL 489
Cdd:cd14192   152 ---RRYKPREKLKVNFGTPEFLAPEVVNY---DFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIV---NCKWDF 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 490 -SRLYKNCPKAMKRLVADCVKKVKEERplfpqiLSSIELLQHS 531
Cdd:cd14192   223 dAEAFENLSEEAKDFISRLLVKEKSCR------MSATQCLKHE 259
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
292-530 3.11e-23

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 99.35  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 292 AVKILKVVDPT------PEQLQAFRNEVAVLRK-TRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLYKHLHV------QET 357
Cdd:cd14093    32 AVKIIDITGEKsseneaEELREATRREIEILRQvSGHPNIIeLHDVFESPTFIFLVFELCRKGELFDYLTEvvtlseKKT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 358 KFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsgSQQVEQPTGSVLWMAPEVIR 437
Cdd:cd14093   112 RRIMRQLFE-------AVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDE---GEKLRELCGTPGYLAPEVLK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 438 --MQDDNP-FSFQSDVYSYGIVLYELMAGELPYAHinnRDQIIF----MVGR-GYASPDlsrlYKNCPKAMKRLVADCVK 509
Cdd:cd14093   182 csMYDNAPgYGKEVDMWACGVIMYTLLAGCPPFWH---RKQMVMlrniMEGKyEFGSPE----WDDISDTAKDLISKLLV 254
                         250       260
                  ....*....|....*....|.
gi 1720416759 510 KVKEERplfpqiLSSIELLQH 530
Cdd:cd14093   255 VDPKKR------LTAEEALEH 269
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
274-523 3.86e-23

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 99.00  E-value: 3.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG----KWHgDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMT-----KDNLAIVTQWCE 344
Cdd:cd14032     9 LGRGSFKTVYKGldteTWV-EVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWEscakgKRCIVLVTELMT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLhvqeTKFQMFQ---LIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLhEGLT--VKIGDFGLATVKsRWSG 417
Cdd:cd14032    88 SGTLKTYL----KRFKVMKpkvLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFI-TGPTgsVKIGDLGLATLK-RASF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVeqpTGSVLWMAPEVIRMQDDNPFsfqsDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKncp 497
Cdd:cd14032   162 AKSV---IGTPEFMAPEMYEEHYDESV----DVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKVTD--- 231
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 498 KAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd14032   232 PEIKEIIGECICKNKEERYEIKDLLS 257
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
274-467 5.16e-23

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 98.85  E-value: 5.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPT----PEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLA-IVTQWCEGSSL 348
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSlllkPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVyVVLELCRRRSL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKhLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSQQvEQPTGSV 428
Cdd:cd14187    95 LE-LHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLAT-KVEYDGERK-KTLCGTP 171
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720416759 429 LWMAPEVIRMQDDnpfSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14187   172 NYIAPEVLSKKGH---SFEVDIWSIGCIMYTLLVGKPPF 207
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
273-480 5.28e-23

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 98.08  E-value: 5.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQlqAFRnEVAVLRK----TRHVNIL-LFMGYMTK--DNLAIVTQW 342
Cdd:cd05118     6 KIGEGAFGTVWLARDKVTgekVAIKKIKNDFRHPKA--ALR-EIKLLKHlndvEGHPNIVkLLDVFEHRggNHLCLVFEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CeGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGLTVKIGDFGLAtvksRWSGSQQV 421
Cdd:cd05118    83 M-GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLADFGLA----RSFTSPPY 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 422 EQPTGSVLWMAPEVIrmQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMV 480
Cdd:cd05118   158 TPYVATRWYRAPEVL--LGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIV 214
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
274-470 5.56e-23

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 98.87  E-value: 5.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKW--HGD---VAVKILKVVDPTPEQ-LQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05111    15 LGSGVFGTVHKGIWipEGDsikIPVAIKVIQDRSGRQsFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQLVTQLLPLGS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGS 427
Cdd:cd05111    95 LLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDDKKYFYSEAKTP 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 428 VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHI 470
Cdd:cd05111   175 IKWMALESIHF---GKYTHQSDVWSYGVTVWEMMTfGAEPYAGM 215
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
267-533 8.16e-23

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 98.54  E-value: 8.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 267 EVMLSTRIGSGSFGTVYKGKWHGD-----VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN------ 335
Cdd:cd05075     1 KLALGKTLGEGEFGSVMEGQLNQDdsvlkVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTesegyp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 --LAIVTQWCEGSS----LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd05075    81 spVVILPFMKHGDLhsflLYSRLGDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 tvKSRWSGS--QQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNrDQIIFMVGRGyas 486
Cdd:cd05075   161 --KKIYNGDyyRQGRISKMPVKWIAIESLA---DRVYTTKSDVWSFGVTMWEIATrGQTPYPGVEN-SEIYDYLRQG--- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 487 pdlSRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLP 533
Cdd:cd05075   232 ---NRLKQppDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKDLP 277
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
268-526 8.73e-23

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 98.38  E-value: 8.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 268 VMLSTRIGSGSFGTVYKGKWHGD------VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG------------ 329
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQDdgsqlkVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGvcftasdlnkpp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 -------YMTKDNLaivtqwcEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK 402
Cdd:cd05035    81 spmvilpFMKHGDL-------HSYLLYSRLGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 403 IGDFGLAtvKSRWSGS--QQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFM 479
Cdd:cd05035   154 VADFGLS--RKIYSGDyyRQGRISKMPVKWIALESLA---DNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYL 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 480 VGRgyaspdlSRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd05035   229 RNG-------NRLKQpeDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLE 270
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
261-523 9.46e-23

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 98.59  E-value: 9.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKgKWHGD----VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNL 336
Cdd:cd06616     1 YEFTAEDLKDLGEIGRGAFGTVNK-MLHKPsgtiMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSSL---YKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLA-- 409
Cdd:cd06616    80 CWICMELMDISLdkfYKYVYeVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISgq 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 ----TVKSRWSGSqqveQPtgsvlWMAPEVIR-MQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGY 484
Cdd:cd06616   160 lvdsIAKTRDAGC----RP-----YMAPERIDpSASRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQVVKGD 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 485 A---SPDLSRLYKNCpkaMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd06616   231 PpilSNSEEREFSPS---FVNFVNLCLIKDESKRPKYKELLK 269
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
273-534 1.39e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 98.13  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTV--YKGKWHG-DVAVKILKVVDPTPEQLqaFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSL 348
Cdd:cd06659    28 KIGEGSTGVVciAREKHSGrQVAVKMMDLRKQQRREL--LFNEVVIMRDYQHPNVVeMYKSYLVGEELWVLMEYLQGGAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsGSQQVEQPTGSV 428
Cdd:cd06659   106 TDI--VSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISK--DVPKRKSLVGTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAhinnRDQIIFMVGRGYAS--PDLSRLYKNCPkAMKRLVAD 506
Cdd:cd06659   182 YWMAPEVI---SRCPYGTEVDIWSLGIMVIEMVDGEPPYF----SDSPVQAMKRLRDSppPKLKNSHKASP-VLRDFLER 253
                         250       260
                  ....*....|....*....|....*...
gi 1720416759 507 CVKKVKEERPLFPQILSSIELLQHSLPK 534
Cdd:cd06659   254 MLVRDPQERATAQELLDHPFLLQTGLPE 281
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
274-522 1.40e-22

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 97.31  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPT----PEQLQAFRNEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQWCEGSSL 348
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSrvakPHQREKIVNEIELHRDLHHKHVVKFSHHFEdAENIYIFLELCSRKSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 ---YKHLHV---QETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvkSRWSGSQQVE 422
Cdd:cd14189    89 ahiWKARHTllePEVRYYLKQII-------SGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLA---ARLEPPEQRK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPT-GSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLykncpkAMK 501
Cdd:cd14189   159 KTIcGTPNYLAPEVLLRQGHGP---ESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSL------PAR 229
                         250       260
                  ....*....|....*....|.
gi 1720416759 502 RLVADCVKKVKEERPLFPQIL 522
Cdd:cd14189   230 HLLAGILKRNPGDRLTLDQIL 250
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
274-477 1.41e-22

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 97.33  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwHGDV----AVKIL---KVVDPtpEQLQAFRNEVAVLRKTRH---VNilLFMGYMTKDNLAIVTQWC 343
Cdd:cd05578     8 IGKGSFGKVCIVQ-KKDTkkmfAMKYMnkqKCIEK--DSVRNVLNELEILQELEHpflVN--LWYSFQDEEDMYMVVDLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrWSGSQQVEQ 423
Cdd:cd05578    83 LGGDLRYHLQ-QKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK---LTDGTLATS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 424 PTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYaHINNR---DQII 477
Cdd:cd05578   159 TSGTKPYMAPEVFMRAG---YSFAVDWWSLGVTAYEMLRGKRPY-EIHSRtsiEEIR 211
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
273-467 2.04e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.03  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGK---WHGDVAVKILK---VVDPTpeqLQA-FRNE---VAVLRktrHVNI-----------LLFmgym 331
Cdd:NF033483   14 RIGRGGMAEVYLAKdtrLDRDVAVKVLRpdlARDPE---FVArFRREaqsAASLS---HPNIvsvydvgedggIPY---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 tkdnlaIVTQWCEGSSL------YKHLHVQETkfqmfqlIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGlTVKIG 404
Cdd:NF033483   84 ------IVMEYVDGRTLkdyireHGPLSPEEA-------VEIMIQILSALEHAHRNGIVHRDIKPQNILItKDG-RVKVT 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 405 DFGLAtvksRWSGSQQVEQpTGSVL----WMAPEVIR--MQDdnpfsFQSDVYSYGIVLYELMAGELPY 467
Cdd:NF033483  150 DFGIA----RALSSTTMTQ-TNSVLgtvhYLSPEQARggTVD-----ARSDIYSLGIVLYEMLTGRPPF 208
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
274-523 2.30e-22

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 96.74  E-value: 2.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVD---PTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN--LAIVTQWCEGSSL 348
Cdd:cd08223     8 IGKGSYGEVWLVRHKRDRKQYVIKKLNlknASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgfLYIVMGFCEGGDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGS 427
Cdd:cd08223    88 YTRLKEQKGVlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLE--SSSDMATTLIGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAgeLPYAhINNRD--QIIFMVGRGyASPDLSRLYKncpKAMKRLVA 505
Cdd:cd08223   166 PYYMSPELF---SNKPYNHKSDVWALGCCVYEMAT--LKHA-FNAKDmnSLVYKILEG-KLPPMPKQYS---PELGELIK 235
                         250
                  ....*....|....*...
gi 1720416759 506 DCVKKVKEERPLFPQILS 523
Cdd:cd08223   236 AMLHQDPEKRPSVKRILR 253
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
274-460 2.95e-22

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 97.43  E-value: 2.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-VAVKILkvvdpTPEQLQAFRNEVAV--LRKTRHVNILLFMG---YMTKDNLA---IVTQWCE 344
Cdd:cd14054     3 IGQGRYGTVWKGSLDERpVAVKVF-----PARHRQNFQNEKDIyeLPLMEHSNILRFIGadeRPTADGRMeylLVLEYAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQETKFQmfQLIDIARQTAQGMDYLHAK---------NIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRW 415
Cdd:cd14054    78 KGSLCSYLRENTLDWM--SSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGS 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 416 SGSQQVEQPT--------GSVLWMAPEV----IRMQDDNPFSFQSDVYSYGIVLYEL 460
Cdd:cd14054   156 SLVRGRPGAAenasisevGTLRYMAPEVlegaVNLRDCESALKQVDVYALGLVLWEI 212
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
270-477 4.07e-22

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 96.31  E-value: 4.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTV---YKGKWHGDVAVKILKVVDPTPEQLQAF------RNEVAVLRKTRHVNIL-LFMGYMTKDNLAIV 339
Cdd:cd14084    10 MSRTLGSGACGEVklaYDKSTCKKVAIKIINKRKFTIGSRREInkprniETEIEILKKLSHPCIIkIEDFFDAEDDYYIV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLY------KHLHVQETKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLat 410
Cdd:cd14084    90 LELMEGGELFdrvvsnKRLKEAICKLYFYQMLL-------AVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGL-- 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 411 vkSRWSGSQQV-EQPTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNR----DQII 477
Cdd:cd14084   161 --SKILGETSLmKTLCGTPTYLAPEVLRSFGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQmslkEQIL 230
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
274-529 4.34e-22

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 96.39  E-value: 4.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-DVAVKILKvvdpTPEQLQAFR-NEVAVLRKTRHVNILLFMGYMTKDN-----LAIVTQWCEGS 346
Cdd:cd14144     3 VGKGRYGEVWKGKWRGeKVAVKIFF----TTEEASWFReTEIYQTVLMRHENILGFIAADIKGTgswtqLYLITDYHENG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHL--HVQETKfqmfQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVKIGDFGLAtVKSRwS 416
Cdd:cd14144    79 SLYDFLrgNTLDTQ----SMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLA-VKFI-S 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 GSQQVEQP----TGSVLWMAPEVIRmQDDNPFSFQS----DVYSYGIVLYELmagelpyahinNRDQIIFMVGRGYASPd 488
Cdd:cd14144   153 ETNEVDLPpntrVGTKRYMAPEVLD-ESLNRNHFDAykmaDMYSFGLVLWEI-----------ARRCISGGIVEEYQLP- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 489 lsrlYKNC----P--KAMKRLVadCVKKVkeeRPLFPQILSSIELLQ 529
Cdd:cd14144   220 ----YYDAvpsdPsyEDMRRVV--CVERR---RPSIPNRWSSDEVLR 257
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
311-524 4.43e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 95.96  E-value: 4.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 311 NEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDM 388
Cdd:cd08221    48 NEIDILSLLNHDNIITYYNhFLDGESLFIEMEYCNGGNLHDKIAQQKNQlFPEEVVLWYLYQIVSAVSHIHKAGILHRDI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 389 KSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYA 468
Cdd:cd08221   128 KTLNIFLTKADLVKLGDFGISKVLD--SESSMAESIVGTPYYMSPELVQ---GVKYNFKSDIWAVGCVLYELLTLKRTFD 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 469 HINNRDQIIFMVGRGYAspDLSRLYKncpKAMKRLVADCVKKVKEERPLFPQILSS 524
Cdd:cd08221   203 ATNPLRLAVKIVQGEYE--DIDEQYS---EEIIQLVHDCLHQDPEDRPTAEELLER 253
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
270-467 5.64e-22

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 95.88  E-value: 5.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKwhgD------VAVKILK-----VVDPTPEQLQAFRNEVAVLRK-TRHVNILLFMGYM-TKDNL 336
Cdd:cd13993     4 LISPIGEGAYGVVYLAV---DlrtgrkYAIKCLYksgpnSKDGNDFQKLPQLREIDLHRRvSRHPNIITLHDVFeTEVAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSSLYKHLH-----VQET---KFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFL-HEGLTVKIGDFG 407
Cdd:cd13993    81 YIVLEYCPNGDLFEAITenriyVGKTeliKNVFLQLID-------AVKHCHSLGIYHRDIKPENILLsQDEGTVKLCDFG 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 408 LATvKSRWSgsqqVEQPTGSVLWMAPEVIRMQDDNPFSFQS---DVYSYGIVLYELMAGELPY 467
Cdd:cd13993   154 LAT-TEKIS----MDFGVGSEFYMAPECFDEVGRSLKGYPCaagDIWSLGIILLNLTFGRNPW 211
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
274-523 5.94e-22

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 95.48  E-value: 5.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTP----EQLqaFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEGSSL 348
Cdd:cd14184     9 IGDGNFAVVKECVERSTGKEFALKIIDKAKccgkEHL--IENEVSILRRVKHPNIIMLIEEMdTPAELYLVMELVKGGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE----GLTVKIGDFGLATVksrwsgsqqVEQP 424
Cdd:cd14184    87 FDAI-TSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLATV---------VEGP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 ----TGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIF---MVGR-GYASPdlsrLYKNC 496
Cdd:cd14184   157 lytvCGTPTYVAPEIIA---ETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFdqiLLGKlEFPSP----YWDNI 229
                         250       260
                  ....*....|....*....|....*..
gi 1720416759 497 PKAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd14184   230 TDSAKELISHMLQVNVEARYTAEQILS 256
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
274-532 5.98e-22

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 95.94  E-value: 5.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG----KWHgDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMT-----KDNLAIVTQWCE 344
Cdd:cd14031    18 LGRGAFKTVYKGldteTWV-EVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWEsvlkgKKCIVLVTELMT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLhvqeTKFQMFQ---LIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLhEGLT--VKIGDFGLATVKsRWSG 417
Cdd:cd14031    97 SGTLKTYL----KRFKVMKpkvLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI-TGPTgsVKIGDLGLATLM-RTSF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVeqpTGSVLWMAPEVIRMQDDNPFsfqsDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLYKncp 497
Cdd:cd14031   171 AKSV---IGTPEFMAPEMYEEHYDESV----DVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKVTD--- 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720416759 498 KAMKRLVADCVKKVKEERplfpqiLSSIELLQHSL 532
Cdd:cd14031   241 PEVKEIIEGCIRQNKSER------LSIKDLLNHAF 269
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
274-521 8.57e-22

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 95.02  E-value: 8.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-DVAVKILKvvdpTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS--SLYK 350
Cdd:cd14068     2 LGDGGFGSVYRAVYRGeDVAVKIFN----KHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPRMLVMELAPKGSldALLQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLHVQETKFQMFQlidIARQTAQGMDYLHAKNIIHRDMKSNNIFL-----HEGLTVKIGDFGLAtvksRWSGSQQVEQPT 425
Cdd:cd14068    78 QDNASLTRTLQHR---IALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIA----QYCCRMGIKTSE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 GSVLWMAPEVIRmqDDNPFSFQSDVYSYGIVLYELMAG--------ELPyahiNNRDQIIFMvGRgyaSPDLSRLYKNCP 497
Cdd:cd14068   151 GTPGFRAPEVAR--GNVIYNQQADVYSFGLLLYDILTCgeriveglKFP----NEFDELAIQ-GK---LPDPVKEYGCAP 220
                         250       260
                  ....*....|....*....|....*
gi 1720416759 498 KAM-KRLVADCVKKVKEERPLFPQI 521
Cdd:cd14068   221 WPGvEALIKDCLKENPQCRPTSAQV 245
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
273-532 9.24e-22

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 95.46  E-value: 9.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYK------GKWhgdVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd07833     8 VVGEGAYGVVLKcrnkatGEI---VAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVnLKEAFRRKGRLYLVFEYVER 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLY------KHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksrwsgsQ 419
Cdd:cd07833    85 TLLElleaspGGLPPDAVRSYIWQLL-------QAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFA---------R 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPTGSVL-------WM-APEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI--IFMVGRGYASPDL 489
Cdd:cd07833   149 ALTARPASPLtdyvatrWYrAPEL--LVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLylIQKCLGPLPPSHQ 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1720416759 490 SRLYKNcpkamKRLVADCVKKVKEERPL---FPQILSS--IELLQHSL 532
Cdd:cd07833   227 ELFSSN-----PRFAGVAFPEPSQPESLerrYPGKVSSpaLDFLKACL 269
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
364-526 9.64e-22

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 97.28  E-value: 9.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 364 LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA---TVKSRWSGSQQVEQPtgsVLWMAPEVIRmqd 440
Cdd:cd05104   216 LLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLArdiRNDSNYVVKGNARLP---VKWMAPESIF--- 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 441 DNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRGY--ASPDLSrlykncPKAMKRLVADCVKKVKEERPL 517
Cdd:cd05104   290 ECVYTFESDVWSYGILLWEIFSlGSSPYPGMPVDSKFYKMIKEGYrmDSPEFA------PSEMYDIMRSCWDADPLKRPT 363

                  ....*....
gi 1720416759 518 FPQILSSIE 526
Cdd:cd05104   364 FKQIVQLIE 372
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
291-521 9.70e-22

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 95.77  E-value: 9.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 291 VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSSLYKHL--HVQETK--------- 358
Cdd:cd05096    49 VAVKILRP-DANKNARNDFLKEVKILSRLKDPNIIRLLGVcVDEDPLCMITEYMENGDLNQFLssHHLDDKeengndavp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 359 ---------FQMfqLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTG--S 427
Cdd:cd05096   128 pahclpaisYSS--LLHVALQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMS--RNLYAGDYYRIQGRAvlP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA--GELPYAHINNrDQIIFMVGRGYASPD----LSRLyKNCPKAMK 501
Cdd:cd05096   204 IRWMAWECILM---GKFTTASDVWAFGVTLWEILMlcKEQPYGELTD-EQVIENAGEFFRDQGrqvyLFRP-PPCPQGLY 278
                         250       260
                  ....*....|....*....|
gi 1720416759 502 RLVADCVKKVKEERPLFPQI 521
Cdd:cd05096   279 ELMLQCWSRDCRERPSFSDI 298
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
274-467 9.99e-22

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 94.51  E-value: 9.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwH----GDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSL 348
Cdd:cd14072     8 IGKGNFAKVKLAR-HvltgREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVkLFEVIETEKTLYLVMEYASGGEV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvkSRWSGSQQVEQPTGSV 428
Cdd:cd14072    87 FDYL-VAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS---NEFTPGNKLDTFCGSP 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQD-DNPfsfQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14072   163 PYAAPELFQGKKyDGP---EVDVWSLGVILYTLVSGSLPF 199
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
262-521 1.78e-21

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 95.04  E-value: 1.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 262 EIEASEVMLSTRIGSGSFGTVYKGKWHG-----------------DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNI 324
Cdd:cd05097     1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGlaeflgegapefdgqpvLVAVKMLRA-DVTKTARNDFLKEIKIMSRLKNPNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 325 LLFMGYMTKDN-LAIVTQWCEGSSLYKHLHVQETKFQMFQ-----------LIDIARQTAQGMDYLHAKNIIHRDMKSNN 392
Cdd:cd05097    80 IRLLGVCVSDDpLCMITEYMENGDLNQFLSQREIESTFTHannipsvsianLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 393 IFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTG--SVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYEL--MAGELPYA 468
Cdd:cd05097   160 CLVGNHYTIKIADFGMS--RNLYSGDYYRIQGRAvlPIRWMAWESILL---GKFTTASDVWAFGVTLWEMftLCKEQPYS 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 469 HINNrDQIIFMVGRGYASPDlSRLYKN----CPKAMKRLVADCVKKVKEERPLFPQI 521
Cdd:cd05097   235 LLSD-EQVIENTGEFFRNQG-RQIYLSqtplCPSPVFKLMMRCWSRDIKDRPTFNKI 289
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
272-515 2.71e-21

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 94.37  E-value: 2.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKGKWHGD-------VAVKILkvvdpTPEQLQAFRNEVAVLR--KTRHVNILLFM-----GYMTKDNLA 337
Cdd:cd14055     1 KLVGKGRFAEVWKAKLKQNasgqyetVAVKIF-----PYEEYASWKNEKDIFTdaSLKHENILQFLtaeerGVGLDRQYW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHL--HVqetkFQMFQLIDIARQTAQGMDYLHAKN---------IIHRDMKSNNIFLHEGLTVKIGDF 406
Cdd:cd14055    76 LITAYHENGSLQDYLtrHI----LSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLADF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 407 GLA-------TVKSrWSGSQQVeqptGSVLWMAPEVI--RMQDDNPFSF-QSDVYSYGIVLYELMAG----------ELP 466
Cdd:cd14055   152 GLAlrldpslSVDE-LANSGQV----GTARYMAPEALesRVNLEDLESFkQIDVYSMALVLWEMASRceasgevkpyELP 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 467 YA-HINNR---DQIIFMVGRGYASPDLSRLYKN-------------C----PKAmkRLVADCVkkvkEER 515
Cdd:cd14055   227 FGsKVRERpcvESMKDLVLRDRGRPEIPDSWLThqgmcvlcdtiteCwdhdPEA--RLTASCV----AER 290
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
226-545 2.88e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 95.28  E-value: 2.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 226 QPKTPVPAQRERAPGsgtqekNKIRPR---------GQRD-----------------------SSYYWEIEA---SEVML 270
Cdd:PLN00034    5 QPPPGVPLPSTARHT------TKSRPRrrpdltlplPQRDpslavplplpppsssssssssssASGSAPSAAkslSELER 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQlqAFRN----EVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEG 345
Cdd:PLN00034   79 VNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHED--TVRRqicrEIEILRDVNHPNVVKCHDmFDHNGEIQVLLEFMDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHlHVQETKFqmfqLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqQVEQP- 424
Cdd:PLN00034  157 GSLEGT-HIADEQF----LADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILA------QTMDPc 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 ---TGSVLWMAPEVIR--MQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGY-----ASPDLSRLYK 494
Cdd:PLN00034  226 nssVGTIAYMSPERINtdLNHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMsqppeAPATASREFR 305
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 495 NcpkamkrLVADCVKKVKEERPlfpqilSSIELLQHSL---PKINRSASEPSLH 545
Cdd:PLN00034  306 H-------FISCCLQREPAKRW------SAMQLLQHPFilrAQPGQGQGGPNLH 346
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
260-467 3.00e-21

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 93.44  E-value: 3.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 260 YWEIEASEVMlstriGSGSFGTVYK--GKWHG-DVAVKILKVvdPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDN 335
Cdd:cd14193     3 YYNVNKEEIL-----GGGRFGQVHKceEKSSGlKLAAKIIKA--RSQKEKEEVKNEIEVMNQLNHANLIqLYDAFESRND 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLAtvkS 413
Cdd:cd14193    76 IVLVMEYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLA---R 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 414 RWSGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14193   153 RYKPREKLRVNFGTPEFLAPEVVNYEF---VSFPTDMWSLGVIAYMLLSGLSPF 203
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
273-524 3.58e-21

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 93.73  E-value: 3.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYK--GKWHGDV-AVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILlfmGYMT------KDNLAIVTQWC 343
Cdd:cd14049    13 RLGKGGYGKVYKvrNKLDGQYyAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIV---GYHTawmehvQLMLYIQMQLC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EgSSLY-------KHLHVQETK-----FQMFQLI-DIARQTAQGMDYLHAKNIIHRDMKSNNIFLH-EGLTVKIGDFGLA 409
Cdd:cd14049    90 E-LSLWdwivernKRPCEEEFKsapytPVDVDVTtKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGLA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 TVKSRWSGSQQVEQP----------TGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMageLPYAHINNRDQIIFM 479
Cdd:cd14049   169 CPDILQDGNDSTTMSrlnglthtsgVGTCLYAAPEQLEGSH---YDFKSDMYSIGVILLELF---QPFGTEMERAEVLTQ 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 480 VGRGYASPDLSRLYKNCPKAMKRLVAdcvkKVKEERPLFPQILSS 524
Cdd:cd14049   243 LRNGQIPKSLCKRWPVQAKYIKLLTS----TEPSERPSASQLLES 283
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
256-528 4.26e-21

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 95.85  E-value: 4.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 256 DSSyyWEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVDPTPEQlQAFRNEVAVLRKT-RHVNILL 326
Cdd:cd05107    29 DSA--WEMPRDNLVLGRTLGSGAFGRVVEATAHGlshsqstmKVAVKMLKSTARSSEK-QALMSELKIMSHLgPHLNIVN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 327 FMGYMTKDN-LAIVTQWCEGSSLYKHLHVQETKFQMF------------------------------------------- 362
Cdd:cd05107   106 LLGACTKGGpIYIITEYCRYGDLVDYLHRNKHTFLQYyldknrddgslisggstplsqrkshvslgsesdggymdmskde 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 363 ------------------------------------------------------QLIDIARQTAQGMDYLHAKNIIHRDM 388
Cdd:cd05107   186 sadyvpmqdmkgtvkyadiessnyespydqylpsapertrrdtlinespalsymDLVGFSYQVANGMEFLASKNCVHRDL 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 389 KSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPY 467
Cdd:cd05107   266 AARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIF---NNLYTTLSDVWSFGILLWEIFTlGGTPY 342
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 468 AHINNRDQIIFMVGRGYASPDLSRLYKNCPKAMKRlvadCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05107   343 PELPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQK----CWEEKFEIRPDFSQLVHLVGDL 399
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
273-460 4.51e-21

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 93.37  E-value: 4.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRnEVAVLRK-TRHVNIL-LFMGYMTKDNLAIVTQWCEGSs 347
Cdd:cd07830     6 QLGDGTFGSVYLARNKETgelVAIKKMKKKFYSWEECMNLR-EVKSLRKlNEHPNIVkLKEVFRENDELYFVFEYMEGN- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA---------T--VKSRW 415
Cdd:cd07830    84 LYQLMKDRKGKpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAreirsrppyTdyVSTRW 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 416 sgsqqveqptgsvlWMAPEVIrMQDDNpFSFQSDVYSYGIVLYEL 460
Cdd:cd07830   164 --------------YRAPEIL-LRSTS-YSSPVDIWALGCIMAEL 192
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
260-467 4.75e-21

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 92.84  E-value: 4.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 260 YWEIEASevmlstrIGSGSFGTVYKGKwH----GDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM-TKD 334
Cdd:cd14071     1 FYDIERT-------IGKGNFAVVKLAR-HritkTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMeTKD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSSLYKHL----HVQETKFQ-MFQLIDIArqtaqgMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd14071    73 MLYLVTEYASNGEIFDYLaqhgRMSEKEARkKFWQILSA------VEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 410 TVksrWSGSQQVEQPTGSVLWMAPEVIRMQD-DNPfsfQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14071   147 NF---FKPGELLKTWCGSPPYAAPEVFEGKEyEGP---QLDIWSLGVVLYVLVCGALPF 199
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
274-461 5.16e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 93.79  E-value: 5.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKV---------VDPTpeqlqAFRnEVAVLRKTRHVNIL-LFMGYMTKDNLAIVT 340
Cdd:cd07841     8 LGEGTYAVVYKARDKETgriVAIKKIKLgerkeakdgINFT-----ALR-EIKLLQELKHPNIIgLLDVFGHKSNINLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEgSSLYKhlhVQETKFQMFQLIDI---ARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSG 417
Cdd:cd07841    82 EFME-TDLEK---VIKDKSIVLTPADIksyMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLA----RSFG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 418 SQQVEQPTGSV-LWM-APEVI---RMqddnpFSFQSDVYSYGIVLYELM 461
Cdd:cd07841   154 SPNRKMTHQVVtRWYrAPELLfgaRH-----YGVGVDMWSVGCIFAELL 197
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
274-467 5.22e-21

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 92.82  E-value: 5.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG----KWHGDVAVK-ILKVVDPTPEQLQAfrNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd14120     1 IGHGAFAVVFKGrhrkKPDLPVAIKcITKKNLSKSQNLLG--KEIKILKELSHENVVaLLDCQETSSSVYLVMEYCNGGD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQ----ETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEG--------LTVKIGDFGLAtvksR 414
Cdd:cd14120    79 LADYLQAKgtlsEDTIRVF-----LQQIAAAMKALHSKGIVHRDLKPQNILLsHNSgrkpspndIRLKIADFGFA----R 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 415 W-SGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14120   150 FlQDGMMAATLCGSPMYMAPEVIMSLQ---YDAKADLWSIGTIVYQCLTGKAPF 200
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
274-467 5.98e-21

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 92.40  E-value: 5.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVyKGKWHG----DVAVKIL---KVVDPTPEQLQafrNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd14075    10 LGSGNFSQV-KLGIHQltkeKVAIKILdktKLDQKTQRLLS---REISSMEKLHHPNIIrLYEVVETLSKLHLVMEYASG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsgSQQVEQPT 425
Cdd:cd14075    86 GELYTKIS-TEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKR---GETLNTFC 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 426 GSVLWMAPEVIRmqDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14075   162 GSPPYAAPELFK--DEHYIGIYVDIWALGVLLYFMVTGVMPF 201
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
274-467 6.40e-21

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 92.98  E-value: 6.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKWHgdvAVKIL---KVVDPTPEQLQAFRNEVAVLRKTRHVnILLFMGYMTKDNLAIVTQWCE 344
Cdd:cd05577     1 LGRGGFGEVCacqvkaTGKMY---ACKKLdkkRIKKKKGETMALNEKIILEKVSSPFI-VSLAYAFETKDKLCLVLTLMN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHL-HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQ 423
Cdd:cd05577    77 GGDLKYHIyNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAV---EFKGGKKIKG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 424 PTGSVLWMAPEVIrmQDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05577   154 RVGTHGYMAPEVL--QKEVAYDFSVDWFALGCMLYEMIAGRSPF 195
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
257-461 6.57e-21

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 93.01  E-value: 6.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 257 SSYYWEIEASEVMlstriGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFM----- 328
Cdd:cd14048     2 SRFLTDFEPIQCL-----GRGGFGVVFEAKNKVDdcnYAVKRIRLPNNELAREKVLR-EVRALAKLDHPGIVRYFnawle 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 329 ----GYMTKDN---LAIVTQWCEGSSLYKHLHVQET--KFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL 399
Cdd:cd14048    76 rppeGWQEKMDevyLYIQMQLCRKENLKDWMNRRCTmeSRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDD 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 400 TVKIGDFGLATVKSRWSGSQQVEQPT----------GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELM 461
Cdd:cd14048   156 VVKVGDFGLVTAMDQGEPEQTVLTPMpayakhtgqvGTRLYMSPEQIH---GNQYSEKVDIFALGLILFELI 224
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
280-521 6.57e-21

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 92.47  E-value: 6.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 280 GTVYKGKWhgdVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLYKHLHVQETK 358
Cdd:cd14043    18 GVAYEGDW---VWLKKFPG-GSHTELRPSTKNVFSKLRELRHENVNLFLGlFVDCGILAIVSEHCSRGSLEDLLRNDDMK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 359 FQ-MFQ---LIDIARqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGSQQVEQPT---GSVLWM 431
Cdd:cd14043    94 LDwMFKsslLLDLIK----GMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYN----EILEAQNLPLPEpapEELLWT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 432 APEVIRMQD-DNPFSFQSDVYSYGIVLYELMAGELPYAHIN-NRDQIIFMVG------RGYASPDLSRLykNCPKAMKRl 503
Cdd:cd14043   166 APELLRDPRlERRGTFPGDVFSFAIIMQEVIVRGAPYCMLGlSPEEIIEKVRsppplcRPSVSMDQAPL--ECIQLMKQ- 242
                         250
                  ....*....|....*...
gi 1720416759 504 vadCVKKVKEERPLFPQI 521
Cdd:cd14043   243 ---CWSEAPERRPTFDQI 257
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
263-515 6.69e-21

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 93.15  E-value: 6.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHGD--------VAVKILKvvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTK- 333
Cdd:cd05094     2 IKRRDIVLKRELGEGAFGKVFLAECYNLsptkdkmlVAVKTLK--DPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DNLAIVTQWCEGSSLYKHLHVQ---------------ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG 398
Cdd:cd05094    80 DPLIMVFEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGAN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 399 LTVKIGDFGLatvkSRWSGSQQVEQPTGSVL----WMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNR 473
Cdd:cd05094   160 LLVKIGDFGM----SRDVYSTDYYRVGGHTMlpirWMPPESIMYRK---FTTESDVWSFGVILWEIFTyGKQPWFQLSNT 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 474 DQI-IFMVGRGYASPDLsrlyknCPKAMKRLVADCVKKVKEER 515
Cdd:cd05094   233 EVIeCITQGRVLERPRV------CPKEVYDIMLGCWQREPQQR 269
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
274-531 6.95e-21

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 92.47  E-value: 6.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwhgDVAVKILKVVDPTPE----QLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSL 348
Cdd:cd06624    16 LGKGTFGVVYAAR---DLSTQVRIAIKEIPErdsrEVQPLHEEIALHSRLSHKNIVQYLGSVSEDGfFKIFMEQVPGGSL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLhvqetKFQMFQLID----IA---RQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLtVKIGDFGlaTVKsRWSGSQ 419
Cdd:cd06624    93 SALL-----RSKWGPLKDnentIGyytKQILEGLKYLHDNKIVHRDIKGDNVLVntYSGV-VKISDFG--TSK-RLAGIN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 -QVEQPTGSVLWMAPEVIrmqDDNPFSF--QSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDL-SRLYKN 495
Cdd:cd06624   164 pCTETFTGTLQYMAPEVI---DKGQRGYgpPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGMFKIHPEIpESLSEE 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 496 CPKAMKRlvadCVKKVKEERPlfpqilSSIELLQHS 531
Cdd:cd06624   241 AKSFILR----CFEPDPDKRA------TASDLLQDP 266
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
270-484 7.41e-21

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 93.27  E-value: 7.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKG----KWHGDVAVKILKVVDPTPEQLQAFR-----NEVAVLRKTRHVNILLFMGYMTKDN-LAIV 339
Cdd:cd14096     5 LINKIGEGAFSNVYKAvplrNTGKPVAIKVVRKADLSSDNLKGSSranilKEVQIMKRLSHPNIVKLLDFQESDEyYYIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYkHLHVQETKFQMfqliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIF--------------------- 394
Cdd:cd14096    85 LELADGGEIF-HQIVRLTYFSE----DLSRhvitQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkadddet 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 395 -LHEGL-----------TVKIGDFGLAtvKSRWsgSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA 462
Cdd:cd14096   160 kVDEGEfipgvggggigIVKLADFGLS--KQVW--DSNTKTPCGTVGYTAPEVVK---DERYSKKVDMWALGCVLYTLLC 232
                         250       260
                  ....*....|....*....|..
gi 1720416759 463 GELPYaHINNRDQIIFMVGRGY 484
Cdd:cd14096   233 GFPPF-YDESIETLTEKISRGD 253
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
261-528 9.12e-21

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 94.71  E-value: 9.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVDPTPEQlQAFRNEVAVLRKT-RHVNILLFMGYM 331
Cdd:cd05105    32 WEFPRDGLVLGRILGSGAFGKVVEGTAYGlsrsqpvmKVAVKMLKPTARSSEK-QALMSELKIMTHLgPHLNIVNLLGAC 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDN-LAIVTQWCEGSSLYKHLHVQETKFQ-------------------------------------------------- 360
Cdd:cd05105   111 TKSGpIYIITEYCFYGDLVNYLHKNRDNFLsrhpekpkkdldifginpadestrsyvilsfenkgdymdmkqadttqyvp 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 361 ---------------------------------------------MFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL 395
Cdd:cd05105   191 mleikeaskysdiqrsnydrpasykgsndsevknllsddgsegltTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 396 HEGLTVKIGDFGLAtvKSRWSGSQQVEQptGS----VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHI 470
Cdd:cd05105   271 AQGKIVKICDFGLA--RDIMHDSNYVSK--GStflpVKWMAPESIF---DNLYTTLSDVWSYGILLWEIFSlGGTPYPGM 343
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 471 NNRDQIIFMVGRGY--ASPDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd05105   344 IVDSTFYNKIKSGYrmAKPD------HATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESL 397
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
274-523 9.82e-21

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 91.96  E-value: 9.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGT---VYKGKWHGDVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSSLY 349
Cdd:cd08219     8 VGEGSFGRallVQHVNSDQKYAMKEIRL-PKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADgHLYIVMEYCDGGDLM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQVEQPTGSV 428
Cdd:cd08219    87 QKIKLQRGKlFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLT--SPGAYACTYVGTP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVirmQDDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRGYASPdlsrLYKNCPKAMKRLVADCV 508
Cdd:cd08219   165 YYVPPEI---WENMPYNNKSDIWSLGCILYELCTLKHPF-QANSWKNLILKVCQGSYKP----LPSHYSYELRSLIKQMF 236
                         250
                  ....*....|....*
gi 1720416759 509 KKVKEERPLFPQILS 523
Cdd:cd08219   237 KRNPRSRPSATTILS 251
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
274-464 1.00e-20

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 92.63  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG--KWHGD-VAVKILKVVDPTPE-QLQAFRnEVAVLRKTRHVNILLFMGYMT-------KDNLAIVTQW 342
Cdd:cd07840     7 IGEGTYGQVYKArnKKTGElVALKKIRMENEKEGfPITAIR-EIKLLQKLDHPNVVRLKEIVTskgsakyKGSIYMVFEY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEG--SSLykhLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGSQQ 420
Cdd:cd07840    86 MDHdlTGL---LDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLA----RPYTKEN 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 421 VEQPTGSV--LWM-APEVIRMQDDnpFSFQSDVYSYGIVLYELMAGE 464
Cdd:cd07840   159 NADYTNRVitLWYrPPELLLGATR--YGPEVDMWSVGCILAELFTGK 203
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
274-478 1.13e-20

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 91.99  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK------WhgDVAVKILKVVDPTPEQLqAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd14201    14 VGHGAFAVVFKGRhrkktdW--EVAIKSINKKNLSKSQI-LLGKEIKILKELQHENIVaLYDVQEMPNSVFLVMEYCNGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHVQ----ETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLH---------EGLTVKIGDFGLAtvks 413
Cdd:cd14201    91 DLADYLQAKgtlsEDTIRVF-----LQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFA---- 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 414 RWSGSQQVEQP-TGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIF 478
Cdd:cd14201   162 RYLQSNMMAATlCGSPMYMAPEVIMSQH---YDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMF 224
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
274-467 1.15e-20

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 92.01  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG---DVAVKILKVVDPtpEQLQAFRNEVAVLRK-TRHVNILLFMG--YMTKDNLA---IVTQWCE 344
Cdd:cd13985     8 LGEGGFSYVYLAHDVNtgrRYALKRMYFNDE--EQLRVAIKEIEIMKRlCGHPNIVQYYDsaILSSEGRKevlLLMEYCP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSsLYKHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLTVKIGDFGLATVKS----RWSG 417
Cdd:cd13985    86 GS-LVDILEKSPpSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHypleRAEE 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 418 SQQVEQPTGS---VLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd13985   165 VNIIEEEIQKnttPMYRAPEMIDLYSKKPIGEKADIWALGCLLYKLCFFKLPF 217
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
263-533 1.19e-20

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 92.41  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHGD--------VAVKILKvvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTK- 333
Cdd:cd05093     2 IKRHNIVLKRELGEGAFGKVFLAECYNLcpeqdkilVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DNLAIVTQWCEGSSLYKHLHV------------QETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTV 401
Cdd:cd05093    80 DPLIMVFEYMKHGDLNKFLRAhgpdavlmaegnRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 402 KIGDFGLatvkSRWSGSQQVEQPTGSVL----WMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQI 476
Cdd:cd05093   160 KIGDFGM----SRDVYSTDYYRVGGHTMlpirWMPPESIMYRK---FTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 477 -IFMVGRGYASPdlsrlyKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLP 533
Cdd:cd05093   233 eCITQGRVLQRP------RTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASP 284
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
274-515 1.58e-20

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 92.04  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMT-----KDNLAIVTQWCEG 345
Cdd:cd14030    33 IGRGSFKTVYKGldtETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEstvkgKKCIVLVTELMTS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLhvqeTKFQMFQLIDI---ARQTAQGMDYLHAKN--IIHRDMKSNNIFLhEGLT--VKIGDFGLATVKsRWSGS 418
Cdd:cd14030   113 GTLKTYL----KRFKVMKIKVLrswCRQILKGLQFLHTRTppIIHRDLKCDNIFI-TGPTgsVKIGDLGLATLK-RASFA 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVeqpTGSVLWMAPEVIRMQDDNPFsfqsDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPDLSRLykNCPK 498
Cdd:cd14030   187 KSV---IGTPEFMAPEMYEEKYDESV----DVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPASFDKV--AIPE 257
                         250
                  ....*....|....*..
gi 1720416759 499 aMKRLVADCVKKVKEER 515
Cdd:cd14030   258 -VKEIIEGCIRQNKDER 273
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
273-466 1.66e-20

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 91.22  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKvvdptpeqlQAFRNEVAVLRKTR----------HVNILLF-MGYMTKDNLAI 338
Cdd:cd14050     8 KLGEGSFGEVFKVRSREDgklYAVKRSR---------SRFRGEKDRKRKLEeverheklgeHPNCVRFiKAWEEKGILYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCeGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLaTVKSRWSGS 418
Cdd:cd14050    79 QTELC-DTSLQQYCE-ETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGL-VVELDKEDI 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 419 QQVEQptGSVLWMAPEVIrmqdDNPFSFQSDVYSYGIVLYELMAG-ELP 466
Cdd:cd14050   156 HDAQE--GDPRYMAPELL----QGSFTKAADIFSLGITILELACNlELP 198
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
274-515 1.84e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 92.38  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKWHgdvAVKIL-KVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05595     3 LGKGTFGKVIlvrekaTGRYY---AMKILrKEVIIAKDEVAHTVTESRVLQNTRHPFLTaLKYAFQTHDRLCFVMEYANG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvQETKFQMfqliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQV 421
Cdd:cd05595    80 GELFFHLS-RERVFTE----DRARfygaEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC--KEGITDGATM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAhinNRD-----QIIFMvgrgyaspDLSRLYKNC 496
Cdd:cd05595   153 KTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPFY---NQDherlfELILM--------EEIRFPRTL 218
                         250
                  ....*....|....*....
gi 1720416759 497 PKAMKRLVADCVKKVKEER 515
Cdd:cd05595   219 SPEAKSLLAGLLKKDPKQR 237
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
269-467 1.88e-20

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 91.07  E-value: 1.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 269 MLSTRIGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLQAF-RNEVAVLRKTRHVNILLFMGY--MTKDNLAIVTQW 342
Cdd:cd14164     3 TLGTTIGEGSFSKVKLAtsqKYCCKVAIKIVDRRRASPDFVQKFlPRELSILRRVNHPNIVQMFECieVANGRLYIVMEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKhlhVQETKF-QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH-EGLTVKIGDFGLAtvksrwsgsQQ 420
Cdd:cd14164    83 AATDLLQK---IQEVHHiPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFA---------RF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 421 VEQPT-------GSVLWMAPEVIRMQDDNPFSFqsDVYSYGIVLYELMAGELPY 467
Cdd:cd14164   151 VEDYPelsttfcGSRAYTPPEVILGTPYDPKKY--DVWSLGVVLYVMVTGTMPF 202
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
261-525 2.68e-20

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 92.37  E-value: 2.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMGYM 331
Cdd:cd14207     2 WEFARERLKLGKSLGRGAFGKVVQASAFGikksptcrVVAVKMLKE-GATASEYKALMTELKILIHIgHHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDN--LAIVTQWCEGSSLYKHLH------------------------------------------------VQETK--- 358
Cdd:cd14207    81 TKSGgpLMVIVEYCKYGNLSNYLKskrdffvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgFQEDKsls 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 359 ----------------FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVE 422
Cdd:cd14207   161 dveeeeedsgdfykrpLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLA--RDIYKNPDYVR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHI-------NNRDQIIFMVGRGYASPDLSrl 492
Cdd:cd14207   239 KGDARlpLKWMAPESIF---DKIYSTKSDVWSYGVLLWEIFSlGASPYPGVqidedfcSKLKEGIRMRAPEFATSEIY-- 313
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1720416759 493 ykncpkamkRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd14207   314 ---------QIMLDCWQGDPNERPRFSELVERL 337
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
274-466 2.77e-20

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 90.94  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK---GKWHGDV-AVKILKVVDPTPEQLQAFRNEVAVLRKTR---HVNILLFM-GYMTKDNLAIVTQWCEG 345
Cdd:cd14052     8 IGSGEFSQVYKvseRVPTGKVyAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIdSWEYHGHLYIQTELCEN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQM--FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrWSGSQQVEQ 423
Cdd:cd14052    88 GSLDVFLSELGLLGRLdeFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATV---WPLIRGIER 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 424 pTGSVLWMAPEVI-RMQDDNPfsfqSDVYSYGIVLYELMAG-ELP 466
Cdd:cd14052   165 -EGDREYIAPEILsEHMYDKP----ADIFSLGLILLEAAANvVLP 204
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
263-533 2.99e-20

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 91.15  E-value: 2.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 263 IEASEVMLSTRIGSGSFGTVYKGKWHGD------VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG------- 329
Cdd:cd14204     4 IDRNLLSLGKVLGEGEFGSVMEGELQQPdgtnhkVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGvclevgs 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 -----------YMTKDNLAIVTQWCEGSSLYKHLHVQE-TKFqmfqLIDIArqtaQGMDYLHAKNIIHRDMKSNNIFLHE 397
Cdd:cd14204    84 qripkpmvilpFMKYGDLHSFLLRSRLGSGPQHVPLQTlLKF----MIDIA----LGMEYLSSRNFLHRDLAARNCMLRD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 398 GLTVKIGDFGLAtvKSRWSGS--QQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRD 474
Cdd:cd14204   156 DMTVCVADFGLS--KKIYSGDyyRQGRIAKMPVKWIAVESLA---DRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHE 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 475 QIIFM-VGRGYASPDlsrlykNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLP 533
Cdd:cd14204   231 IYDYLlHGHRLKQPE------DCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESLP 284
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
273-507 3.80e-20

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 90.87  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD-VAVKILKvvdpTPEQLQAFR-NEVAVLRKTRHVNILLFM-----GYMTKDNLAIVTQWCEG 345
Cdd:cd14220     2 QIGKGRYGEVWMGKWRGEkVAVKVFF----TTEEASWFReTEIYQTVLMRHENILGFIaadikGTGSWTQLYLITDYHEN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVqeTKFQMFQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVKIGDFGLAtVKSRwSG 417
Cdd:cd14220    78 GSLYDFLKC--TTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLA-VKFN-SD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQP----TGSVLWMAPEVIRmQDDNPFSFQ----SDVYSYGIVLYEL----MAG------ELPYAHINNRD----- 474
Cdd:cd14220   154 TNEVDVPlntrVGTKRYMAPEVLD-ESLNKNHFQayimADIYSFGLIIWEMarrcVTGgiveeyQLPYYDMVPSDpsyed 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720416759 475 --QIIFMVGrgyASPDLSRLYKN--CPKAMKRLVADC 507
Cdd:cd14220   233 mrEVVCVKR---LRPTVSNRWNSdeCLRAVLKLMSEC 266
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
274-469 3.89e-20

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 90.97  E-value: 3.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKV-VDPTPEQLQAFRNEVAVLRKTRHVNILLFMgyMTKDNLAIVT--------- 340
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTgeyVAIKKCRQeLSPSDKNRERWCLEVQIMKKLNHPNVVSAR--DVPPELEKLSpndlpllam 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLHVQETKFQM--FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG---LTVKIGDFGLAtvKSRW 415
Cdd:cd13989    79 EYCSGGDLRKVLNQPENCCGLkeSEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGggrVIYKLIDLGYA--KELD 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 416 SGSQQVEQpTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAH 469
Cdd:cd13989   157 QGSLCTSF-VGTLQYLAPELFESK---KYTCTVDYWSFGTLAFECITGYRPFLP 206
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
271-523 4.25e-20

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 90.41  E-value: 4.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGSFGT-VYKGKWHG-DVAVK-ILkvvdptPEQLQAFRNEVAVLRKT-RHVNILLFMgYMTKDN--LAIVTQWCE 344
Cdd:cd13982     6 PKVLGYGSEGTiVFRGTFDGrPVAVKrLL------PEFFDFADREVQLLRESdEHPNVIRYF-CTEKDRqfLYIALELCA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GS--SLYKHLHV-QETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-----HEGLTVKIGDFGLA-TVKSRW 415
Cdd:cd13982    79 ASlqDLVESPREsKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMISDFGLCkKLDVGR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQPTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVL-YELMAGELPYAHINNRDQIIFmvgRGYASPDLSRLYK 494
Cdd:cd13982   159 SSFSRRSGVAGTSGWIAPEMLSGSTKRRQTRAVDIFSLGCVFyYVLSGGSHPFGDKLEREANIL---KGKYSLDKLLSLG 235
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 495 NCPKAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd13982   236 EHGPEAQDLIERMIDFDPEKRPSAEEVLN 264
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
274-467 5.25e-20

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 89.92  E-value: 5.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK---WHGDVAVKIL-KVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSL 348
Cdd:cd14186     9 LGKGSFACVYRARslhTGLEVAIKMIdKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNyVYLVLEMCHNGEM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksrwsgsqQVEQPT--- 425
Cdd:cd14186    89 SRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLAT---------QLKMPHekh 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759 426 ----GSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14186   160 ftmcGTPNYISPEIATR---SAHGLESDVWSLGCMFYTLLVGRPPF 202
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
274-529 5.30e-20

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 90.10  E-value: 5.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-----VAVKILKVVdPTPEQLQAFRNEVAVLRKT-RHVNILLFMGYM-TKDNLAIVTQWCEGS 346
Cdd:cd05047     3 IGEGNFGQVLKARIKKDglrmdAAIKRMKEY-ASKDDHRDFAGELEVLCKLgHHPNIINLLGACeHRGYLYLAIEYAPHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHL---------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV 411
Cdd:cd05047    82 NLLDFLrksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 412 KSRWSGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQIIFMVGRGYaspdls 490
Cdd:cd05047   162 QEVYVKKTMGRLP---VRWMAIESLNY---SVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCA-ELYEKLPQGY------ 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 491 RLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQ 529
Cdd:cd05047   229 RLEKplNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRML 269
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
261-476 5.68e-20

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 89.78  E-value: 5.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMlstriGSGSFGTVYKGKWHG---DVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNL 336
Cdd:cd14082     3 YQIFPDEVL-----GSGQFGIVYGGKHRKtgrDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECmFETPERV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEG-------SSLYKHLHVQETKFQMFQLIDIARqtaqgmdYLHAKNIIHRDMKSNNIFL--HEGL-TVKIGDF 406
Cdd:cd14082    78 FVVMEKLHGdmlemilSSEKGRLPERITKFLVTQILVALR-------YLHSKNIVHCDLKPENVLLasAEPFpQVKLCDF 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 407 GLATVKSRWSGSQQVeqpTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY---AHINnrDQI 476
Cdd:cd14082   151 GFARIIGEKSFRRSV---VGTPAYLAPEVLRNK---GYNRSLDMWSVGVIIYVSLSGTFPFnedEDIN--DQI 215
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
291-526 8.29e-20

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 90.05  E-value: 8.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 291 VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLID--- 366
Cdd:cd05095    49 VAVKMLRA-DANKNARNDFLKEIKIMSRLKDPNIIRLLAVcITDDPLCMITEYMENGDLNQFLSRQQPEGQLALPSNalt 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 367 --------IARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTG--SVLWMAPEVI 436
Cdd:cd05095   128 vsysdlrfMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMS--RNLYSGDYYRIQGRAvlPIRWMSWESI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 437 RMqddNPFSFQSDVYSYGIVLYELMA--GELPYAHINNrDQIIFMVGRGY---------ASPDLsrlyknCPKAMKRLVA 505
Cdd:cd05095   206 LL---GKFTTASDVWAFGVTLWETLTfcREQPYSQLSD-EQVIENTGEFFrdqgrqtylPQPAL------CPDSVYKLML 275
                         250       260
                  ....*....|....*....|.
gi 1720416759 506 DCVKKVKEERPLFPQILSSIE 526
Cdd:cd05095   276 SCWRRDTKDRPSFQEIHTLLQ 296
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
261-529 8.44e-20

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 90.81  E-value: 8.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVVDPTPEQlQAFRNEVAVLRKT-RHVNILLFMGYM 331
Cdd:cd05102     2 WEFPRDRLRLGKVLGHGAFGKVVEASAFGidksssceTVAVKMLKEGATASEH-KALMSELKILIHIgNHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDN--LAIVTQWCEGSSLYKHLHVQ------------ETKFQMFQLIDIAR---------------------------- 369
Cdd:cd05102    81 TKPNgpLMVIVEFCKYGNLSNFLRAKregfspyrerspRTRSQVRSMVEAVRadrrsrqgsdrvasftestsstnqprqe 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 370 -------------------QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS--V 428
Cdd:cd05102   161 vddlwqspltmedlicysfQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA--RDIYKDPDYVRKGSARlpL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRG-------YASPDLSRLYKNCPKAM 500
Cdd:cd05102   239 KWMAPESIF---DKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQINEEFCQRLKDGtrmrapeYATPEIYRIMLSCWHGD 315
                         330       340       350
                  ....*....|....*....|....*....|
gi 1720416759 501 KRlvadcvkkvkeERPLFPQILSSI-ELLQ 529
Cdd:cd05102   316 PK-----------ERPTFSDLVEILgDLLQ 334
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
274-472 9.00e-20

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 89.18  E-value: 9.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVdPTPEQLQAF--RNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLYK 350
Cdd:cd14114    10 LGTGAFGVVHRCTERATGNNFAAKFI-MTPHESDKEtvRKEIQIMNQLHHPKLInLHDAFEDDNEMVLILEFLSGGELFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH--EGLTVKIGDFGLATvksRWSGSQQVEQPTGSV 428
Cdd:cd14114    89 RIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLAT---HLDPKESVKVTTGTA 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 429 LWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAHINN 472
Cdd:cd14114   166 EFAAPEIV---EREPVGFYTDMWAVGVLSYVLLSGLSPFAGEND 206
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
271-460 9.11e-20

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 89.64  E-value: 9.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGSFGTVYKGKWHGD---VAVKilKVVDPTPEQ---LQAFRnEVAVLRKTR---HVNI--LL--FMGYMTKD--N 335
Cdd:cd07838     4 VAEIGEGAYGTVYKARDLQDgrfVALK--KVRVPLSEEgipLSTIR-EIALLKQLEsfeHPNVvrLLdvCHGPRTDRelK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEgSSLYKHL-HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 414
Cdd:cd07838    81 LTLVFEHVD-QDLATYLdKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIYSF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 wsgsqqvEQPTGSV---LWM-APEVIrMQDdnPFSFQSDVYSYGIVLYEL 460
Cdd:cd07838   160 -------EMALTSVvvtLWYrAPEVL-LQS--SYATPVDMWSVGCIFAEL 199
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
273-467 9.47e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 89.71  E-value: 9.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTV------YKGKwhgDVAVKILKVVDPTPEQLqaFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd06658    29 KIGEGSTGIVciatekHTGK---QVAVKKMDLRKQQRREL--LFNEVVIMRDYHHENVVdMYNSYLVGDELWVVMEFLEG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQveQPT 425
Cdd:cd06658   104 GALTDI--VTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRK--SLV 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 426 GSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd06658   180 GTPYWMAPEVISRL---PYGTEVDIWSLGIMVIEMIDGEPPY 218
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
274-521 1.22e-19

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 89.48  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWH---GDVAVKilKVV-DPTpeqlqaFRN-EVAVLRKTRHVNIL-LFMGYMTKDN------LAIVTQ 341
Cdd:cd14137    12 IGSGSFGVVYQAKLLetgEVVAIK--KVLqDKR------YKNrELQIMRRLKHPNIVkLKYFFYSSGEkkdevyLNLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 wCEGSSLYKHLHVQETKFQMFQLIDI---ARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGLTVKIGDFGLAT--VKSRW 415
Cdd:cd14137    84 -YMPETLYRVIRHYSKNKQTIPIIYVklySYQLFRGLAYLHSLGICHRDIKPQNLLVdPETGVLKLCDFGSAKrlVPGEP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVeqptgSVLWMAPEVI-RMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQ---IIFMVGrgyaSPDLSR 491
Cdd:cd14137   163 NVSYIC-----SRYYRAPELIfGATD---YTTAIDIWSAGCVLAELLLGQPLFPGESSVDQlveIIKVLG----TPTREQ 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 1720416759 492 LykncpKAMkrlvadcvkKVKEERPLFPQI 521
Cdd:cd14137   231 I-----KAM---------NPNYTEFKFPQI 246
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
274-540 1.25e-19

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 89.36  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQwCEGSSLY 349
Cdd:cd06618    23 IGSGTCGQVYKMRHKKTghvMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYfITDSDVFICME-LMSTCLD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQMFQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLAtvkSRWSGSQQVEQPTGSV 428
Cdd:cd06618   102 KLLKRIQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGIS---GRLVDSKAKTRSAGCA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVgRGYASPDLSrLYKNCPKAMKRLVADCV 508
Cdd:cd06618   179 AYMAPERIDPPDNPKYDIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKI-LNEEPPSLP-PNEGFSPDFCSFVDLCL 256
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 509 KKVKEERPLFPqilssiELLQHSLPKINRSAS 540
Cdd:cd06618   257 TKDHRYRPKYR------ELLQHPFIRRYETAE 282
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
270-467 1.46e-19

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 88.48  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKwHG----DVAVKIL-KVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWC 343
Cdd:cd14079     6 LGKTLGVGSFGKVKLAE-HEltghKVAVKILnRQKIKSLDMEEKIRREIQILKLFRHPHIIrLYEVIETPTDIFMVMEYV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKsrwSGSQQVEQ 423
Cdd:cd14079    85 SGGELFDYI-VQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIM---RDGEFLKT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGSVLWMAPEVIrmqddnpfSFQS------DVYSYGIVLYELMAGELPY 467
Cdd:cd14079   161 SCGSPNYAAPEVI--------SGKLyagpevDVWSCGVILYALLCGSLPF 202
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
274-467 1.72e-19

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 90.14  E-value: 1.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKWHgdvAVKILKV-VDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05593    23 LGKGTFGKVIlvrekaSGKYY---AMKILKKeVIIAKDEVAHTLTESRVLKNTRHPFLTsLKYSFQTKDRLCFVMEYVNG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPT 425
Cdd:cd05593   100 GELFFHLS-RERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC--KEGITDAATMKTFC 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 426 GSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05593   177 GTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF 215
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
274-474 2.23e-19

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 89.34  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGDV-AVKILKvvdptPEQLQAfRNEVA-------VLRKTRH-VNILLFMGYMTKDNLAIVTQW 342
Cdd:cd05571     3 LGKGTFGKVIlcREKATGELyAIKILK-----KEVIIA-KDEVAhtltenrVLQNTRHpFLTSLKYSFQTNDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLHvQETKFQMfqliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGS 418
Cdd:cd05571    77 VNGGELFFHLS-RERVFSE----DRTRfygaEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC--KEEISYG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 419 QQVEQPTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYahiNNRD 474
Cdd:cd05571   150 ATTKTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF---YNRD 199
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
292-506 2.63e-19

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 88.10  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 292 AVKILKVVDP--TPEQLQAFRN----EVAVLRKTR-HVNIL-LFMGYMTKDNLAIVTQWCEGSSLYKHLhVQETKFQMFQ 363
Cdd:cd14181    39 AVKIIEVTAErlSPEQLEEVRSstlkEIHILRQVSgHPSIItLIDSYESSTFIFLVFDLMRRGELFDYL-TEKVTLSEKE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 364 LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQPTGSVLWMAPEVIR--MQDD 441
Cdd:cd14181   118 TRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSC---HLEPGEKLRELCGTPGYLAPEILKcsMDET 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 442 NP-FSFQSDVYSYGIVLYELMAGELPYAHinnRDQIIF----MVGR-GYASPD-----------LSRLYKNCPKamKRLV 504
Cdd:cd14181   195 HPgYGKEVDLWACGVILFTLLAGSPPFWH---RRQMLMlrmiMEGRyQFSSPEwddrsstvkdlISRLLVVDPE--IRLT 269

                  ..
gi 1720416759 505 AD 506
Cdd:cd14181   270 AE 271
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
262-522 2.90e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 92.11  E-value: 2.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  262 EIEASEVMLSTRIGSGSFGTVYKGK---------WHGdVAVKILKvvDPTPEQLQAfrnEVAVLRKTRHVNILLFMG-YM 331
Cdd:PTZ00266     9 ESRLNEYEVIKKIGNGRFGEVFLVKhkrtqeffcWKA-ISYRGLK--EREKSQLVI---EVNVMRELKHKNIVRYIDrFL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  332 TKDN--LAIVTQWCEGSSLYKHLhvqETKFQMF------QLIDIARQTAQGMDYLH-------AKNIIHRDMKSNNIFLH 396
Cdd:PTZ00266    83 NKANqkLYILMEFCDAGDLSRNI---QKCYKMFgkieehAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759  397 EGL-----------------TVKIGDFGLatvkSRWSGSQQVEQP-TGSVLWMAPEVIrMQDDNPFSFQSDVYSYGIVLY 458
Cdd:PTZ00266   160 TGIrhigkitaqannlngrpIAKIGDFGL----SKNIGIESMAHScVGTPYYWSPELL-LHETKSYDDKSDMWALGCIIY 234
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759  459 ELMAGELPYAHINNRDQIIFMVGRGyasPDLSrlYKNCPKAMKRLVADCVKKVKEERPLFPQIL 522
Cdd:PTZ00266   235 ELCSGKTPFHKANNFSQLISELKRG---PDLP--IKGKSKELNILIKNLLNLSAKERPSALQCL 293
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
303-522 2.96e-19

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 87.76  E-value: 2.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 303 PEQLQAFRNEVAVLRKTRHVNILLFMGYMT-KDNLAIVTQWCEGSSL------YKHLHVQETKFQMfqlidiaRQTAQGM 375
Cdd:cd14188    42 PHQREKIDKEIELHRILHHKHVVQFYHYFEdKENIYILLEYCSRRSMahilkaRKVLTEPEVRYYL-------RQIVSGL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 376 DYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvkSRWSGSQQVEQPT-GSVLWMAPEVIRMQDDnpfSFQSDVYSYG 454
Cdd:cd14188   115 KYLHEQEILHRDLKLGNFFINENMELKVGDFGLA---ARLEPLEHRRRTIcGTPNYLSPEVLNKQGH---GCESDIWALG 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 455 IVLYELMAGELPYAHINNRDQIIFMVGRGYASPdlsrlyKNCPKAMKRLVADCVKKVKEERPLFPQIL 522
Cdd:cd14188   189 CVMYTMLLGRPPFETTNLKETYRCIREARYSLP------SSLLAPAKHLIASMLSKNPEDRPSLDEII 250
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
261-531 3.51e-19

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 88.88  E-value: 3.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTRIGSGSFGTVYKGKWHG--------DVAVKILKVvDPTPEQLQAFRNEVAVLRKT-RHVNILLFMGYM 331
Cdd:cd05103     2 WEFPRDRLKLGKPLGRGAFGQVIEADAFGidktatcrTVAVKMLKE-GATHSEHRALMSELKILIHIgHHLNVVNLLGAC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 TKDN--LAIVTQWCEGSSLYKHLHVQETKFQMFQ---------------------------------------------- 363
Cdd:cd05103    81 TKPGgpLMVIVEFCKFGNLSAYLRSKRSEFVPYKtkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 364 --------------------LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQ 423
Cdd:cd05103   161 veeeeagqedlykdfltledLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA--RDIYKDPDYVRK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGS--VLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRG-------YASPDlsrly 493
Cdd:cd05103   239 GDARlpLKWMAPETIF---DRVYTIQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCRRLKEGtrmrapdYTTPE----- 310
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1720416759 494 kncpkaMKRLVADCVKKVKEERPLFPQILSSI-ELLQHS 531
Cdd:cd05103   311 ------MYQTMLDCWHGEPSQRPTFSELVEHLgNLLQAN 343
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
274-467 4.27e-19

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 88.52  E-value: 4.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK---VVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05616     8 LGKGSFGKVMLAERKGTdelYAVKILKkdvVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSqQVEQPTGS 427
Cdd:cd05616    88 LMYHIQ-QVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK-ENIWDGV-TTKTFCGT 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05616   165 PDYIAPEIIAYQ---PYGKSVDWWAFGVLLYEMLAGQAPF 201
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
266-467 4.34e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 87.39  E-value: 4.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 266 SEVMLSTRIGSGSFGTVYKGKWHGD---VAVK---ILKVVDPTPEQlqAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAI 338
Cdd:cd08228     2 ANFQIEKKIGRGQFSEVYRATCLLDrkpVALKkvqIFEMMDAKARQ--DCVKEIDLLKQLNHPNVIKYLDSFIEDNeLNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEG---SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrw 415
Cdd:cd08228    80 VLELADAgdlSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS-- 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 416 SGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd08228   158 SKTTAAHSLVGTPYYMSPERIH---ENGYNFKSDIWSLGCLLYEMAALQSPF 206
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
267-467 4.38e-19

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 87.54  E-value: 4.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 267 EVMLSTRIGSGSFGTVYKGkWHGD---------VAVKILKVVD-PTPEQLQAFRNEVAVLRKTRHVNILLFMGYM-TKDN 335
Cdd:cd14076     2 PYILGRTLGEGEFGKVKLG-WPLPkanhrsgvqVAIKLIRRDTqQENCQTSKIMREINILKGLTHPNIVRLLDVLkTKKY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRW 415
Cdd:cd14076    81 IGIVLEFVSGGELFDYILARR-RLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 416 SGsQQVEQPTGSVLWMAPEVIRMqdDNPFS-FQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14076   160 NG-DLMSTSCGSPCYAAPELVVS--DSMYAgRKADIWSCGVILYAMLAGYLPF 209
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
270-532 4.83e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 87.02  E-value: 4.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVY------KGKwhgDVAVKILKVVDPTPE---QLQAFRNEVAVLRKTRHVNILLFMGYM---TKDNLA 337
Cdd:cd06652     6 LGKLLGQGAFGRVYlcydadTGR---ELAVKQVQFDPESPEtskEVNALECEIQLLKNLLHERIVQYYGCLrdpQERTLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLHVQETkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG----LATVKS 413
Cdd:cd06652    83 IFMEYMPGGSIKDQLKSYGA-LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGaskrLQTICL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RWSGSQQVeqpTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGYASPDLsrly 493
Cdd:cd06652   162 SGTGMKSV---TGTPYWMSPEVISGEG---YGRKADIWSVGCTVVEMLTEKPPWAEFEAM-AAIFKIATQPTNPQL---- 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 494 kncPKAMKRLVADCVKKVKEERPLFPqilSSIELLQHSL 532
Cdd:cd06652   231 ---PAHVSDHCRDFLKRIFVEAKLRP---SADELLRHTF 263
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
273-467 5.88e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 87.39  E-value: 5.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFR-NEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLYK 350
Cdd:cd06657    27 KIGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLfNEVVIMRDYQHENVVeMYNSYLVGDELWVVMEFLEGGALTD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HlhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsGSQQVEQPTGSVLW 430
Cdd:cd06657   107 I--VTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK--EVPRRKSLVGTPYW 182
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720416759 431 MAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd06657   183 MAPELISRL---PYGPEVDIWSLGIMVIEMVDGEPPY 216
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
275-495 6.48e-19

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 86.42  E-value: 6.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 275 GSGSFGTVY--KGKWHGDVAVKilKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLYKH 351
Cdd:cd14111    12 ARGRFGVIRrcRENATGKNFPA--KIVPYQAEEKQGVLQEYEILKSLHHERIMaLHEAYITPRYLVLIAEFCSGKELLHS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSgSQQVEQPTGSVLWM 431
Cdd:cd14111    90 L-IDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLS-LRQLGRRTGTLEYM 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 432 APEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGrgyASPDLSRLYKN 495
Cdd:cd14111   168 APEMVK---GEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILV---AKFDAFKLYPN 225
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
311-521 7.74e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 87.00  E-value: 7.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 311 NEVAVLRK--TRHVnILLFMGYMTKDNLAIVTQWCEGSSLYKHL-HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRD 387
Cdd:cd05630    49 NEKQILEKvnSRFV-VSLAYAYETKDALCLVLTLMNGGDLKFHIyHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 388 MKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05630   128 LKPENILLDDHGHIRISDLGLAV---HVPEGQTIKGRVGTVGYMAPEVVK---NERYTFSPDWWALGCLLYEMIAGQSPF 201
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 468 AHIN---NRDQIIFMVGRG---YA---SPDLSRLYKN--CPKAMKRLvaDC----VKKVKEErPLFPQI 521
Cdd:cd05630   202 QQRKkkiKREEVERLVKEVpeeYSekfSPQARSLCSMllCKDPAERL--GCrgggAREVKEH-PLFKKL 267
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
273-476 8.33e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 86.21  E-value: 8.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYK------GK-WHGdvavKILKVVdpTPEQLQAFRNEVAVLRKTRHVNILLFM-GYMTKDNLAIVTQWCE 344
Cdd:cd14191     9 RLGSGKFGQVFRlvekktKKvWAG----KFFKAY--SAKEKENIRQEISIMNCLHHPKLVQCVdAFEEKANIVMVLEMVS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLAtvkSRWSGSQQVE 422
Cdd:cd14191    83 GGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLA---RRLENAGSLK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 423 QPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI 476
Cdd:cd14191   160 VLFGTPEFVAPEVINYE---PIGYATDMWSIGVICYILVSGLSPFMGDNDNETL 210
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
274-469 8.63e-19

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 86.21  E-value: 8.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV--YKGKWHGD---VAVKILKVVDPTPEQLQ---AFRNEVAVLRKTRHVNILLFMGYM--TKDNLAIVTQWC 343
Cdd:cd13994     1 IGKGATSVVriVTKKNPRSgvlYAVKEYRRRDDESKRKDyvkRLTSEYIISSKLHHPNIVKVLDLCqdLHGKWCLVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLY------KHLHVQEtKFQMFqlidiaRQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV------ 411
Cdd:cd13994    81 PGGDLFtliekaDSLSLEE-KDCFF------KQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVfgmpae 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 412 -KSRWSGSqqveqPTGSVLWMAPEVIRMQDDNPFSfqSDVYSYGIVLYELMAGELPYAH 469
Cdd:cd13994   154 kESPMSAG-----LCGSEPYMAPEVFTSGSYDGRA--VDVWSCGIVLFALFTGRFPWRS 205
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
274-468 9.50e-19

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 86.23  E-value: 9.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKwhgDVAVKILKVvDP----TPEQLQAFRNEVAVLRKTRHVNILLFMGYM---TKDNLAIVT 340
Cdd:cd06653    10 LGRGAFGEVYlcydadTGR---ELAVKQVPF-DPdsqeTSKEVNALECEIQLLKNLRHDRIVQYYGCLrdpEEKKLSIFV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT-VKSRW 415
Cdd:cd06653    86 EYMPGGSVKDQLKaygaLTENVTRRY-----TRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrIQTIC 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 416 SGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYA 468
Cdd:cd06653   161 MSGTGIKSVTGTPYWMSPEVISGEG---YGRKADVWSVACTVVEMLTEKPPWA 210
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
271-530 9.51e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 86.22  E-value: 9.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGSFGTVYKG---KWHGDVAVKILKVvdptpEQLQAfrNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd13995     9 SDFIPRGAFGKVYLAqdtKTKKRMACKLIPV-----EQFKP--SDVEIQACFRHENIAeLYGALLWEETVHLFMEAGEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLhvqETKFQM--FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIgDFGLATvksrwSGSQQVEQP 424
Cdd:cd13995    82 SVLEKL---ESCGPMreFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSV-----QMTEDVYVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 T---GSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRD---QIIFMVGRgyASPDLSRLYKNCPK 498
Cdd:cd13995   153 KdlrGTEIYMSPEVILCRGHNT---KADIYSLGATIIHMQTGSPPWVRRYPRSaypSYLYIIHK--QAPPLEDIAQDCSP 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 499 AMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd13995   228 AMRELLEAALERNPNHRS------SAAELLKH 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
274-467 9.98e-19

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 85.90  E-value: 9.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG---DVAVK-ILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSL 348
Cdd:cd14073     9 LGKGTYGKVKLAIERAtgrEVAIKsIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIrIYEVFENKDKIVIVMEYASGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrWSGSQQVEQPTGSV 428
Cdd:cd14073    89 YDYIS-ERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNL---YSKDKLLQTFCGSP 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720416759 429 LWMAPEVIRMQddnPFSF-QSDVYSYGIVLYELMAGELPY 467
Cdd:cd14073   165 LYASPEIVNGT---PYQGpEVDCWSLGVLLYTLVYGTMPF 201
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
274-474 1.09e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 87.33  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGDV-AVKIL--KVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05604     4 IGKGSFGKVLlaKRKRDGKYyAVKVLqkKVILNRKEQKHIMAERNVLLKNVKHPFLVgLHYSFQTTDKLYFVLDFVNGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS 427
Cdd:cd05604    84 LFFHLQ-RERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC--KEGISNSDTTTTFCGT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 428 VLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAhinNRD 474
Cdd:cd05604   161 PEYLAPEVIRKQ---PYDNTVDWWCLGSVLYEMLYGLPPFY---CRD 201
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
274-530 1.12e-18

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 86.20  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTP--EQLQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEGSSLYK 350
Cdd:cd14183    14 IGDGNFAVVKECVERSTGREYALKIINKSKcrGKEHMIQNEVSILRRVKHPNIVLLIEEMdMPTELYLVMELVKGGDLFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE----GLTVKIGDFGLATVksrwsgsqqVEQP-- 424
Cdd:cd14183    94 AI-TSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLATV---------VDGPly 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 --TGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIF---MVGR-GYASPdlsrLYKNCPK 498
Cdd:cd14183   164 tvCGTPTYVAPEIIA---ETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFdqiLMGQvDFPSP----YWDNVSD 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 499 AMKRLVADCVKKVKEERplfpqiLSSIELLQH 530
Cdd:cd14183   237 SAKELITMMLQVDVDQR------YSALQVLEH 262
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
274-541 1.17e-18

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 87.20  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFR--NEVAVLRKTRHVNIL----LF--MGYMTKDNLAIVTQW 342
Cdd:cd07834     8 IGSGAYGVVcsaYDKRTGRKVAIK--KISNVFDDLIDAKRilREIKILRHLKHENIIglldILrpPSPEEFNDVYIVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEgSSLYK---------HLHVQetkFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvks 413
Cdd:cd07834    86 ME-TDLHKvikspqpltDDHIQ---YFLYQIL-------RGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLA---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RwsgsQQVEQPTGSVL-------WM-APEVIRMQDDnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQ---IIFMVGr 482
Cdd:cd07834   151 R----GVDPDEDKGFLteyvvtrWYrAPELLLSSKK--YTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQlnlIVEVLG- 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 483 gyaSPDLSRL-YKNCPKAMKRLVAdcvkKVKEERPLFPQILSS-----IELLQHSL---PKINRSASE 541
Cdd:cd07834   224 ---TPSEEDLkFISSEKARNYLKS----LPKKPKKPLSEVFPGaspeaIDLLEKMLvfnPKKRITADE 284
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
274-467 1.19e-18

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 87.06  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK----VVDPTPEQLQAFRNEVAVLRKTrHVNILLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05587     4 LGKGSFGKVMLAERKGTdelYAIKILKkdviIQDDDVECTMVEKRVLALSGKP-PFLTQLHSCFQTMDRLYFVMEYVNGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTG 426
Cdd:cd05587    83 DLMYHIQ-QVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMC--KEGIFGGKTTRTFCG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 427 SVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05587   160 TPDYIAPEIIAYQ---PYGKSVDWWAYGVLLYEMLAGQPPF 197
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
274-511 1.27e-18

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 85.81  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGT--VYKGKWHGD-VAVKILKVVDPTPEQLQafrNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEGSSLY 349
Cdd:cd14665     8 IGSGNFGVarLMRDKQTKElVAVKYIERGEKIDENVQ---REIINHRSLRHPNIVRFKEVIlTPTHLAIVMEYAAGGELF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHL------HVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLhEGLT---VKIGDFGLAtvKSRWSGSQQ 420
Cdd:cd14665    85 ERIcnagrfSEDEARFFFQQLI-------SGVSYCHSMQICHRDLKLENTLL-DGSPaprLKICDFGYS--KSSVLHSQP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 vEQPTGSVLWMAPEVIRMQD-DNPFsfqSDVYSYGIVLYELMAGELPYAHI----NNRDQIIFMVGRGYASPDLSRLYKN 495
Cdd:cd14665   155 -KSTVGTPAYIAPEVLLKKEyDGKI---ADVWSCGVTLYVMLVGAYPFEDPeeprNFRKTIQRILSVQYSIPDYVHISPE 230
                         250
                  ....*....|....*..
gi 1720416759 496 CPKAMKRL-VADCVKKV 511
Cdd:cd14665   231 CRHLISRIfVADPATRI 247
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
274-495 1.30e-18

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 85.66  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLYKHL 352
Cdd:cd14087     9 IGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRHTNIIQLIEvFETKERVYMVMELATGGELFDRI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 353 hVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNN-IFLHEGLTVK--IGDFGLATvkSRWSGSQQVEQPT-GSV 428
Cdd:cd14087    89 -IAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENlLYYHPGPDSKimITDFGLAS--TRKKGPNCLMKTTcGTP 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 429 LWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGYAS------PDLSRLYKN 495
Cdd:cd14087   166 EYIAPEILLRK---PYTQSVDMWAVGVIAYILLSGTMPFDD-DNRTRLYRQILRAKYSysgepwPSVSNLAKD 234
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
274-476 1.41e-18

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 86.92  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK----VVDPTPEqLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05620     3 LGKGSFGKVLLAELKGKgeyFAVKALKkdvvLIDDDVE-CTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYkhLHVQET-KFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPT 425
Cdd:cd05620    82 DLM--FHIQDKgRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMC--KENVFGDNRASTFC 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 426 GSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYaHINNRDQI 476
Cdd:cd05620   158 GTPDYIAPEILQGLK---YTFSVDWWSFGVLLYEMLIGQSPF-HGDDEDEL 204
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
274-471 1.55e-18

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 86.09  E-value: 1.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGD-VAVKIL---KVVDPtpEQLQAFRNEVAVLRKTRH---VNilLFMGYMTKDNLAIVTQWCE 344
Cdd:cd05580     9 LGTGSFGRVRlvKHKDSGKyYALKILkkaKIIKL--KQVEHVLNEKRILSEVRHpfiVN--LLGSFQDDRNLYMVMEYVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLhVQETKFQmfqlIDIAR-QTAQ---GMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrwsgsqq 420
Cdd:cd05580    85 GGELFSLL-RRSGRFP----NDVAKfYAAEvvlALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKR--------- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 421 VEQPT----GSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHIN 471
Cdd:cd05580   151 VKDRTytlcGTPEYLAPEIILSK---GHGKAVDWWALGILIYEMLAGYPPFFDEN 202
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
273-545 1.65e-18

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 86.17  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQ---LQAFRnEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCE---G 345
Cdd:cd07870     7 KLGEGSYATVYKGISRINGQLVALKVISMKTEEgvpFTAIR-EASLLKGLKHANIVLLHDIIhTKETLTFVFEYMHtdlA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKH---LHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVE 422
Cdd:cd07870    86 QYMIQHpggLHPYNVRLFMFQLL-------RGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTgsvLWMAPEVIRMQDDNpFSFQSDVYSYGIVLYELMAGELPYAHINN----RDQIIFMVGRGYAS--PDLSRL---- 492
Cdd:cd07870   159 VVT---LWYRPPDVLLGATD-YSSALDIWGAGCIFIEMLQGQPAFPGVSDvfeqLEKIWTVLGVPTEDtwPGVSKLpnyk 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 493 ---YKNCPKAMKRLVADCVKKVKEERPLFPQILSsiellqhSLPKINRSASEPSLH 545
Cdd:cd07870   235 pewFLPCKPQQLRVVWKRLSRPPKAEDLASQMLM-------MFPKDRISAQDALLH 283
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
277-462 1.71e-18

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 86.25  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 277 GSFGTVYKGKWHGD-VAVKILKVVDPtpeqlQAFRNEVAV--LRKTRHVNILLFMGYMTKD-----NLAIVTQWCEGSSL 348
Cdd:cd14141     6 GRFGCVWKAQLLNEyVAVKIFPIQDK-----LSWQNEYEIysLPGMKHENILQFIGAEKRGtnldvDLWLITAFHEKGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQmfQLIDIARQTAQGMDYLHAK----------NIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGS 418
Cdd:cd14141    81 TDYLKANVVSWN--ELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSA 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPTGSVLWMAPEVIrmqdDNPFSFQS------DVYSYGIVLYELMA 462
Cdd:cd14141   159 GDTHGQVGTRRYMAPEVL----EGAINFQRdaflriDMYAMGLVLWELAS 204
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
274-547 1.74e-18

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 85.95  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKV--VDPTPE-QLQAFRnEVAVLRKTRHVNILLFMG--YMTKDNLAIVTQWCEGSSL 348
Cdd:cd06620    13 LGAGNGGSVSKVLHIPTGTIMAKKVihIDAKSSvRKQILR-ELQILHECHSPYIVSFYGafLNENNNIIICMEYMDCGSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQeTKFQMFQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGSQQVEQPTGS 427
Cdd:cd06620    92 DKILKKK-GPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGV----SGELINSIADTFVGT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEviRMQDDNpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQiifmvgrGYASP----DL-------------- 489
Cdd:cd06620   167 STYMSPE--RIQGGK-YSVKSDVWSLGLSIIELALGEFPFAGSNDDDD-------GYNGPmgilDLlqrivneppprlpk 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 490 SRLYkncPKAMKRLVADCVKKVKEERPlfpqilsSIELLQHSLPKINRSASEPSLHRA 547
Cdd:cd06620   237 DRIF---PKDLRDFVDRCLLKDPRERP-------SPQLLLDHDPFIQAVRASDVDLRA 284
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
274-530 1.98e-18

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 85.34  E-value: 1.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD--VAVKILKVVDPTPEQLQAFRNEVAVLRKTRH-VNILLFMGY---MTKDNLAIVTQwCEGSS 347
Cdd:cd14131     9 LGKGGSSKVYKVLNPKKkiYALKRVDLEGADEQTLQSYKNEIELLKKLKGsDRIIQLYDYevtDEDDYLYMVME-CGEID 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGlTVKIGDFGLATVKSRWSGSQQVEQPTG 426
Cdd:cd14131    88 LATILKKKRpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG-RLKLIDFGIAKAIQNDTTSIVRDSQVG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 427 SVLWMAPE-VIRMQDDNPF------SFQSDVYSYGIVLYELMAGELPYAHI-----------NNRDQIIFMVgrgYASPD 488
Cdd:cd14131   167 TLNYMSPEaIKDTSASGEGkpkskiGRPSDVWSLGCILYQMVYGKTPFQHItnpiaklqaiiDPNHEIEFPD---IPNPD 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 489 LSRLYKNCpkamkrLVADcvkkvKEERPLFPqilssiELLQH 530
Cdd:cd14131   244 LIDVMKRC------LQRD-----PKKRPSIP------ELLNH 268
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
265-530 2.14e-18

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 86.26  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 265 ASEVMLSTRIGSGSFGTVYKGKWHGD-VAVKILKvvdpTPEQLQAFR-NEVAVLRKTRHVNILLFM-----GYMTKDNLA 337
Cdd:cd14219     4 AKQIQMVKQIGKGRYGEVWMGKWRGEkVAVKVFF----TTEEASWFReTEIYQTVLMRHENILGFIaadikGTGSWTQLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLhvQETKFQMFQLIDIARQTAQGMDYLHAK--------NIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd14219    80 LITDYHENGSLYDYL--KSTTLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIADLGLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 TvkSRWSGSQQVEQP----TGSVLWMAPEVIRmQDDNPFSFQS----DVYSYGIVLYELmagelpyahinNRDQIIFMVG 481
Cdd:cd14219   158 V--KFISDTNEVDIPpntrVGTKRYMPPEVLD-ESLNRNHFQSyimaDMYSFGLILWEV-----------ARRCVSGGIV 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 482 RGYASPdLSRLYKNCP--KAMKRLVadCVKKVkeeRPLFPQILSSIELLQH 530
Cdd:cd14219   224 EEYQLP-YHDLVPSDPsyEDMREIV--CIKRL---RPSFPNRWSSDECLRQ 268
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
274-467 2.46e-18

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 84.74  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwH---GD-VAVKILKVVDPTPEqLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSL 348
Cdd:cd14078    11 IGSGGFAKVKLAT-HiltGEkVAIKIMDKKALGDD-LPRVKTEIEALKNLSHQHICrLYHVIETDNKIFMVLEYCPGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHL----HVQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSQQVEQP 424
Cdd:cd14078    89 FDYIvakdRLSEDEARVF-----FRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCA-KPKGGMDHHLETC 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 425 TGSVLWMAPEVIrmQDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14078   163 CGSPAYAAPELI--QGKPYIGSEADVWSMGVLLYALLCGFLPF 203
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
274-531 2.55e-18

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 85.01  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKvvdPTPEQLQAFRNEVAVLR------KTRHVNILLFMGY-MTKDNLAIVTQWC 343
Cdd:cd14133     7 LGKGTFGQVVKCydlLTGEEVALKIIK---NNKDYLDQSLDEIRLLEllnkkdKADKYHIVRLKDVfYFKNHLCIVFELL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 eGSSLYKHLhvQETKFQMFQLI---DIARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGlatvkSRWSGS 418
Cdd:cd14133    84 -SQNLYEFL--KQNKFQYLSLPrirKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFG-----SSCFLT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVG-RGYASPdlsRLYKNCP 497
Cdd:cd14133   156 QRLYSYIQSRYYRAPEVIL---GLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGtIGIPPA---HMLDQGK 229
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 498 KAMKRLVaDCVKKVKEERPLfpQILSSIELLQHS 531
Cdd:cd14133   230 ADDELFV-DFLKKLLEIDPK--ERPTASQALSHP 260
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
274-467 2.88e-18

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 85.54  E-value: 2.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV------YKGKWHgdvAVKILKVVdPTPEQLQAFRnEVAVLRKTR-HVNILLFMGYMTKDN-LAIVTQWCEG 345
Cdd:cd14090    10 LGEGAYASVqtcinlYTGKEY---AVKIIEKH-PGHSRSRVFR-EVETLHQCQgHPNILQLIEYFEDDErFYLVFEKMRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIF---LHEGLTVKIGDFGLA------TVKSRWS 416
Cdd:cd14090    85 GPLLSHIEKRVH-FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGsgiklsSTSMTPV 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 417 GSQQVEQPTGSVLWMAPEVIrmqddNPFSFQS-------DVYSYGIVLYELMAGELPY 467
Cdd:cd14090   164 TTPELLTPVGSAEYMAPEVV-----DAFVGEAlsydkrcDLWSLGVILYIMLCGYPPF 216
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
273-532 3.17e-18

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 85.15  E-value: 3.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYK--GKWHGDV-AVKILK--VVDPTPEQlQAFrNEV---AVLRKTRHVnILLFMGYMTKDNLAIVTQWCE 344
Cdd:cd14051     7 KIGSGEFGSVYKciNRLDGCVyAIKKSKkpVAGSVDEQ-NAL-NEVyahAVLGKHPHV-VRYYSAWAEDDHMIIQNEYCN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSL-------YKHLHVqetkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIF----------------------- 394
Cdd:cd14051    84 GGSLadaisenEKAGER----FSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFisrtpnpvsseeeeedfegeedn 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 395 -LHEGLTVKIGDFGLATVKSrwsgSQQVEQptGSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGE-LPyahiNN 472
Cdd:cd14051   160 pESNEVTYKIGDLGHVTSIS----NPQVEE--GDCRFLANEI--LQENYSHLPKADIFALALTVYEAAGGGpLP----KN 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 473 RDQiIFMVGRGYAsPDLSrlykNCPKAMKRLVADCVKKVKEERPlfpqilSSIELLQHSL 532
Cdd:cd14051   228 GDE-WHEIRQGNL-PPLP----QCSPEFNELLRSMIHPDPEKRP------SAAALLQHPV 275
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
274-495 4.56e-18

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 85.41  E-value: 4.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKIL--KVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDgkfYAVKVLqkKTILKKKEQNHIMAERNVLLKNLKHPFLVgLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksrwSGSQQVEQPT-- 425
Cdd:cd05603    83 LFFHLQ-RERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCK-----EGMEPEETTStf 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 426 -GSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPyahinnrdqiifmvgrgYASPDLSRLYKN 495
Cdd:cd05603   157 cGTPEYLAPEVLRKE---PYDRTVDWWCLGAVLYEMLYGLPP-----------------FYSRDVSQMYDN 207
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
261-467 5.20e-18

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 83.85  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVmlSTRIGSGSFGTVYKGKWHGDVAVKILKVVdpTPEQLQ------AFRNEVAVLRKTRHVNILLFMGYM-TK 333
Cdd:cd14116     2 WALEDFEI--GRPLGKGKFGNVYLAREKQSKFILALKVL--FKAQLEkagvehQLRREVEIQSHLRHPNILRLYGYFhDA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DNLAIVTQWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvks 413
Cdd:cd14116    78 TRVYLILEYAPLGTVYRELQ-KLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG------ 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 414 rWSgsqqVEQPT-------GSVLWMAPEVI--RMQDDnpfsfQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14116   151 -WS----VHAPSsrrttlcGTLDYLPPEMIegRMHDE-----KVDLWSLGVLCYEFLVGKPPF 203
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
274-478 5.43e-18

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 83.81  E-value: 5.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK---VVDP-TPEQLQafrNEVAVLRKTRHVNILLFMGYMtKDNLAI--VTQWCE 344
Cdd:cd05572     1 LGVGGFGRVELVQLKSKgrtFALKCVKkrhIVQTrQQEHIF---SEKEILEECNSPFIVKLYRTF-KDKKYLymLMEYCL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHV------QETKFQMFQLIDIarqtaqgMDYLHAKNIIHRDMKSNNIFL-HEGLtVKIGDFGLAtvKSRWSG 417
Cdd:cd05572    77 GGELWTILRDrglfdeYTARFYTACVVLA-------FEYLHSRGIIYRDLKPENLLLdSNGY-VKLVDFGFA--KKLGSG 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 418 sqqveQPT----GSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIF 478
Cdd:cd05572   147 -----RKTwtfcGTPEYVAPEIILNKG---YDFSVDYWSLGILLYELLTGRPPFGGDDEDPMKIY 203
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
274-480 5.53e-18

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 84.18  E-value: 5.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-----VAVKILKVVDPTPEQLQaFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSS 347
Cdd:cd05042     3 IGNGWFGKVLLGEIYSGtsvaqVVVKELKASANPKEQDT-FLKEGQPYRILQHPNILQCLGQCVEAIpYLLVMEFCDLGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQM----FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd05042    82 LKAYLRSEREHERGdsdtRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKEDYIETDDK 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 424 PTGSVLWMAPEVIRMQDDNPF----SFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMV 480
Cdd:cd05042   162 LWFPLRWTAPELVTEFHDRLLvvdqTKYSNIWSLGVTLWELFEnGAQPYSNLSDLDVLAQVV 223
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
274-467 5.73e-18

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 84.04  E-value: 5.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRN-------------EVAVLRKTRHVNIL-LFMGYMTKDNL 336
Cdd:cd14077     9 IGAGSMGKVKLAKHIRTgekCAIKIIPRASNAGLKKEREKRlekeisrdirtirEAALSSLLNHPHICrLRDFLRTPNHY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRws 416
Cdd:cd14077    89 YMLFEYVDGGQLLDYI-ISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNLYDP-- 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 417 gSQQVEQPTGSVLWMAPEVIRMQddnPFSF-QSDVYSYGIVLYELMAGELPY 467
Cdd:cd14077   166 -RRLLRTFCGSLYFAAPELLQAQ---PYTGpEVDVWSFGVVLYVLVCGKVPF 213
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
274-521 7.18e-18

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 84.76  E-value: 7.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY-----KGKWHGDV-AVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05582     3 LGQGSFGKVFlvrkiTGPDAGTLyAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVkLHYAFQTEGKLYLILDFLRGG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLhvqeTKFQMFQLIDIA---RQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQ 423
Cdd:cd05582    83 DLFTRL----SKEVMFTEEDVKfylAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLS--KESIDHEKKAYS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGSVLWMAPEVIRMQDDnpfSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGR------GYASPD----LSRLY 493
Cdd:cd05582   157 FCGTVEYMAPEVVNRRGH---TQSADWWSFGVLMFEMLTGSLPF-QGKDRKETMTMILKaklgmpQFLSPEaqslLRALF 232
                         250       260
                  ....*....|....*....|....*...
gi 1720416759 494 KNCPKAMKRLVADCVKKVKEErPLFPQI 521
Cdd:cd05582   233 KRNPANRLGAGPDGVEEIKRH-PFFATI 259
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
290-479 7.95e-18

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 83.81  E-value: 7.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 290 DVAVKILKVVD---PTPEQLQAFRN----EVAVLRKTR-HVNIL-LFMGYMTKDNLAIVTQWCEGSSLYKHLHVQ----- 355
Cdd:cd14182    30 EYAVKIIDITGggsFSPEEVQELREatlkEIDILRKVSgHPNIIqLKDTYETNTFFFLVFDLMKKGELFDYLTEKvtlse 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 356 -ETKFQMFQLIDIarqtaqgMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQPTGSVLWMAPE 434
Cdd:cd14182   110 kETRKIMRALLEV-------ICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSC---QLDPGEKLREVCGTPGYLAPE 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720416759 435 VIR--MQDDNP-FSFQSDVYSYGIVLYELMAGELPYAHinnRDQIIFM 479
Cdd:cd14182   180 IIEcsMDDNHPgYGKEVDMWSTGVIMYTLLAGSPPFWH---RKQMLML 224
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
261-467 9.59e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 84.48  E-value: 9.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIeaSEVMLSTRIGSGSFGTVY--KGKWHGD-VAVKILKVVDPTP-EQLQAFRNEVAVLRKTRHVNILLFM-GYMTKDN 335
Cdd:PTZ00263   15 WKL--SDFEMGETLGTGSFGRVRiaKHKGTGEyYAIKCLKKREILKmKQVQHVAQEKSILMELSHPFIVNMMcSFQDENR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQWCEGSSLYKHLHvQETKFQMfqliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtv 411
Cdd:PTZ00263   93 VYFLLEFVVGGELFTHLR-KAGRFPN----DVAKfyhaELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFA-- 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 412 ksrwsgsQQVEQPT----GSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPY 467
Cdd:PTZ00263  166 -------KKVPDRTftlcGTPEYLAPEVIQSKGHGK---AVDWWTMGVLLYEFIAGYPPF 215
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
265-467 1.00e-17

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 83.05  E-value: 1.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 265 ASEVMLSTR--IGSGSFGTVYK--GKWHG-DVAVKILKvvDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAI 338
Cdd:cd14190     1 SSTFSIHSKevLGGGKFGKVHTctEKRTGlKLAAKVIN--KQNSKDKEMVLLEIQVMNQLNHRNLIqLYEAIETPNEIVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSSLYKHL-----HVQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLAtv 411
Cdd:cd14190    79 FMEYVEGGELFERIvdedyHLTEVDAMVF-----VRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLA-- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 412 kSRWSGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14190   152 -RRYNPREKLKVNFGTPEFLSPEVVNYDQ---VSFPTDMWSMGVITYMLLSGLSPF 203
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
274-467 1.00e-17

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 84.66  E-value: 1.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK---VVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05615    18 LGKGSFGKVMLAERKGSdelYAIKILKkdvVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS 427
Cdd:cd05615    98 LMYHIQ-QVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMC--KEHMVEGVTTRTFCGT 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05615   175 PDYIAPEIIAYQ---PYGRSVDWWAYGVLLYEMLAGQPPF 211
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
269-463 1.11e-17

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 84.13  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 269 MLSTrIGSGSFGTVYKG---KWHGDVAVKILKVVDPTpeQLQAfRNEVAVLRKTRH------VNILLFMGYMT-KDNLAI 338
Cdd:cd14210    17 VLSV-LGKGSFGQVVKCldhKTGQLVAIKIIRNKKRF--HQQA-LVEVKILKHLNDndpddkHNIVRYKDSFIfRGHLCI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTqwcE--GSSLYKHLhvQETKFQMFQLI---DIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT--VKIGDFGlatv 411
Cdd:cd14210    93 VF---EllSINLYELL--KSNNFQGLSLSlirKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFG---- 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 412 KSRWSGsQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAG 463
Cdd:cd14210   164 SSCFEG-EKVYTYIQSRFYRAPEVIL---GLPYDTAIDMWSLGCILAELYTG 211
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
274-477 1.41e-17

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 83.80  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV----YKGKwhGDV-AVKILK---VVDPtpEQLQAFRNEVAVLRKTRHVNIL--LFMGYMTKDNLAIVTQWC 343
Cdd:cd05570     3 LGKGSFGKVmlaeRKKT--DELyAIKVLKkevIIED--DDVECTMTEKRVLALANRHPFLtgLHACFQTEDRLYFVMEYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGlTVKIGDFGLAtvKSRWSGSQQVE 422
Cdd:cd05570    79 NGGDLMFHIQ-RARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLdAEG-HIKIADFGMC--KEGIWGGNTTS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 423 QPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYaHINNRDQII 477
Cdd:cd05570   155 TFCGTPDYIAPEILREQD---YGFSVDWWALGVLLYEMLAGQSPF-EGDDEDELF 205
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
273-480 1.59e-17

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 83.59  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEG--- 345
Cdd:cd07869    12 KLGEGSYATVYKGKSKVNgklVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIhTKETLTLVFEYVHTdlc 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKH---LHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVE 422
Cdd:cd07869    91 QYMDKHpggLHPENVKLFLFQLL-------RGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNE 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 423 QPTgsvLWMAPEVIrMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINN-RDQI--IFMV 480
Cdd:cd07869   164 VVT---LWYRPPDV-LLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiQDQLerIFLV 220
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
269-476 1.70e-17

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 82.99  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 269 MLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd14104     3 MIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILrLHESFESHEELVMIFEFISGVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI--FLHEGLTVKIGDFGLAtvkSRWSGSQQVEQPT 425
Cdd:cd14104    83 IFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIiyCTRRGSYIKIIEFGQS---RQLKPGDKFRLQY 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 426 GSVLWMAPEVirmQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI 476
Cdd:cd14104   160 TSAEFYAPEV---HQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTI 207
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
274-467 1.93e-17

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 82.31  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG--DVAVKILKVVDPTPEQ-LQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLY 349
Cdd:cd14161    11 LGKGTYGRVKKARDSSgrLVAIKSIRKDRIKDEQdLLHIRREIEIMSSLNHPHIIsVYEVFENSSKIVIVMEYASRGDLY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHL----HVQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrWSGSQQVEQPT 425
Cdd:cd14161    91 DYIserqRLSELEARHF-----FRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNL---YNQDKFLQTYC 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 426 GSVLWMAPEVIrmqDDNPFSF-QSDVYSYGIVLYELMAGELPY 467
Cdd:cd14161   163 GSPLYASPEIV---NGRPYIGpEVDSWSLGVLLYILVHGTMPF 202
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
273-480 1.98e-17

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 83.13  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGK---WHGDVAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEgSSL 348
Cdd:cd07873     9 KLGEGTYATVYKGRsklTDNLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIIhTEKSLTLVFEYLD-KDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHL-------HVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQV 421
Cdd:cd07873    87 KQYLddcgnsiNMHNVKLFLFQLL-------RGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSN 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 422 EQPTgsvLWMAPEVIRMQDDNpFSFQSDVYSYGIVLYELMAGE--LPYAHINNRDQIIFMV 480
Cdd:cd07873   160 EVVT---LWYRPPDILLGSTD-YSTQIDMWGVGCIFYEMSTGRplFPGSTVEEQLHFIFRI 216
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
275-525 2.34e-17

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 82.14  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 275 GSGSFGTVYKGKWH--GDVAVK----ILKVVDPTPEQL-QAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05037     8 GQGTFTNIYDGILRevGDGRVQevevLLKVLDSDHRDIsESFFETASLMSQISHKHLVKLYGVCVADENIMVQEYVRYGP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGLT-----VKIGDFGLATvksrwsGSQQV 421
Cdd:cd05037    88 LDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLaREGLDgyppfIKLSDPGVPI------TVLSR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGSVLWMAPEVIRMQDDNPfSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGRG-YASPDLSRLYKncpka 499
Cdd:cd05037   162 EERVDRIPWIAPECLRNLQANL-TIAADKWSFGTTLWEICSgGEEPLSALSSQEKLQFYEDQHqLPAPDCAELAE----- 235
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 500 mkrLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd05037   236 ---LIMQCWTYEPTKRPSFRAILRDL 258
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
273-478 2.59e-17

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 82.75  E-value: 2.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG--KWHGD-VAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEgSSL 348
Cdd:cd07871    12 KLGEGTYATVFKGrsKLTENlVALKEIRLEHEEGAPCTAIR-EVSLLKNLKHANIVTLHDIIhTERCLTLVFEYLD-SDL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLH-------VQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQV 421
Cdd:cd07871    90 KQYLDncgnlmsMHNVKIFMFQLL-------RGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSN 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 422 EQPTgsvLWMAPEVIrMQDDNPFSFQSDVYSYGIVLYELMAGE--LPYAHINNRDQIIF 478
Cdd:cd07871   163 EVVT---LWYRPPDV-LLGSTEYSTPIDMWGVGCILYEMATGRpmFPGSTVKEELHLIF 217
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
274-480 2.66e-17

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 82.31  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD-----VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSS 347
Cdd:cd14206     5 IGNGWFGKVILGEIFSDytpaqVVVKELRV-SAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETiPFLLIMEFCQLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQM---------FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGS 418
Cdd:cd14206    84 LKRYLRAQRKADGMtpdlptrdlRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNNYKEDYY 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRMQDDNPF----SFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMV 480
Cdd:cd14206   164 LTPDRLWIPLRWVAPELLDELHGNLIvvdqSKESNVWSLGVTIWELFEfGAQPYRHLSDEEVLTFVV 230
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
274-526 2.94e-17

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 82.24  E-value: 2.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-DVAVKILKVVDPTpeQLQA----FRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSS 347
Cdd:cd14160     1 IGEGEIFEVYRVRIGNrSYAVKLFKQEKKM--QWKKhwkrFLSELEVLLLFQHPNILELAAYFTEtEKFCLVYPYMQNGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLH-VQETKFQMFQL-IDIARQTAQGMDYLHAKN---IIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVE 422
Cdd:cd14160    79 LFDRLQcHGVTKPLSWHErINILIGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFALAHFRPHLEDQSCTI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTGSV---LWMAPE-VIRmqdDNPFSFQSDVYSYGIVLYELMAG-----ELPyAHINNRDQII-FMVGRGYAS--PDLS 490
Cdd:cd14160   159 NMTTALhkhLWYMPEeYIR---QGKLSVKTDVYSFGIVIMEVLTGckvvlDDP-KHLQLRDLLHeLMEKRGLDSclSFLD 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1720416759 491 RLYKNCPKAMK----RLVADCVKKVKEERPLFPQILSSIE 526
Cdd:cd14160   235 LKFPPCPRNFSaklfRLAGRCTATKAKLRPDMDEVLQRLE 274
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
274-495 2.98e-17

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 82.45  E-value: 2.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGD-VAVKIL---KVVdpTPEQLQAFRNEVAVLRKTRHVNiLLFMGYMTKDN--LAIVTQWCEG 345
Cdd:cd14209     9 LGTGSFGRVMlvRHKETGNyYAMKILdkqKVV--KLKQVEHTLNEKRILQAINFPF-LVKLEYSFKDNsnLYMVMEYVPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT-VKSR-WSgsqqveq 423
Cdd:cd14209    86 GEMFSHLR-RIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKrVKGRtWT------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHinnrDQIIFMVGR---------GYASPDLSRLYK 494
Cdd:cd14209   158 LCGTPEYLAPEIILSK---GYNKAVDWWALGVLIYEMAAGYPPFFA----DQPIQIYEKivsgkvrfpSHFSSDLKDLLR 230

                  .
gi 1720416759 495 N 495
Cdd:cd14209   231 N 231
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
261-527 3.05e-17

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 82.35  E-value: 3.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEieasEVMLSTRIGSGSFGTVYKGKWHGD-----VAVKILKVVDPTPEQlQAFRNEVAVLRKT-RHVNILLFMGYM-TK 333
Cdd:cd05089     1 WE----DIKFEDVIGEGNFGQVIKAMIKKDglkmnAAIKMLKEFASENDH-RDFAGELEVLCKLgHHPNIINLLGACeNR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 DNLAIVTQWCEGSSLYKHL---------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG 398
Cdd:cd05089    76 GYLYIAIEYAPYGNLLDFLrksrvletdpafakeHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGEN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 399 LTVKIGDFGLATVKSRWSGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQII 477
Cdd:cd05089   156 LVSKIADFGLSRGEEVYVKKTMGRLP---VRWMAIESLNY---SVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCA-ELY 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 478 FMVGRGY--ASPdlsrlyKNCPKAMKRLVADCVKKVKEERPLFPQIlsSIEL 527
Cdd:cd05089   229 EKLPQGYrmEKP------RNCDDEVYELMRQCWRDRPYERPPFSQI--SVQL 272
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
273-478 4.66e-17

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 81.26  E-value: 4.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKIL--KVVDPTPEQLQafrNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd14083    10 VLGTGAFSEVVLAEDKATgklVAIKCIdkKALKGKEDSLE---NEIAVLRKIKHPNIVqLLDIYESKSHLYLVMELVTGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLTVKIGDFGLatvkSRWSGSQQVEQ 423
Cdd:cd14083    87 ELFDRI-VEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYspdEDSKIMISDFGL----SKMEDSGVMST 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 424 PTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHINnrDQIIF 478
Cdd:cd14083   162 ACGTPGYVAPEVLAQK---PYGKAVDCWSIGVISYILLCGYPPFYDEN--DSKLF 211
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
274-480 4.89e-17

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 81.57  E-value: 4.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG-----DVAVKILKVVDPTPEQLQaFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSS 347
Cdd:cd05087     5 IGHGWFGKVFLGEVNSglsstQVVVKELKASASVQDQMQ-FLEEAQPYRALQHTNLLQCLAQCAEvTPYLLVMEFCPLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQM----FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd05087    84 LKGYLRSCRAAESMapdpLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFVTADQ 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 424 PTGSVLWMAPEVIRMQDDNPF----SFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMV 480
Cdd:cd05087   164 LWVPLRWIAPELVDEVHGNLLvvdqTKQSNVWSLGVTIWELFElGNQPYRHYSDRQVLTYTV 225
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
269-467 5.53e-17

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 81.02  E-value: 5.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 269 MLSTRIGSGSFGTVYKGkWHGDVAVKI-LKVVDPTPEQLQAF-----RNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQ 341
Cdd:cd14070     5 LIGRKLGEGSFAKVREG-LHAVTGEKVaIKVIDKKKAKKDSYvtknlRREGRIQQMIRHPNITQLLDILETENsYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSG 417
Cdd:cd14070    84 LCPGGNLMHRIYdkkrLEEREARRY-----IRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGY 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14070   159 SDPFSTQCGSPAYAAPELLARKKYGP---KVDVWSIGVNMYAMLTGTLPF 205
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
273-481 5.56e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 82.03  E-value: 5.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKwhgD------VAVKIL---KVVDPTPeqLQAFRnEVAVLRKTRHVNILLFMGYMTK---DNLAIVT 340
Cdd:cd07845    14 RIGEGTYGIVYRAR---DttsgeiVALKKVrmdNERDGIP--ISSLR-EITLLLNLRHPNIVELKEVVVGkhlDSIFLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEgSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvkSRWSGSQQ 420
Cdd:cd07845    88 EYCE-QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA---RTYGLPAK 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 421 VEQPTGSVLWM-APEVIRMQDDNPFSFqsDVYSYGIVLYELMAGE--LPYA-HINNRDQIIFMVG 481
Cdd:cd07845   164 PMTPKVVTLWYrAPELLLGCTTYTTAI--DMWAVGCILAELLAHKplLPGKsEIEQLDLIIQLLG 226
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
274-521 6.73e-17

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 80.99  E-value: 6.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGD-VAVKILKVVD-PTPEQLQAFRNEVAVLRKTRHVNIL--LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05611     4 ISKGAFGSVYlaKKRSTGDyFAIKVLKKSDmIAKNQVTNVKAERAIMMIQGESPYVakLYYSFQSKDYLYLVMEYLNGGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LykhlhvqETKFQMFQLI--DIARQ----TAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrwsGSQQV 421
Cdd:cd05611    84 C-------ASLIKTLGGLpeDWAKQyiaeVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRN-----GLEKR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQP--TGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYaHINNRDQIIFMVGRG----------YASP-- 487
Cdd:cd05611   152 HNKkfVGTPDYLAPETILGVGDDK---MSDWWSLGCVIFEFLFGYPPF-HAETPDAVFDNILSRrinwpeevkeFCSPea 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720416759 488 -DL-SRLYknCPKAMKRLVADCVKKVKEErPLFPQI 521
Cdd:cd05611   228 vDLiNRLL--CMDPAKRLGANGYQEIKSH-PFFKSI 260
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
266-467 7.94e-17

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 81.89  E-value: 7.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 266 SEVMLSTRIGSGSFGTVYKGKWHGD---VAVKILKV-VDPTPEQLQAFRNEVAVLRKTRHVNIL--LFMGYMTKDNLAIV 339
Cdd:cd05619     5 EDFVLHKMLGKGSFGKVFLAELKGTnqfFAIKALKKdVVLMDDDVECTMVEKRVLSLAWEHPFLthLFCTFQTKENLFFV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYkhLHVQET-KFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGS 418
Cdd:cd05619    85 MEYLNGGDLM--FHIQSChKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC--KENMLGD 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05619   161 AKTSTFCGTPDYIAPEILLGQK---YNTSVDWWSFGVLLYEMLIGQSPF 206
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
311-467 8.81e-17

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 80.86  E-value: 8.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 311 NEVAVLRK--TRHVnILLFMGYMTKDNLAIVTQWCEGSSLYKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRD 387
Cdd:cd05605    49 NEKQILEKvnSRFV-VSLAYAYETKDALCLVLTIMNGGDLKFHIYnMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 388 MKSNNIFLHEGLTVKIGDFGLA-------TVKSRwsgsqqveqpTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYEL 460
Cdd:cd05605   128 LKPENILLDDHGHVRISDLGLAveipegeTIRGR----------VGTVGYMAPEVV---KNERYTFSPDWWGLGCLIYEM 194

                  ....*..
gi 1720416759 461 MAGELPY 467
Cdd:cd05605   195 IEGQAPF 201
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
271-468 1.15e-16

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 80.09  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGSFGTVYK------GKwhgDVAVKILKVVDPTPEQLQAFRNEVAVLR----KTRHVNilLFMGYMTKDNLAIVT 340
Cdd:cd14106    13 STPLGRGKFAVVRKcihketGK---EYAAKFLRKRRRGQDCRNEILHEIAVLElckdCPRVVN--LHEVYETRSELILIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-----HEGLtvKIGDFGLATVKSRw 415
Cdd:cd14106    88 ELAAGGELQTLL-DEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtsefpLGDI--KLCDFGISRVIGE- 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 416 sgSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYA 468
Cdd:cd14106   164 --GEEIREILGTPDYVAPEILSYE---PISLATDMWSIGVLTYVLLTGHSPFG 211
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
274-467 1.16e-16

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 81.61  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV--YKGKWHGDV-AVKILKvvdptpEQLQAFRNEVA-------VLRKTRHVNIL-LFMGYMTKDNLAIVTQW 342
Cdd:cd05594    33 LGKGTFGKVilVKEKATGRYyAMKILK------KEVIVAKDEVAhtltenrVLQNSRHPFLTaLKYSFQTHDRLCFVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHA-KNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQV 421
Cdd:cd05594   107 ANGGELFFHLS-RERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLC--KEGIKDGATM 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759 422 EQPTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05594   184 KTFCGTPEYLAPEVL---EDNDYGRAVDWWGLGVVMYEMMCGRLPF 226
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
273-463 1.21e-16

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 80.50  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQ---LQAFRnEVAVLRKTRHVNIL-------------LFMGYMTKDnL 336
Cdd:cd07844     7 KLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEgapFTAIR-EASLLKDLKHANIVtlhdiihtkktltLVFEYLDTD-L 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSslykhLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWS 416
Cdd:cd07844    85 KQYMDDCGGG-----LSMHNVRLFLFQLL-------RGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPS 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 417 GSQQVEQPTgsvLWMAPEVIRMQDDNpFSFQSDVYSYGIVLYELMAG 463
Cdd:cd07844   153 KTYSNEVVT---LWYRPPDVLLGSTE-YSTSLDMWGVGCIFYEMATG 195
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
274-523 1.26e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 80.39  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV-YKGKWHGD-VAVKILKV----------VDPTPEQLQA---------FRNEVAVLRKTRHVNILLFMGyMT 332
Cdd:cd14067     1 LGQGGSGTViYRARYQGQpVAVKRFHIkkckkrtdgsADTMLKHLRAadamknfseFRQEASMLHSLQHPCIVYLIG-IS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 333 KDNLAIVTQWCEGSSLYKHLHVQETKFQMFQL-----IDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-----HEGLTVK 402
Cdd:cd14067    80 IHPLCFALELAPLGSLNTVLEENHKGSSFMPLghmltFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQEHINIK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 403 IGDFGLatvkSRWSGSQQVEQPTGSVLWMAPEV-IRMQDDNpfsfQSDVYSYGIVLYELMAGELPyAHINNRDQIIFMVG 481
Cdd:cd14067   160 LSDYGI----SRQSFHEGALGVEGTPGYQAPEIrPRIVYDE----KVDMFSYGMVLYELLSGQRP-SLGHHQLQIAKKLS 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759 482 RG----YASPDLSRLYKncpkaMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd14067   231 KGirpvLGQPEEVQFFR-----LQALMMECWDTKPEKRPLACSVVE 271
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
260-525 1.54e-16

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 80.43  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 260 YWEIEASEVMLSTRIGSGSFGTVYKGK-----WHGDVAVKILKVVdPTPEQLQAFRNEVAVL-RKTRHVNILLFMGYMT- 332
Cdd:cd05088     1 YPVLEWNDIKFQDVIGEGNFGQVLKARikkdgLRMDAAIKRMKEY-ASKDDHRDFAGELEVLcKLGHHPNIINLLGACEh 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 333 KDNLAIVTQWCEGSSLYKHL---------------HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE 397
Cdd:cd05088    80 RGYLYLAIEYAPHGNLLDFLrksrvletdpafaiaNSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 398 GLTVKIGDFGLATVKSRWSGSQQVEQPtgsVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRdQI 476
Cdd:cd05088   160 NYVAKIADFGLSRGQEVYVKKTMGRLP---VRWMAIESLNY---SVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCA-EL 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 477 IFMVGRGYaspdlsRLYK--NCPKAMKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd05088   233 YEKLPQGY------RLEKplNCDDEVYDLMRQCWREKPYERPSFAQILVSL 277
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
270-516 1.58e-16

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 80.46  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKW---HGDVAVKILKVVDPTPEQLQA-FRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCE 344
Cdd:cd08229    28 IEKKIGRGQFSEVYRATClldGVPVALKKVQIFDLMDAKARAdCIKEIDLLKQLNHPNVIKYYASFIEDNeLNIVLELAD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 G---SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwSGSQQV 421
Cdd:cd08229   108 AgdlSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFS--SKTTAA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELP-YAHINNRDQIIFMVGRGYASPDLSRLYKncpKAM 500
Cdd:cd08229   186 HSLVGTPYYMSPERIH---ENGYNFKSDIWSLGCLLYEMAALQSPfYGDKMNLYSLCKKIEQCDYPPLPSDHYS---EEL 259
                         250
                  ....*....|....*.
gi 1720416759 501 KRLVADCVKKVKEERP 516
Cdd:cd08229   260 RQLVNMCINPDPEKRP 275
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
274-478 1.78e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 80.06  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLQA-----FRNEVAVLRKTRHVNILLFMGYMTKDNLAIVT--QWC 343
Cdd:cd13990     8 LGKGGFSEVYKAfdlVEQRYVACKIHQLNKDWSEEKKQnyikhALREYEIHKSLDHPRIVKLYDVFEIDTDSFCTvlEYC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHVQETkFQMFQLIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLT---VKIGDFGLATV----KSR 414
Cdd:cd13990    88 DGNDLDFYLKQHKS-IPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITDFGLSKImddeSYN 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVIRMQDDNP-FSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIF 478
Cdd:cd13990   167 SDGMELTSQGAGTYWYLPPECFVVGKTPPkISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILE 231
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
274-472 2.05e-16

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 79.30  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY---KGKWHGDVAVKIL--KVVDPTPEQLQafrNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSS 347
Cdd:cd14167    11 LGTGAFSEVVlaeEKRTQKLVAIKCIakKALEGKETSIE---NEIAVLHKIKHPNIVALDDiYESGGHLYLIMQLVSGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIF---LHEGLTVKIGDFGLATVKSrwSGSqQVEQP 424
Cdd:cd14167    88 LFDRI-VEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEG--SGS-VMSTA 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720416759 425 TGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHINN 472
Cdd:cd14167   164 CGTPGYVAPEVLAQK---PYSKAVDCWSIGVIAYILLCGYPPFYDEND 208
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
297-474 2.23e-16

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 79.19  E-value: 2.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 297 KVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGM 375
Cdd:cd14110    34 KIIPYKPEDKQLVLREYQVLRRLSHPRIAqLHSAYLSPRHLVLIEELCSGPELLYNL-AERNSYSEAEVTDYLWQILSAV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 376 DYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksrwSGSQQVEQPTGS----VLWMAPEVIRMQDDNPfsfQSDVY 451
Cdd:cd14110   113 DYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQ-----PFNQGKVLMTDKkgdyVETMAPELLEGQGAGP---QTDIW 184
                         170       180
                  ....*....|....*....|...
gi 1720416759 452 SYGIVLYELMAGELPYAHINNRD 474
Cdd:cd14110   185 AIGVTAFIMLSADYPVSSDLNWE 207
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
274-545 2.24e-16

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 80.31  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK---WHGDVAVKilKVVDP--TPEQLQAFRNEVAVLRKTRHVNIL----LFMGYMtkDNLAIVTQwCE 344
Cdd:cd07856    18 VGMGAFGLVCSARdqlTGQNVAVK--KIMKPfsTPVLAKRTYRELKLLKHLRHENIIslsdIFISPL--EDIYFVTE-LL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQ--ETKFQMFQLIDIARqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrwsgsqQVE 422
Cdd:cd07856    93 GTDLHRLLTSRplEKQFIQYFLYQILR----GLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI--------QDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTGSV---LWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYA---HINNRDQIIFMVG-------RGYASPDL 489
Cdd:cd07856   161 QMTGYVstrYYRAPEI--MLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPgkdHVNQFSIITELLGtppddviNTICSENT 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 490 SRLYKNCPKAMKRLVADCVKKVKeerplfPQILSSIELLQHSLPKINRSASEPSLH 545
Cdd:cd07856   239 LRFVQSLPKRERVPFSEKFKNAD------PDAIDLLEKMLVFDPKKRISAAEALAH 288
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
312-474 2.33e-16

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 79.75  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 312 EVAVLRKTRHVNILLFMGYMTKDN--LAIVTQWCE---GSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLH-AKNIIH 385
Cdd:cd14001    55 EAKILKSLNHPNIVGFRAFTKSEDgsLCLAMEYGGkslNDLIEERYEAGLGPFPAATILKVALSIARALEYLHnEKKILH 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 386 RDMKSNNIFLHEGL-TVKIGDFGlatVKSRWSGSQQV-EQPT----GSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYE 459
Cdd:cd14001   135 GDIKSGNVLIKGDFeSVKLCDFG---VSLPLTENLEVdSDPKaqyvGTEPWKAKEA--LEEGGVITDKADIFAYGLVLWE 209
                         170
                  ....*....|....*
gi 1720416759 460 LMAGELPYAHINNRD 474
Cdd:cd14001   210 MMTLSVPHLNLLDIE 224
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
274-535 2.73e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 79.36  E-value: 2.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKwhgDVAVKILKVVDPTPE---QLQAFRNEVAVLRKTRHVNILLFMGYM---TKDNLAIVTQ 341
Cdd:cd06651    15 LGQGAFGRVYlcydvdTGR---ELAAKQVQFDPESPEtskEVSALECEIQLLKNLQHERIVQYYGCLrdrAEKTLTIFME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG----LATVKS 413
Cdd:cd06651    92 YMPGGSVKDQLKaygaLTESVTRKY-----TRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTICM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RWSGSQQVeqpTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRdQIIFMVGRGYASPDLsrly 493
Cdd:cd06651   167 SGTGIRSV---TGTPYWMSPEVISGEG---YGRKADVWSLGCTVVEMLTEKPPWAEYEAM-AAIFKIATQPTNPQL---- 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 494 kncPKAMKRLVADCVKKVKEERPLFPqilSSIELLQHSLPKI 535
Cdd:cd06651   236 ---PSHISEHARDFLGCIFVEARHRP---SAEELLRHPFAQL 271
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
274-467 3.28e-16

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 79.27  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTP-EQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLYKH 351
Cdd:cd14166    11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPlSRDSSLENEIAVLKRIKHENIVTLEDiYESTTHYYLVMQLVSGGELFDR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLatvkSRWSGSQQVEQPTGSV 428
Cdd:cd14166    91 I-LERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGL----SKMEQNGIMSTACGTP 165
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720416759 429 LWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14166   166 GYVAPEVLAQK---PYSKAVDCWSIGVITYILLCGYPPF 201
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
271-516 3.76e-16

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 78.81  E-value: 3.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 271 STRIGSGSFGTVYK--GKWHGDV-AVKILKVVDPTPEQLQAFRNEVAVLRKT----RHVNilLFMGYMTKDNLAIVTQWC 343
Cdd:cd14198    13 SKELGRGKFAVVRQciSKSTGQEyAAKFLKKRRRGQDCRAEILHEIAVLELAksnpRVVN--LHEVYETTSEIILILEYA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKH-LHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE----GlTVKIGDFGLAtvkSRWSGS 418
Cdd:cd14198    91 AGGEIFNLcVPDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiyplG-DIKIVDFGMS---RKIGHA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI--IFMVGRGYASPDLSRLYKNC 496
Cdd:cd14198   167 CELREIMGTPEYLAPEILNY---DPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFlnISQVNVDYSEETFSSVSQLA 243
                         250       260
                  ....*....|....*....|
gi 1720416759 497 PKAMKRLVAdcvkKVKEERP 516
Cdd:cd14198   244 TDFIQKLLV----KNPEKRP 259
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
274-522 3.76e-16

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 78.58  E-value: 3.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV----YKGKwHGDVAVK-ILK---VVD---------PTPEQLQAfrneVAVLRKTRHVNILLFMGYM-TKDN 335
Cdd:cd14004     8 MGEGAYGQVnlaiYKSK-GKEVVIKfIFKeriLVDtwvrdrklgTVPLEIHI----LDTLNKRSHPNIVKLLDFFeDDEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 LAIVTQwCEGSSLykhlhvqetkfQMFQLID------------IARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI 403
Cdd:cd14004    83 YYLVME-KHGSGM-----------DLFDFIErkpnmdekeakyIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 404 GDFGLATVKSRWSGSQQVeqptGSVLWMAPEVIRmqdDNPFSFQS-DVYSYGIVLYELMAGELPYAHInnrDQIIfmvgr 482
Cdd:cd14004   151 IDFGSAAYIKSGPFDTFV----GTIDYAAPEVLR---GNPYGGKEqDIWALGVLLYTLVFKENPFYNI---EEIL----- 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1720416759 483 gyaSPDLsRLYKNCPKAMKRLVADCVKKVKEERPLFPQIL 522
Cdd:cd14004   216 ---EADL-RIPYAVSEDLIDLISRMLNRDVGDRPTIEELL 251
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
274-466 4.09e-16

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 79.67  E-value: 4.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILkvvdptpeQLQAF--RNEVAVLRKTRHV---NIL------LFMGYMTKDNLAIV 339
Cdd:cd05575     3 IGKGSFGKVLLARHKAEgklYAVKVL--------QKKAIlkRNEVKHIMAERNVllkNVKhpflvgLHYSFQTKDKLYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHL----HVQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGlTVKIGDFGLAtvKSR 414
Cdd:cd05575    75 LDYVNGGELFFHLqrerHFPEPRARFY-----AAEIASALGYLHSLNIIYRDLKPENILLdSQG-HVVLTDFGLC--KEG 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGeLP 466
Cdd:cd05575   147 IEPSDTTSTFCGTPEYLAPEVLRKQ---PYDRTVDWWCLGAVLYEMLYG-LP 194
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
274-511 4.18e-16

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 78.27  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGT--VYKGKWHGD-VAVKILKVVDPTPEQLQafrNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLY 349
Cdd:cd14662     8 IGSGNFGVarLMRNKETKElVAVKYIERGLKIDENVQ---REIINHRSLRHPNIIRFKEvVLTPTHLAIVMEYAAGGELF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHL------HVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLT--VKIGDFGLAtvKSRWSGSQQv 421
Cdd:cd14662    85 ERIcnagrfSEDEARYFFQQLI-------SGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYS--KSSVLHSQP- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGSVLWMAPEVI-RMQDDNPFsfqSDVYSYGIVLYELMAGELPYAH----INNRDQIIFMVGRGYASPDLSRLYKNC 496
Cdd:cd14662   155 KSTVGTPAYIAPEVLsRKEYDGKV---ADVWSCGVTLYVMLVGAYPFEDpddpKNFRKTIQRIMSVQYKIPDYVRVSQDC 231
                         250
                  ....*....|....*.
gi 1720416759 497 PKAMKRL-VADCVKKV 511
Cdd:cd14662   232 RHLLSRIfVANPAKRI 247
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
310-530 4.32e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 80.83  E-value: 4.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 310 RNEVAVLRKTRHVNILL-FMGYMTKDNLAIVTQWCEGSSLYKHLHvQETK----FQMFQLIDIARQTAQGMDYLHAKNII 384
Cdd:PTZ00267  113 RSELHCLAACDHFGIVKhFDDFKSDDKLLLIMEYGSGGDLNKQIK-QRLKehlpFQEYEVGLLFYQIVLALDEVHSRKMM 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 385 HRDMKSNNIFLHEGLTVKIGDFGLAtvkSRWSGSQQVEQPT---GSVLWMAPEVirmQDDNPFSFQSDVYSYGIVLYELM 461
Cdd:PTZ00267  192 HRDLKSANIFLMPTGIIKLGDFGFS---KQYSDSVSLDVASsfcGTPYYLAPEL---WERKRYSKKADMWSLGVILYELL 265
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 462 AGELPYAHINNRdQIIFMVGRGYASPdlsrlyKNCP--KAMKRLVADCVKKVKEERPLFPQILSSiELLQH 530
Cdd:PTZ00267  266 TLHRPFKGPSQR-EIMQQVLYGKYDP------FPCPvsSGMKALLDPLLSKNPALRPTTQQLLHT-EFLKY 328
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
326-467 6.54e-16

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 78.41  E-value: 6.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 326 LFMGYMTKDNLAIVTQWCEGSSLYKHL-HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIG 404
Cdd:cd05607    67 LAYAFETKTHLCLVMSLMNGGDLKYHIyNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLS 146
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 405 DFGLATvksRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05607   147 DLGLAV---EVKEGKPITQRAGTNGYMAPEILK---EESYSYPVDWFAMGCSIYEMVAGRTPF 203
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
290-467 6.71e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 78.53  E-value: 6.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 290 DVAVKILKVvDPTPEQLQAFRnEVAVLRKTR-HVNILLFMGYMTK-DNLAIVTQWCEGSSLYKHLHvQETKFQMFQLIDI 367
Cdd:cd14173    29 EYAVKIIEK-RPGHSRSRVFR-EVEMLYQCQgHRNVLELIEFFEEeDKFYLVFEKMRGGSILSHIH-RRRHFNELEASVV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 368 ARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLAT---VKSRWS--GSQQVEQPTGSVLWMAPEVIRM- 438
Cdd:cd14173   106 VQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSgikLNSDCSpiSTPELLTPCGSAEYMAPEVVEAf 185
                         170       180       190
                  ....*....|....*....|....*....|
gi 1720416759 439 -QDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14173   186 nEEASIYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
270-504 8.37e-16

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 77.34  E-value: 8.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTV---YKGKWHGDVAVKILKVVDPTPEQLQAF-RNEVAVLRKTRHVNILLF--MGYMTKDNLAIVTQWC 343
Cdd:cd14163     4 LGKTIGEGTYSKVkeaFSKKHQRKVAIKIIDKSGGPEEFIQRFlPRELQIVERLDHKNIIHVyeMLESADGKIYLVMELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLhEGLTVKIGDFGLATVKSRwSGSQQVEQ 423
Cdd:cd14163    84 EDGDVFDCV-LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPK-GGRELSQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 424 PTGSVLWMAPEVIRMQDDNpfSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGYASPDLSRLYKNCPKAMKRL 503
Cdd:cd14163   161 FCGSTAYAAPEVLQGVPHD--SRKGDIWSMGVVLYVMLCAQLPFDD-TDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKRL 237

                  .
gi 1720416759 504 V 504
Cdd:cd14163   238 L 238
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
274-486 1.03e-15

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 77.67  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK------GKwhgDVAVKILKVV--DPtpeqlqafRNEVAVL-RKTRHVNIL-LFMGYMTKDNLAIVTQWC 343
Cdd:cd14091     8 IGKGSYSVCKRcihkatGK---EYAVKIIDKSkrDP--------SEEIEILlRYGQHPNIItLRDVYDDGNSVYLVTELL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLY------KHLHVQETKFQMFQLidiarqtAQGMDYLHAKNIIHRDMKSNNIF--LHEGL--TVKIGDFGLAtvks 413
Cdd:cd14091    77 RGGELLdrilrqKFFSEREASAVMKTL-------TKTVEYLHSQGVVHRDLKPSNILyaDESGDpeSLRICDFGFA---- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 rwsgsQQVEQPTGSVL-------WMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINN--RDQIIFMVGRGY 484
Cdd:cd14091   146 -----KQLRAENGLLMtpcytanFVAPEVLKKQG---YDAACDIWSLGVLLYTMLAGYTPFASGPNdtPEVILARIGSGK 217

                  ..
gi 1720416759 485 AS 486
Cdd:cd14091   218 ID 219
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
277-462 1.11e-15

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 77.76  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 277 GSFGTVYKGKWHGD-VAVKILKVVDPtpeqlQAFRNEVAVLRK--TRHVNILLFM-----GYMTKDNLAIVTQWCEGSSL 348
Cdd:cd14140     6 GRFGCVWKAQLMNEyVAVKIFPIQDK-----QSWQSEREIFSTpgMKHENLLQFIaaekrGSNLEMELWLITAFHDKGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQmfQLIDIARQTAQGMDYLHAK-----------NIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSG 417
Cdd:cd14140    81 TDYLKGNIVSWN--ELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKP 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVLWMAPEV----IRMQDDnpfSF-QSDVYSYGIVLYELMA 462
Cdd:cd14140   159 PGDTHGQVGTRRYMAPEVlegaINFQRD---SFlRIDMYAMGLVLWELVS 205
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
274-531 1.16e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 77.70  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK------GKWhgdVAVKILKVvdPTPEQ---LQAFRnEVAVLRKTR---HVNILLFM---GYMTKDNLAI 338
Cdd:cd07863     8 IGVGAYGTVYKardphsGHF---VALKSVRV--QTNEDglpLSTVR-EVALLKRLEafdHPNIVRLMdvcATSRTDRETK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCE--GSSLYKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrw 415
Cdd:cd07863    82 VTLVFEhvDQDLRTYLDkVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYS-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 sgSQQVEQPTGSVLWM-APEVIrMQddNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI--IF-MVG---------- 481
Cdd:cd07863   160 --CQMALTPVVVTLWYrAPEVL-LQ--STYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLgkIFdLIGlppeddwprd 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 482 ----RGYASPDLSRLYKNCPKAMKRLVADCVKKVKEERPLfpQILSSIELLQHS 531
Cdd:cd07863   235 vtlpRGAFSPRGPRPVQSVVPEIEESGAQLLLEMLTFNPH--KRISAFRALQHP 286
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
274-535 1.23e-15

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 77.46  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwHGD----VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGS-- 346
Cdd:cd06617     9 LGRGAYGVVDKMR-HVPtgtiMAVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREgDVWICMEVMDTSld 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLatvksrwSG----SQQV 421
Cdd:cd06617    88 KFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGI-------SGylvdSVAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGSVLWMAPEVIRMQ-DDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGyASPDL--SRLYKNCpk 498
Cdd:cd06617   161 TIDAGCKPYMAPERINPElNQKGYDVKSDVWSLGITMIELATGRFPYDSWKTPFQQLKQVVEE-PSPQLpaEKFSPEF-- 237
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720416759 499 amKRLVADCVKKVKEERPLFPQIL--SSIELLQHSLPKI 535
Cdd:cd06617   238 --QDFVNKCLKKNYKERPNYPELLqhPFFELHLSKNTDV 274
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
273-501 1.29e-15

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 76.91  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKilkvVDPTPEQLQAFRNEVAVLRKT---RHVNILLFMGyMTKDNLAIVTQWCeGS 346
Cdd:cd14017     7 KIGGGGFGEIYKVRDVVDgeeVAMK----VESKSQPKQVLKMEVAVLKKLqgkPHFCRLIGCG-RTERYNYIVMTLL-GP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLHVQ-ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL----TVKIGDFGLATVKSRWSGSqqV 421
Cdd:cd14017    81 NLAELRRSQpRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPsderTVYILDFGLARQYTNKDGE--V 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPT-------GSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMvGRGYaspDLSRLYK 494
Cdd:cd14017   159 ERPPrnaagfrGTVRYASVNAHRNKE---QGRRDDLWSWFYMLIEFVTGQLPWRKLKDKEEVGKM-KEKI---DHEELLK 231

                  ....*..
gi 1720416759 495 NCPKAMK 501
Cdd:cd14017   232 GLPKEFF 238
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
274-512 1.35e-15

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 76.68  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVyKGKWH---GD-VAVKIL---KVVDPTPEQLqaFRnEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd14074    11 LGRGHFAVV-KLARHvftGEkVAVKVIdktKLDDVSKAHL--FQ-EVRCMKLVQHPNVVrLYEVIDTQTKLYLILELGDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL-TVKIGDFGLAtvkSRWSGSQQVEQP 424
Cdd:cd14074    87 GDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFS---NKFQPGEKLETS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 TGSVLWMAPEVIrMQD--DNPfsfQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPD-LSRLYKNCPKAMk 501
Cdd:cd14074   164 CGSLAYSAPEIL-LGDeyDAP---AVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAhVSPECKDLIRRM- 238
                         250
                  ....*....|.
gi 1720416759 502 rLVADCVKKVK 512
Cdd:cd14074   239 -LIRDPKKRAS 248
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
274-523 1.40e-15

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 76.85  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFmgYMTKDNLAIVTQWCEGSSLYK 350
Cdd:cd14107    10 IGRGTFGFVKRVTHKGNgecCAAKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQ--FETRKTLILILELCSSEELLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 351 HLH----VQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGLAtvKSRWSGSQQVEQp 424
Cdd:cd14107    88 RLFlkgvVTEAEVKLY-----IQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFA--QEITPSEHQFSK- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 425 TGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIfMVGRG---YASPDLSRLYKNCPKAMK 501
Cdd:cd14107   160 YGSPEFVAPEIVH---QEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLL-NVAEGvvsWDTPEITHLSEDAKDFIK 235
                         250       260
                  ....*....|....*....|..
gi 1720416759 502 RLvadcVKKVKEERPLFPQILS 523
Cdd:cd14107   236 RV----LQPDPEKRPSASECLS 253
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
282-460 1.45e-15

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 76.82  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 282 VYKGKwhgDVAVKILKVVDPTPEQlqAFRNEVAVLRKTRHVNILLFMGYMTK-DNLAIVTQWCEGSSLYKHLHVQETKFQ 360
Cdd:cd14045    27 IYDGR---TVAIKKIAKKSFTLSK--RIRKEVKQVRELDHPNLCKFIGGCIEvPNVAIITEYCPKGSLNDVLLNEDIPLN 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 361 MFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKsRWSGSQQVE--QPTGSVLWMAPEVIRM 438
Cdd:cd14045   102 WGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYR-KEDGSENASgyQQRLMQVYLPPENHSN 180
                         170       180
                  ....*....|....*....|..
gi 1720416759 439 QDDNPfSFQSDVYSYGIVLYEL 460
Cdd:cd14045   181 TDTEP-TQATDVYSYAIILLEI 201
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
274-467 1.48e-15

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 76.74  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---YKGKWHGDVAVKILKVVDPTPEQLQAF-RNEVAVLRKTRHVNIL-LFMGYMTKDN-LAIVTQWCEGSS 347
Cdd:cd14165     9 LGEGSYAKVksaYSERLKCNVAIKIIDKKKAPDDFVEKFlPRELEILARLNHKSIIkTYEIFETSDGkVYIVMELGVQGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLhvqETKFQMFQliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd14165    89 LLEFI---KLRGALPE--DVARkmfhQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENGRIVLS 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759 424 PT--GSVLWMAPEVIRMQDDNPfsFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14165   164 KTfcGSAAYAAPEVLQGIPYDP--RIYDIWSLGVILYIMVCGSMPY 207
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
274-474 1.63e-15

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 76.83  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV-----YKGKWHGDVAVKILKVVDPTPEQLQaFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSS 347
Cdd:cd05086     5 IGNGWFGKVllgeiYTGTSVARVVVKELKASANPKEQDD-FLQQGEPYYILQHPNILQCVGQCVEAiPYLLVFEFCDLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKF----QMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQ 423
Cdd:cd05086    84 LKTYLANQQEKLrgdsQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRYKEDYIETDDK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 424 PTGSVLWMAPEVIRMQDDNPFSFQ----SDVYSYGIVLYELMA-GELPYAHINNRD 474
Cdd:cd05086   164 KYAPLRWTAPELVTSFQDGLLAAEqtkySNIWSLGVTLWELFEnAAQPYSDLSDRE 219
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
58-106 1.74e-15

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 70.55  E-value: 1.74e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759  58 HNFARKTFLKLAFCDICQKFL----LNGFRCQTCGYKFHEHCSTKVPTMCVDW 106
Cdd:pfam00130   1 HHFVHRNFKQPTFCDHCGEFLwglgKQGLKCSWCKLNVHKRCHEKVPPECGCD 53
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
274-467 1.77e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 77.75  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKIL--KVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05602    15 IGKGSFGKVLLARHKSDekfYAVKVLqkKAILKKKEEKHIMSERNVLLKNVKHPFLVgLHFSFQTTDKLYFVLDYINGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS 427
Cdd:cd05602    95 LFYHLQ-RERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLC--KENIEPNGTTSTFCGT 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05602   172 PEYLAPEVLHKQ---PYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
274-467 2.16e-15

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 77.15  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG--KWHGD-VAVKI---LKVVDPtpeqLQAFRNEVAVLRKTRHVNILLFMGY---MTKDNLAIVTQWCE 344
Cdd:cd13988     1 LGQGATANVFRGrhKKTGDlYAVKVfnnLSFMRP----LDVQMREFEVLKKLNHKNIVKLFAIeeeLTTRHKVLVMELCP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQETKFQM--FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI--FLHE-GLTV-KIGDFGLAtvkSRWSGS 418
Cdd:cd13988    77 CGSLYTVLEEPSNAYGLpeSEFLIVLRDVVAGMNHLRENGIVHRDIKPGNImrVIGEdGQSVyKLTDFGAA---RELEDD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 419 QQVEQPTGSVLWMAPE-----VIRMQDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd13988   154 EQFVSLYGTEEYLHPDmyeraVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
272-464 2.30e-15

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 76.64  E-value: 2.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYKGKwHGD----VAVKilKVV----DPTPEQLqAFRnEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQW 342
Cdd:cd07847     7 SKIGEGSYGVVFKCR-NREtgqiVAIK--KFVesedDPVIKKI-ALR-EIRMLKQLKHPNLVnLIEVFRRKRKLHLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLY---KHLH-VQETkfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT-------- 410
Cdd:cd07847    82 CDHTVLNeleKNPRgVPEH-----LIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARiltgpgdd 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 411 ----VKSRWsgsqqveqptgsvlWMAPEVIrmQDDNPFSFQSDVYSYGIVLYELMAGE 464
Cdd:cd07847   157 ytdyVATRW--------------YRAPELL--VGDTQYGPPVDVWAIGCVFAELLTGQ 198
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
308-472 2.88e-15

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 76.62  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 308 AFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHR 386
Cdd:cd14168    54 SIENEIAVLRKIKHENIVALEDiYESPNHLYLVMQLVSGGELFDRI-VEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 387 DMKSNNIFLH---EGLTVKIGDFGLatvkSRWSGSQQV-EQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMA 462
Cdd:cd14168   133 DLKPENLLYFsqdEESKIMISDFGL----SKMEGKGDVmSTACGTPGYVAPEVLAQK---PYSKAVDCWSIGVIAYILLC 205
                         170
                  ....*....|
gi 1720416759 463 GELPYAHINN 472
Cdd:cd14168   206 GYPPFYDEND 215
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
274-470 3.49e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 76.07  E-value: 3.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGkWHGD----VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSL 348
Cdd:cd06619     9 LGHGNGGTVYKA-YHLLtrriLAVKVIPL-DITVELQKQIMSELEILYKCDSPYIIGFYGaFFVENRISICTEFMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETkfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVeqptGSV 428
Cdd:cd06619    87 DVYRKIPEH-----VLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYV----GTN 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 429 LWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHI 470
Cdd:cd06619   158 AYMAPERISGEQ---YGIHSDVWSLGISFMELALGRFPYPQI 196
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
261-520 3.80e-15

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 77.01  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLsTRIGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFRN--EVAVLRKTRHVNILLFMGYMTK-- 333
Cdd:cd07878    11 WEVPERYQNL-TPVGSGAYGSVcsaYDTRLRQKVAVK--KLSRPFQSLIHARRTyrELRLLKHMKHENVIGLLDVFTPat 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 -----DNLAIVTQWCeGSSL-----YKHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI 403
Cdd:cd07878    88 sienfNEVYLVTNLM-GADLnnivkCQKLSDEHVQFLIYQLL-------RGLKYIHSAGIIHRDLKPSNVAVNEDCELRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 404 GDFGLAtvksrwsgSQQVEQPTGSVL---WMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYA---HINNRDQII 477
Cdd:cd07878   160 LDFGLA--------RQADDEMTGYVAtrwYRAPEI--MLNWMHYNQTVDIWSVGCIMAELLKGKALFPgndYIDQLKRIM 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 478 FMVGrgyaSPDlsrlykncPKAMKRLVADCVKKVKEERPLFPQ 520
Cdd:cd07878   230 EVVG----TPS--------PEVLKKISSEHARKYIQSLPHMPQ 260
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
273-546 4.04e-15

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 75.83  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKwHGD----VAVKilKVVDPTPE---QLQAFRnEVAVLRKTR-HVNIL-------------LFMGYM 331
Cdd:cd07832     7 RIGEGAHGIVFKAK-DREtgetVALK--KVALRKLEggiPNQALR-EIKALQACQgHPYVVklrdvfphgtgfvLVFEYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 332 tkdnlaivtqwceGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV 411
Cdd:cd07832    83 -------------LSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 412 KSRwSGSQQVEQPTGSVLWMAPEVIRMQDDnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQ---IIFMVGR------ 482
Cdd:cd07832   150 FSE-EDPRLYSHQVATRWYRAPELLYGSRK--YDEGVDLWAVGCIFAELLNGSPLFPGENDIEQlaiVLRTLGTpnektw 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 483 -GYAS-PDLSRLY--KNCPKAMKRLVADCVKkvkeerplfpqilSSIELLQHSL---PKINRSASEPSLHR 546
Cdd:cd07832   227 pELTSlPDYNKITfpESKGIRLEEIFPDCSP-------------EAIDLLKGLLvynPKKRLSAEEALRHP 284
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-468 4.38e-15

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 75.51  E-value: 4.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY-----KGKWHGDV-AVKILK---VVDPTpEQLQAFRNEVAVLRKTRHVNIL--LFMGYMTKDNLAIVTQW 342
Cdd:cd05583     2 LGTGAYGKVFlvrkvGGHDAGKLyAMKVLKkatIVQKA-KTAEHTMTERQVLEAVRQSPFLvtLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVE 422
Cdd:cd05583    81 VNGGELFTHLY-QREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLS--KEFLPGENDRA 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 423 QP-TGSVLWMAPEVIRMQDDNpFSFQSDVYSYGIVLYELMAGELPYA 468
Cdd:cd05583   158 YSfCGTIEYMAPEVVRGGSDG-HDKAVDWWSLGVLTYELLTGASPFT 203
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
261-481 4.94e-15

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 76.62  E-value: 4.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTrIGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFRN--EVAVLRKTRHVNILLFMGYMTK-- 333
Cdd:cd07877    13 WEVPERYQNLSP-VGSGAYGSVcaaFDTKTGLRVAVK--KLSRPFQSIIHAKRTyrELRLLKHMKHENVIGLLDVFTPar 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 334 -----DNLAIVTQWCeGSSLYKHLHVQE-----TKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI 403
Cdd:cd07877    90 sleefNDVYLVTHLM-GADLNNIVKCQKltddhVQFLIYQIL-------RGLKYIHSADIIHRDLKPSNLAVNEDCELKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 404 GDFGLAtvksrwsgSQQVEQPTGSVL---WMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYA---HINNRDQII 477
Cdd:cd07877   162 LDFGLA--------RHTDDEMTGYVAtrwYRAPEI--MLNWMHYNQTVDIWSVGCIMAELLTGRTLFPgtdHIDQLKLIL 231

                  ....
gi 1720416759 478 FMVG 481
Cdd:cd07877   232 RLVG 235
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
270-467 5.07e-15

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 75.22  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHG---DVAVKILKVVDPTPEQLQAFRN----EVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQ 341
Cdd:cd14105     9 IGEELGSGQFAVVKKCREKStglEYAAKFIKKRRSKASRRGVSREdierEVSILRQVLHPNIItLHDVFENKTDVVLILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHVQETKFQMfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT----VKIGDFGLAtvkSRWSG 417
Cdd:cd14105    89 LVAGGELFDFLAEKESLSEE-EATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLA---HKIED 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14105   165 GNEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 211
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
270-467 5.94e-15

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 75.37  E-value: 5.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHGDVAVKILKVVD-------------PTP--------EQ------LQAFRNEVAVLRKTRHV 322
Cdd:cd14200     4 LQSEIGKGSYGVVKLAYNESDDKYYAMKVLSkkkllkqygfprrPPPrgskaaqgEQakplapLERVYQEIAILKKLDHV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 323 NILLFMGYM---TKDNLAIVTQWCEGSSLykhLHV-QETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG 398
Cdd:cd14200    84 NIVKLIEVLddpAEDNLYMVFDLLRKGPV---MEVpSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 399 LTVKIGDFGlatVKSRWSGSQ-QVEQPTGSVLWMAPEVIrmqDDNPFSFQS---DVYSYGIVLYELMAGELPY 467
Cdd:cd14200   161 GHVKIADFG---VSNQFEGNDaLLSSTAGTPAFMAPETL---SDSGQSFSGkalDVWAMGVTLYCFVYGKCPF 227
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
276-462 6.68e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.45  E-value: 6.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 276 SGSFGTVYKGKWHGDVAVKILKVvdptpEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQ 355
Cdd:PHA03209   76 PGSEGRVFVATKPGQPDPVVLKI-----GQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKR 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 356 ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKsrwsgsqqVEQP-----TGSVLW 430
Cdd:PHA03209  151 SRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFP--------VVAPaflglAGTVET 222
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720416759 431 MAPEVIRMQDDNPfsfQSDVYSYGIVLYELMA 462
Cdd:PHA03209  223 NAPEVLARDKYNS---KADIWSAGIVLFEMLA 251
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
273-477 6.96e-15

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 75.21  E-value: 6.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVV-----DPTPEQlqAFRnEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd07836     7 KLGEGTYATVYKGRNRTTGEIVALKEIhldaeEGTPST--AIR-EISLMKELKHENIVrLHDVIHTENKLMLVFEYMDKD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 sLYKH---------LHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSG 417
Cdd:cd07836    84 -LKKYmdthgvrgaLDPNTVKSFTYQLL-------KGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA----RAFG 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 418 ------SQQVeqptgSVLWM-APEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQII 477
Cdd:cd07836   152 ipvntfSNEV-----VTLWYrAPDV--LLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLL 211
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-516 7.06e-15

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 75.42  E-value: 7.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY---------KGKWHgdvAVKILK--VVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY--MTKDNLAIVT 340
Cdd:cd05613     8 LGTGAYGKVFlvrkvsghdAGKLY---AMKVLKkaTIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYafQTDTKLHLIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGSQQ 420
Cdd:cd05613    85 DYINGGELFTHL-SQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGL----SKEFLLDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQP---TGSVLWMAPEVIRmQDDNPFSFQSDVYSYGIVLYELMAGELPYAhinnrdqiifMVGRGYASPDLS-RLYKN- 495
Cdd:cd05613   160 NERAysfCGTIEYMAPEIVR-GGDSGHDKAVDWWSLGVLMYELLTGASPFT----------VDGEKNSQAEISrRILKSe 228
                         250       260
                  ....*....|....*....|...
gi 1720416759 496 --CPKAMKRLVADCVKKVKEERP 516
Cdd:cd05613   229 ppYPQEMSALAKDIIQRLLMKDP 251
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
274-528 8.22e-15

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 74.85  E-value: 8.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK---GKWHGDVAVKILKVVDPtpEQLQAFRNEVAVLRKTR-HVNILLFMG--YMTK-------DNLAIVT 340
Cdd:cd14036     8 IAEGGFAFVYEaqdVGTGKEYALKRLLSNEE--EKNKAIIQEINFMKKLSgHPNIVQFCSaaSIGKeesdqgqAEYLLLT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSsLYKHLHVQETKFQMF--QLIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLTVKIGDFGLATVKS--- 413
Cdd:cd14036    86 ELCKGQ-LVDFVKKVEAPGPFSpdTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAhyp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 --RWSGSQ--QVEQPTGSV---LWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIfmvGRGYAS 486
Cdd:cd14036   165 dySWSAQKrsLVEDEITRNttpMYRTPEMIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFED-GAKLRII---NAKYTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 487 PDLSRLYkncpKAMKRLVADCVKKVKEERPLFPQILSSIELL 528
Cdd:cd14036   241 PPNDTQY----TVFHDLIRSTLKVNPEERLSITEIVEQLQEL 278
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-482 9.21e-15

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 75.41  E-value: 9.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK------GKwhgDVAVKIL-KVVDPTpeqlqafrNEVAVLRKTR-HVNIL-LFMGYMTKDNLAIVTQWCE 344
Cdd:cd14092    14 LGDGSFSVCRKcvhkktGQ---EFAVKIVsRRLDTS--------REVQLLRLCQgHPNIVkLHEVFQDELHTYLVMELLR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI-FLH--EGLTVKIGDFGLATVKsrwSGSQQV 421
Cdd:cd14092    83 GGELLERIR-KKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLlFTDedDDAEIKIVDFGFARLK---PENQPL 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 422 EQPTGSVLWMAPEVIRMQDDNP-FSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGR 482
Cdd:cd14092   159 KTPCFTLPYAAPEVLKQALSTQgYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKR 220
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
274-524 9.87e-15

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 74.20  E-value: 9.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKI---------LKVVDPTPEQLqafrnEVAVLRKT-----RHVnILLFMGYMTKDNL 336
Cdd:cd14005     8 LGKGGFGTVYSGVRIRDglpVAVKFvpksrvtewAMINGPVPVPL-----EIALLLKAskpgvPGV-IRLLDWYERPDGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSS-----LYKHLHVQETkfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH-EGLTVKIGDFGLAT 410
Cdd:cd14005    82 LLIMERPEPCQdlfdfITERGALSEN-----LARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 411 VKSRwsgsQQVEQPTGSVLWMAPEVIRMQDDNPFSfqSDVYSYGIVLYELMAGELPYahiNNRDQIIFmvGRGYASPDLS 490
Cdd:cd14005   157 LLKD----SVYTDFDGTRVYSPPEWIRHGRYHGRP--ATVWSLGILLYDMLCGDIPF---ENDEQILR--GNVLFRPRLS 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1720416759 491 rlykncpKAMKRLVADCVKKVKEERPLFPQILSS 524
Cdd:cd14005   226 -------KECCDLISRCLQFDPSKRPSLEQILSH 252
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
274-467 1.13e-14

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 74.32  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---YKGKWHGDVAVKIL-------------------------KVVDPtpeqLQAFRNEVAVLRKTRHVNIL 325
Cdd:cd14118     2 IGKGSYGIVklaYNEEDNTLYAMKILskkkllkqagffrrppprrkpgalgKPLDP----LDRVYREIAILKKLDHPNVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 326 LFMGYM---TKDNLAIVTQWCEGSSLykhLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTV 401
Cdd:cd14118    78 KLVEVLddpNEDNLYMVFELVDKGAV---MEVPTDNpLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 402 KIGDFGlatVKSRWSGSQQVEQPT-GSVLWMAPEVIRMQDDNpFSFQS-DVYSYGIVLYELMAGELPY 467
Cdd:cd14118   155 KIADFG---VSNEFEGDDALLSSTaGTPAFMAPEALSESRKK-FSGKAlDIWAMGVTLYCFVFGRCPF 218
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
270-467 1.24e-14

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 74.78  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHGD---VAVKILKVVDPTP-EQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCE 344
Cdd:cd05612     5 RIKTIGTGTFGRVHLVRDRISehyYALKVMAIPEVIRlKQEQHVHNEKRVLKEVSHPFIIrLFWTEHDQRFLYMLMEYVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT--VKSRWSgsqqve 422
Cdd:cd05612    85 GGELFSYLR-NSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKklRDRTWT------ 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 423 qPTGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05612   158 -LCGTPEYLAPEVIQSKGHNK---AVDWWALGILIYEMLVGYPPF 198
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
274-531 1.44e-14

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 73.83  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTpeQLQA----FRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSL 348
Cdd:cd14185     8 IGDGNFAVVKECRHWNENQEYAMKIIDKS--KLKGkedmIESEILIIKSLSHPNIVkLFEVYETEKEIYLILEYVRGGDL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLhVQETKF----QMFQLIDIArqtaQGMDYLHAKNIIHRDMKSNNIFLH----EGLTVKIGDFGLATVKSRwsgsqQ 420
Cdd:cd14185    86 FDAI-IESVKFtehdAALMIIDLC----EALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFGLAKYVTG-----P 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQPTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPY-AHINNRDQIIFMVGRGYASpDLSRLYKNCPKA 499
Cdd:cd14185   156 IFTVCGTPTYVAPEIL---SEKGYGLEVDMWAAGVILYILLCGFPPFrSPERDQEELFQIIQLGHYE-FLPPYWDNISEA 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720416759 500 MKRLVADCVKKVKEERplfpqiLSSIELLQHS 531
Cdd:cd14185   232 AKDLISRLLVVDPEKR------YTAKQVLQHP 257
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
274-467 1.58e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 73.90  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG---DVAVKILKVVDPTPEQLQAFRN----EVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd14194    13 LGSGQFAVVKKCREKStglQYAAKFIKKRRTKSSRRGVSREdierEVSILKEIQHPNVItLHEVYENKTDVILILELVAG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQMfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT----VKIGDFGLAtvkSRWSGSQQV 421
Cdd:cd14194    93 GELFDFLAEKESLTEE-EATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLA---HKIDFGNEF 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759 422 EQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14194   169 KNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 211
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
270-478 1.59e-14

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 74.48  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHG---DVAVKILK-VVDptpeqLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCE 344
Cdd:cd14085     7 IESELGRGATSVVYRCRQKGtqkPYAVKKLKkTVD-----KKIVRTEIGVLLRLSHPNIIkLKEIFETPTEISLVLELVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIF---LHEGLTVKIGDFGLATVKsrwsgSQQV 421
Cdd:cd14085    82 GGELFDRI-VEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSKIV-----DQQV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 422 EQPT--GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYaHINNRDQIIF 478
Cdd:cd14085   156 TMKTvcGTPGYCAPEILR---GCAYGPEVDMWSVGVITYILLCGFEPF-YDERGDQYMF 210
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
274-469 1.60e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 74.18  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV--YKGKWHGD-VAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLF------MGYMTKDNLAIVTQWCE 344
Cdd:cd14039     1 LGTGGFGNVclYQNQETGEkIAIKSCRL-ELSVKNKDRWCHEIQIMKKLNHPNVVKAcdvpeeMNFLVNDVPLLAMEYCS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQET--KFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHE--GLTV-KIGDFGLAtvKSRWSGSq 419
Cdd:cd14039    80 GGDLRKLLNKPENccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEinGKIVhKIIDLGYA--KDLDQGS- 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPTGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAH 469
Cdd:cd14039   157 LCTSFVGTLQYLAPELF---ENKSYTVTVDYWSFGTMVFECIAGFRPFLH 203
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
274-467 1.63e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 73.84  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHG---DVAVKILKvvdptPEQLQAFRN---------EVAVLRKTRHVNILLFMG-YMTKDNLAIVT 340
Cdd:cd14196    13 LGSGQFAIVKKCREKStglEYAAKFIK-----KRQSRASRRgvsreeierEVSILRQVLHPNIITLHDvYENRTDVVLIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT----VKIGDFGLAtvkSRWS 416
Cdd:cd14196    88 ELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLA---HEIE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 417 GSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14196   164 DGVEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 211
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
274-530 1.63e-14

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 73.86  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILK-VVDPTPEQLQAFRNEVAVLRK-TRHVNILLFMGYMT---KDN---LAIVTQWCEG 345
Cdd:cd14037    11 LAEGGFAHVYLVKTSNGGNRAALKrVYVNDEHDLNVCKREIEIMKRlSGHKNIVGYIDSSAnrsGNGvyeVLLLMEYCKG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLY----KHLHvqeTKFQMFQLIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR----W 415
Cdd:cd14037    91 GGVIdlmnQRLQ---TGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSATTKILppqtK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQ-----PTGSvlWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYahinNRDQIIFMVGRGYASPDLS 490
Cdd:cd14037   168 QGVTYVEEdikkyTTLQ--YRAPEMIDLYRGKPITEKSDIWALGCLLYKLCFYTTPF----EESGQLAILNGNFTFPDNS 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1720416759 491 RLYKNcpkaMKRLVADCVKKVKEERPLFPQILSSIELLQH 530
Cdd:cd14037   242 RYSKR----LHKLIRYMLEEDPEKRPNIYQVSYEAFELAG 277
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
270-546 1.74e-14

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 74.38  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYK--GKWHGDV-AVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLA-IVTQWCEG 345
Cdd:cd14086     5 LKEELGKGAFSVVRRcvQKSTGQEfAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHyLVFDLVTG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQE------TKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLATvksrws 416
Cdd:cd14086    85 GELFEDIVAREfyseadASHCIQQILE-------SVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAI------ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 gSQQVEQPT-----GSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAhinNRDQ-----IIFMVGRGYAS 486
Cdd:cd14086   152 -EVQGDQQAwfgfaGTPGYLSPEVLRKD---PYGKPVDIWACGVILYILLVGYPPFW---DEDQhrlyaQIKAGAYDYPS 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 487 PD---LSRLYKNCPKAMkrLVADCVKKVkeerplfpqilSSIELLQHslPKI-NRSASEPSLHR 546
Cdd:cd14086   225 PEwdtVTPEAKDLINQM--LTVNPAKRI-----------TAAEALKH--PWIcQRDRVASMVHR 273
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
274-467 2.04e-14

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 74.34  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK--VV--DPTPEQLQAFRNEVAVlrKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05592     3 LGKGSFGKVMLAELKGTnqyFAIKALKkdVVleDDDVECTMIERRVLAL--ASQHPFLThLFCTFQTESHLFFVMEYLNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPT 425
Cdd:cd05592    81 GDLMFHIQ-QSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC--KENIYGENKASTFC 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 426 GSVLWMAPEVIRMQDDNpfsFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05592   158 GTPDYIAPEILKGQKYN---QSVDWWSFGVLLYEMLIGQSPF 196
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
270-409 2.13e-14

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 74.27  E-value: 2.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHGDVAVKILKVV------DPTPeqLQAFRnEVAVLRKTRHVNI--LLFMGYMTKDNLA---- 337
Cdd:cd07866    12 ILGKLGEGTFGEVYKARQIKTGRVVALKKIlmhnekDGFP--ITALR-EIKILKKLKHPNVvpLIDMAVERPDKSKrkrg 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 338 ---IVTQWCEgSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd07866    89 svyMVTPYMD-HDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLA 162
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
273-478 2.49e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 73.87  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGK---WHGDVAVKILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEgSSL 348
Cdd:cd07872    13 KLGEGTYATVFKGRsklTENLVALKEIRLEHEEGAPCTAIR-EVSLLKDLKHANIVTLHDIVHTDkSLTLVFEYLD-KDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTgsv 428
Cdd:cd07872    91 KQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVT--- 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 429 LWMAPEVIrMQDDNPFSFQSDVYSYGIVLYELMAGE--LPYAHINNRDQIIF 478
Cdd:cd07872   168 LWYRPPDV-LLGSSEYSTQIDMWGVGCIFFEMASGRplFPGSTVEDELHLIF 218
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
311-467 2.68e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 73.49  E-value: 2.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 311 NEVAVLRK--TRHVnILLFMGYMTKDNLAIVTQWCEGSSLYKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRD 387
Cdd:cd05631    49 NEKRILEKvnSRFV-VSLAYAYETKDALCLVLTIMNGGDLKFHIYnMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 388 MKSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05631   128 LKPENILLDDRGHIRISDLGLAV---QIPEGETVRGRVGTVGYMAPEVIN---NEKYTFSPDWWGLGCLIYEMIQGQSPF 201
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
270-467 2.74e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 73.11  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHG---DVAVKILKVVDPTPEQLQAFRNE----VAVLRKTRHVNILLFMG-YMTKDNLAIVTQ 341
Cdd:cd14195     9 MGEELGSGQFAIVRKCREKGtgkEYAAKFIKKRRLSSSRRGVSREEiereVNILREIQHPNIITLHDiFENKTDVVLILE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHVQE--TKFQMFQLIdiaRQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT----VKIGDFGLAtvkSRW 415
Cdd:cd14195    89 LVSGGELFDFLAEKEslTEEEATQFL---KQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIA---HKI 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 416 SGSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14195   163 EAGNEFKNIFGTPEFVAPEIVNYE---PLGLEADMWSIGVITYILLSGASPF 211
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
291-525 3.06e-14

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 73.00  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 291 VAVKILKVVDPTPEQLQafRNEVAVLRKTRHVNILLFMGYMTKDNLAI-VTQWCEGSSL---------YKHLHVQETKFQ 360
Cdd:cd14044    34 VILKDLKNNEGNFTEKQ--KIELNKLLQIDYYNLTKFYGTVKLDTMIFgVIEYCERGSLrdvlndkisYPDGTFMDWEFK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 361 MFQLIDIARqtaqGMDYLHAKNI-IHRDMKSNNIFLHEGLTVKIGDFGLATVksrwsgsqqveQPTGSVLWMAPEVIRMQ 439
Cdd:cd14044   112 ISVMYDIAK----GMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFGCNSI-----------LPPSKDLWTAPEHLRQA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 440 DdnpFSFQSDVYSYGIVLYELMAGELPY--AHINNRDQIIFMV----GRGYASPDLsrlykNCPKAMKR------LVADC 507
Cdd:cd14044   177 G---TSQKGDVYSYGIIAQEIILRKETFytAACSDRKEKIYRVqnpkGMKPFRPDL-----NLESAGERerevygLVKNC 248
                         250
                  ....*....|....*...
gi 1720416759 508 VKKVKEERPLFPQILSSI 525
Cdd:cd14044   249 WEEDPEKRPDFKKIENTL 266
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
273-410 3.20e-14

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 72.88  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKILKVvDPTPEQLqafRNEVAVLRKTR-HVNILLFMGYMTKDNL-AIVTQWCeGSS 347
Cdd:cd14016     7 KIGSGSFGEVYLGidlKTGEEVAIKIEKK-DSKHPQL---EYEAKVYKLLQgGPGIPRLYWFGQEGDYnVMVMDLL-GPS 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 348 LYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL---TVKIGDFGLAT 410
Cdd:cd14016    82 LEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKnsnKVYLIDFGLAK 147
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
274-566 3.54e-14

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 73.90  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGT----VYKGKwHGDVAVKILKVV--DPTPEQlqafrnEVaVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGS 346
Cdd:cd14176    27 IGVGSYSVckrcIHKAT-NMEFAVKIIDKSkrDPTEEI------EI-LLRYGQHPNIITLKDvYDDGKYVYVVTELMKGG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI-FLHEG---LTVKIGDFGLAtvKSRWSGSQQVE 422
Cdd:cd14176    99 ELLDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESgnpESIRICDFGFA--KQLRAENGLLM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 423 QPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAH--INNRDQIIFMVGRGYASpdLSRLYKNcpkAM 500
Cdd:cd14176   176 TPCYTANFVAPEVLERQG---YDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFS--LSGGYWN---SV 247
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 501 KRLVADCVKKVKEERPlfPQILSSIELLQH-------SLPK--INRSASePSLHRAAHTEDINACTLTTSPRL-PV 566
Cdd:cd14176   248 SDTAKDLVSKMLHVDP--HQRLTAALVLRHpwivhwdQLPQyqLNRQDA-PHLVKGAMAATYSALNRNQSPVLePV 320
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
311-467 4.25e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 73.47  E-value: 4.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 311 NEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLYKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDM 388
Cdd:cd05632    51 NEKQILEKVNSQFVVnLAYAYETKDALCLVLTIMNGGDLKFHIYnMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDL 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 389 KSNNIFLHEGLTVKIGDFGLATvksRWSGSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05632   131 KPENILLDDYGHIRISDLGLAV---KIPEGESIRGRVGTVGYMAPEVLNNQR---YTLSPDYWGLGCLIYEMIEGQSPF 203
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
273-467 5.08e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 72.69  E-value: 5.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKgkWHG-----DVAVKILKVvDPTPEQLQAFRNEVAVLRKTRHVNILLF------MGYMTKDNLAIVT- 340
Cdd:cd14038     1 RLGTGGFGNVLR--WINqetgeQVAIKQCRQ-ELSPKNRERWCLEIQIMKRLNHPNVVAArdvpegLQKLAPNDLPLLAm 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLHVQETKFQMFQ--LIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEG---LTVKIGDFGLAtvKSRW 415
Cdd:cd14038    78 EYCQGGDLRKYLNQFENCCGLREgaILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGeqrLIHKIIDLGYA--KELD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 416 SGSQQVEQpTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14038   156 QGSLCTSF-VGTLQYLAPELLEQQK---YTVTVDYWSFGTLAFECITGFRPF 203
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
261-481 5.84e-14

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 73.45  E-value: 5.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLStRIGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFR--NEVAVLRKTRHVNILLFMGYMTKDN 335
Cdd:cd07880    11 WEVPDRYRDLK-QVGSGAYGTVcsaLDRRTGAKVAIK--KLYRPFQSELFAKRayRELRLLKHMKHENVIGLLDVFTPDL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 336 ---------LAIVTQWCEGSSLYKHLHVQETKFQMfqlidIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDF 406
Cdd:cd07880    88 sldrfhdfyLVMPFMGTDLGKLMKHEKLSEDRIQF-----LVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 407 GLAtvksRWSGSQQveqpTGSVL---WMAPEVIR--MQddnpFSFQSDVYSYGIVLYELMAGELPYA---HINNRDQIIF 478
Cdd:cd07880   163 GLA----RQTDSEM----TGYVVtrwYRAPEVILnwMH----YTQTVDIWSVGCIMAEMLTGKPLFKghdHLDQLMEIMK 230

                  ...
gi 1720416759 479 MVG 481
Cdd:cd07880   231 VTG 233
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
326-467 5.97e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 72.61  E-value: 5.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 326 LFMGYMTKDNLAIVTQWCEGSSLYKHLH-VQETK--FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK 402
Cdd:cd05608    66 LAYAFQTKTDLCLVMTIMNGGDLRYHIYnVDEENpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVR 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 403 IGDFGLATVKSrwSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05608   146 ISDLGLAVELK--DGQTKTKGYAGTPGFMAPELLL---GEEYDYSVDYFTLGVTLYEMIAARGPF 205
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
295-525 6.32e-14

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 72.28  E-value: 6.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 295 ILKVVDPTPEQLQ-AFRNEVAVLRKTRHVNILLFMGYMTKDNLAI-VTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTA 372
Cdd:cd05077    40 ILKVLDPSHRDISlAFFETASMMRQVSHKHIVLLYGVCVRDVENImVEEFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 373 QGMDYLHAKNIIHRDMKSNNIFL-HEGLT------VKIGDFGLA-TVKSRwsgSQQVEQptgsVLWMAPEVIrmQDDNPF 444
Cdd:cd05077   120 SALSYLEDKDLVHGNVCTKNILLaREGIDgecgpfIKLSDPGIPiTVLSR---QECVER----IPWIAPECV--EDSKNL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 445 SFQSDVYSYGIVLYEL-MAGELPYahinnRDQIIFMVGRGYASPdlSRLYKNCPKAMKRLVADCVKKVKEERPLFPQILS 523
Cdd:cd05077   191 SIAADKWSFGTTLWEIcYNGEIPL-----KDKTLAEKERFYEGQ--CMLVTPSCKELADLMTHCMNYDPNQRPFFRAIMR 263

                  ..
gi 1720416759 524 SI 525
Cdd:cd05077   264 DI 265
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
261-488 6.38e-14

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 73.10  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLSTrIGSGSFGTVYKGKWHG-DVAVKILKVVDPTPEQLQAFR--NEVAVLRKTRHVNILLFMGYMTKD--- 334
Cdd:cd07851    11 WEVPDRYQNLSP-VGSGAYGQVCSAFDTKtGRKVAIKKLSRPFQSAIHAKRtyRELRLLKHMKHENVIGLLDVFTPAssl 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 ----NLAIVTQWCeGSSLYKHLHVQ-----ETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGD 405
Cdd:cd07851    90 edfqDVYLVTHLM-GADLNNIVKCQklsddHIQFLVYQIL-------RGLKYIHSAGIIHRDLKPSNLAVNEDCELKILD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 406 FGLAtvksrwsgSQQVEQPTGSVL--W-MAPEVI--RMQddnpFSFQSDVYSYGIVLYELMAGELPYA---HINNRDQII 477
Cdd:cd07851   162 FGLA--------RHTDDEMTGYVAtrWyRAPEIMlnWMH----YNQTVDIWSVGCIMAELLTGKTLFPgsdHIDQLKRIM 229
                         250
                  ....*....|.
gi 1720416759 478 FMVGrgyaSPD 488
Cdd:cd07851   230 NLVG----TPD 236
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
367-501 7.13e-14

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 71.97  E-value: 7.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 367 IARQTAQGMDYLHAKNIIHRDMKSNNIFL--HEGLTVKIGDFGL-----ATVKSRWsgsqqveqptGSVLWMAPEVIRMQ 439
Cdd:cd13987    96 CAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLtrrvgSTVKRVS----------GTIPYTAPEVCEAK 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 440 DDNPFSFQ--SDVYSYGIVLYELMAGELPYAHINNRDQIIFMV-----GRGYASPDLSRLYKncPKAMK 501
Cdd:cd13987   166 KNEGFVVDpsIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFvrwqkRKNTAVPSQWRRFT--PKALR 232
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
260-409 7.80e-14

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 72.57  E-value: 7.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 260 YWEIEASEVMLST--------RIGSGSFGTVYKGkWHGD----VAVKILKvvdptPEQLQAFRNEVAVLRKTR-HVNIL- 325
Cdd:cd14132     4 YWDYENLNVEWGSqddyeiirKIGRGKYSEVFEG-INIGnnekVVIKVLK-----PVKKKKIKREIKILQNLRgGPNIVk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 326 ---LFMGYMTKdNLAIVTQWCEGS---SLYKHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFL-HEG 398
Cdd:cd14132    78 lldVVKDPQSK-TPSLIFEYVNNTdfkTLYPTLTDYDIRYYMYELL-------KALDYCHSKGIMHRDVKPHNIMIdHEK 149
                         170
                  ....*....|.
gi 1720416759 399 LTVKIGDFGLA 409
Cdd:cd14132   150 RKLRLIDWGLA 160
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
274-481 9.54e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 72.49  E-value: 9.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQLQAFRN------------EVAVLRKTRHVNIllfMG----YMTKD 334
Cdd:PTZ00024   17 LGEGTYGKVEKAydtLTGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEIKHENI---MGlvdvYVEGD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 NLAIVTQWCEGSslYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT---- 410
Cdd:PTZ00024   94 FINLVMDIMASD--LKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARrygy 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 411 -----VKSRWSGSQQVEQPTGSV--LWM-APEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQ---IIFM 479
Cdd:PTZ00024  172 ppysdTLSKDETMQRREEMTSKVvtLWYrAPEL--LMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQlgrIFEL 249

                  ..
gi 1720416759 480 VG 481
Cdd:PTZ00024  250 LG 251
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
273-463 9.83e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 72.59  E-value: 9.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKilKVVDptpeqlqAFRN---------EVAVLRKTR-HVNI--------------- 324
Cdd:cd07852    14 KLGKGAYGIVWKAidkKTGEVVALK--KIFD-------AFRNatdaqrtfrEIMFLQELNdHPNIikllnviraendkdi 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 325 -LLFmGYMTKDnLAIVTQwcegSSLYKHLHVQetkFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI 403
Cdd:cd07852    85 yLVF-EYMETD-LHAVIR----ANILEDIHKQ---YIMYQLL-------KALKYLHSGGVIHRDLKPSNILLNSDCRVKL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 404 GDFGLAtvksRwSGSQQVEQPTGSVL-------WM-APEVIrmQDDNPFSFQSDVYSYGIVLYELMAG 463
Cdd:cd07852   149 ADFGLA----R-SLSQLEEDDENPVLtdyvatrWYrAPEIL--LGSTRYTKGVDMWSVGCILGEMLLG 209
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
274-467 9.87e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 71.98  E-value: 9.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKwhgDVAVKILKVvDPTPEQLQAFRnEVAVLRKTR-HVNILLFMGYMTKDN-LAIVTQWCEG 345
Cdd:cd14174    10 LGEGAYAKVQgcvslqNGK---EYAVKIIEK-NAGHSRSRVFR-EVETLYQCQgNKNILELIEFFEDDTrFYLVFEKLRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI---FLHEGLTVKIGDFGLAT-VKSRWS----G 417
Cdd:cd14174    85 GSILAHIQKRK-HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIlceSPDKVSPVKICDFDLGSgVKLNSActpiT 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 418 SQQVEQPTGSVLWMAPEVIRMQDDNP--FSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14174   164 TPELTTPCGSAEYMAPEVVEVFTDEAtfYDKRCDLWSLGVILYIMLSGYPPF 215
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
274-532 1.07e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 72.14  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQ----LQAFRnEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGS--- 346
Cdd:cd07864    15 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKegfpITAIR-EIKILRQLNHRSVVNLKEIVTDKQDALDFKKDKGAfyl 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 -------SLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGSQ 419
Cdd:cd07864    94 vfeymdhDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLA----RLYNSE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 420 QVEQPTGSV--LWMAPEVIRMQDDNpFSFQSDVYSYGIVLYELMAGElPYAHINNRDQIIFMVGRGYAS------PDLSR 491
Cdd:cd07864   170 ESRPYTNKVitLWYRPPELLLGEER-YGPAIDVWSCGCILGELFTKK-PIFQANQELAQLELISRLCGSpcpavwPDVIK 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 492 L-YKNC--PKAMKRlvadcvKKVKEERPLFPQilSSIELLQHSL 532
Cdd:cd07864   248 LpYFNTmkPKKQYR------RRLREEFSFIPT--PALDLLDHML 283
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
369-517 1.20e-13

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 71.80  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 369 RQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT---VKIGDFGLATvksRWSGSQQVEQ-PTGSVLWMAPEVIRMQddnPF 444
Cdd:cd14094   116 RQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI---QLGESGLVAGgRVGTPHFMAPEVVKRE---PY 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 445 SFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGR----GYASPDLSRLYKNCpkAMKRLVADCVKKVKEERPL 517
Cdd:cd14094   190 GKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKykmnPRQWSHISESAKDL--VRRMLMLDPAERITVYEAL 264
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
274-467 1.38e-13

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 71.02  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG-----KWHGDVAVKILKVVDPTPEQLQAFRNevavLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd14112    11 IFRGRFSVIVKAvdsttETDAHCAVKIFEVSDEASEAVREFES----LRTLQHENVQrLIAAFKPSNFAYLVMEKLQEDV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 L----YKHLHVQEtkfqmfQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLH--EGLTVKIGDFGLAtvkSRWSGSQQV 421
Cdd:cd14112    87 FtrfsSNDYYSEE------QVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRA---QKVSKLGKV 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759 422 EQPtGSVLWMAPEVIrmQDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14112   158 PVD-GDTDWASPEFH--NPETPITVQSDIWGLGVLTFCLLSGFHPF 200
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
274-467 1.56e-13

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 71.05  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY---KGKWHGDVAVKILKVVDPTPEQLQ-AFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSL 348
Cdd:cd14117    14 LGKGKFGNVYlarEKQSKFIVALKVLFKSQIEKEGVEhQLRREIEIQSHLRHPNILRLYNYFHDRKrIYLILEYAPRGEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvksrWSgsqqVEQPT--- 425
Cdd:cd14117    94 YKELQ-KHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG-------WS----VHAPSlrr 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720416759 426 ----GSVLWMAPEVI--RMQDDnpfsfQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14117   162 rtmcGTLDYLPPEMIegRTHDE-----KVDLWCIGVLCYELLVGMPPF 204
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
270-526 1.69e-13

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 70.60  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYK-GKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRK-TRHVNILLFMGYMtkdnlaIVTQWCEGSS 347
Cdd:cd13975     4 LGRELGRGQYGVVYAcDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSlPKHERIVSLHGSV------IDYSYGGGSS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 ---------LYKHLHVQ-ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSG 417
Cdd:cd13975    78 iavllimerLHRDLYTGiKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SqqveqPTGSVLWMAPEVIRMQDDNPFsfqsDVYSYGIVLYELMAG--ELPYAHIN--NRDQIIFMVGRGYASPDLSRLY 493
Cdd:cd13975   158 S-----IVGTPIHMAPELFSGKYDNSV----DVYAFGILFWYLCAGhvKLPEAFEQcaSKDHLWNNVRKGVRPERLPVFD 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720416759 494 KNCPKAMKRlvadCVKKVKEERPLFPQILSSIE 526
Cdd:cd13975   229 EECWNLMEA----CWSGDPSQRPLLGIVQPKLQ 257
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
273-479 1.89e-13

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 71.10  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKwhgD------VAVKILKVvDPTPE--QLQAFRnEVAVLRKTRHVNIL----LFMGyMTKDNLAIVT 340
Cdd:cd07843    12 RIEEGTYGVVYRAR---DkktgeiVALKKLKM-EKEKEgfPITSLR-EINILLKLQHPNIVtvkeVVVG-SNLDKIYMVM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGS--SLYKHLH----VQETKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksr 414
Cdd:cd07843    86 EYVEHDlkSLMETMKqpflQSEVKCLMLQLLS-------GVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLA----- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 415 wsgsQQVEQPTGS------VLWM-APEVIRMQDDnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI--IFM 479
Cdd:cd07843   154 ----REYGSPLKPytqlvvTLWYrAPELLLGAKE--YSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLnkIFK 221
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
273-409 2.19e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 70.92  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILKVV--DPTPEQL--QAFRnEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGS- 346
Cdd:cd07839     7 KIGEGTYGTVFKAKNRETHEIVALKRVrlDDDDEGVpsSALR-EICLLKELKHKNIVRLYDVLHSDKkLTLVFEYCDQDl 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 347 -----SLYKHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd07839    86 kkyfdSCNGDIDPEIVKSFMFQLL-------KGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLA 146
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
312-467 2.25e-13

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 70.76  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 312 EVAVLRKTRHVNILLFMGYM---TKDNLAIVTQWCEGSSLY-----KHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNI 383
Cdd:cd14199    75 EIAILKKLDHPNVVKLVEVLddpSEDHLYMVFELVKQGPVMevptlKPLSEDQARFYFQDLI-------KGIEYLHYQKI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 384 IHRDMKSNNIFLHEGLTVKIGDFGlatVKSRWSGSQQVEQPT-GSVLWMAPEVIRMQDDNpFSFQS-DVYSYGIVLYELM 461
Cdd:cd14199   148 IHRDVKPSNLLVGEDGHIKIADFG---VSNEFEGSDALLTNTvGTPAFMAPETLSETRKI-FSGKAlDVWAMGVTLYCFV 223

                  ....*.
gi 1720416759 462 AGELPY 467
Cdd:cd14199   224 FGQCPF 229
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
266-467 2.55e-13

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 70.30  E-value: 2.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 266 SEVMLSTRIGSGSFGTVYKGKWHGD---VAVK-ILKVVDPTPEQLqaFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVT 340
Cdd:cd14169     3 SVYELKEKLGEGAFSEVVLAQERGSqrlVALKcIPKKALRGKEAM--VENEIAVLRRINHENIVsLEDIYESPTHLYLAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHL--HVQETKFQMFQLIdiaRQTAQGMDYLHAKNIIHRDMKSNNIFLH---EGLTVKIGDFGLatvkSRW 415
Cdd:cd14169    81 ELVTGGELFDRIieRGSYTEKDASQLI---GQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGL----SKI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 416 SGSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14169   154 EAQGMLSTACGTPGYVAPELLEQK---PYGKAVDVWAIGVISYILLCGYPPF 202
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
305-464 2.62e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 71.95  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 305 QLQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNII 384
Cdd:PHA03212  126 QRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKR-NIAICDILAIERSVLRAIQYLHENRII 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 385 HRDMKSNNIFLHEGLTVKIGDFGLA-----TVKSRWSGSqqveqpTGSVLWMAPEVIRMqddNPFSFQSDVYSYGIVLYE 459
Cdd:PHA03212  205 HRDIKAENIFINHPGDVCLGDFGAAcfpvdINANKYYGW------AGTIATNAPELLAR---DPYGPAVDIWSAGIVLFE 275

                  ....*
gi 1720416759 460 LMAGE 464
Cdd:PHA03212  276 MATCH 280
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
274-476 2.83e-13

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 71.35  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKVVDPTPEQlQAFRnEVAVLRKTRHVNILLF---MGYMTKDNLAIVTQWCEGSS 347
Cdd:cd07854    13 LGCGSNGLVFSAvdsDCDKRVAVKKIVLTDPQSVK-HALR-EIKIIRRLDHDNIVKVyevLGPSGSDLTEDVGSLTELNS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQET----------------KFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLH-EGLTVKIGDFGLA- 409
Cdd:cd07854    91 VYIVQEYMETdlanvleqgplseehaRLFMYQLL-------RGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLAr 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 410 TVKSRWSGSQQVEQPTGSVLWMAPEVIrMQDDNpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI 476
Cdd:cd07854   164 IVDPHYSHKGYLSEGLVTKWYRSPRLL-LSPNN-YTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQM 228
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
274-409 3.20e-13

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 70.78  E-value: 3.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKW-HGDVAVKI-LKVVDPTPEQLQ-----AFRnEVAVLRKTRHVNIL----LFMGYMTKdNLAIVTQW 342
Cdd:cd07842     8 IGRGTYGRVYKAKRkNGKDGKEYaIKKFKGDKEQYTgisqsACR-EIALLRELKHENVVslveVFLEHADK-SVYLLFDY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CE----------GSSLYKHLHVQETKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFL----HEGLTVKIGDFGL 408
Cdd:cd07842    86 AEhdlwqiikfhRQAKRVSIPPSMVKSLLWQILN-------GIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGL 158

                  .
gi 1720416759 409 A 409
Cdd:cd07842   159 A 159
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
277-466 3.50e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 71.41  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 277 GSFGTVYKGKWHGDVAVK--ILKVVD--PTPEQlqafrnEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQW--CEgssLY 349
Cdd:PHA03207  103 GSEGEVFVCTKHGDEQRKkvIVKAVTggKTPGR------EIDILKTISHRAIInLIHAYRWKSTVCMVMPKykCD---LF 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVL 429
Cdd:PHA03207  174 TYVDRSGP-LPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPQCYGWSGTLE 252
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720416759 430 WMAPEVIRMqddNPFSFQSDVYSYGIVLYELMAGELP 466
Cdd:PHA03207  253 TNSPELLAL---DPYCAKTDIWSAGLVLFEMSVKNVT 286
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
266-522 4.13e-13

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 69.88  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 266 SEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQ--LQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQW 342
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDEskFNQIIMELDILHKAVSPYIVDFYGAFFIEGaVYMCMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKhLHVQETKFQMF---QLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLA--TVKSrws 416
Cdd:cd06622    81 MDAGSLDK-LYAGGVATEGIpedVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSgnLVAS--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 gsqQVEQPTGSVLWMAPEVIR---MQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDqiIFMVGRGYASPDLSRLY 493
Cdd:cd06622   157 ---LAKTNIGCQSYMAPERIKsggPNQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYAN--IFAQLSAIVDGDPPTLP 231
                         250       260
                  ....*....|....*....|....*....
gi 1720416759 494 KNCPKAMKRLVADCVKKVKEERPLFPQIL 522
Cdd:cd06622   232 SGYSDDAQDFVAKCLNKIPNRRPTYAQLL 260
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
307-467 5.75e-13

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 69.28  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 307 QAFRNEVAVLRKTRHVNILLFMG-YMTKDNLAIVTQWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIH 385
Cdd:cd14088    44 KAAKNEINILKMVKHPNILQLVDvFETRKEYFIFLELATGREVFDWI-LDQGYYSERDTSNVIRQVLEAVAYLHSLKIVH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 386 RDMKSNNIFLHEGL---TVKIGDFGLATVKsrwsgSQQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMA 462
Cdd:cd14088   123 RNLKLENLVYYNRLknsKIVISDFHLAKLE-----NGLIKEPCGTPEYLAPEVVGRQR---YGRPVDCWAIGVIMYILLS 194

                  ....*
gi 1720416759 463 GELPY 467
Cdd:cd14088   195 GNPPF 199
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
58-103 6.18e-13

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.26  E-value: 6.18e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720416759   58 HNFARKTFLKLAFCDICQKFL----LNGFRCQTCGYKFHEHCSTKVPTMC 103
Cdd:smart00109   1 HKHVFRTFTKPTFCCVCRKSIwgsfKQGLRCSECKVKCHKKCADKVPKAC 50
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
252-522 1.06e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 69.69  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 252 RGQRDSSYY-WEIEASEVMLSTR------IGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFR--NEVAVLRKT 319
Cdd:cd07875     3 RSKRDNNFYsVEIGDSTFTVLKRyqnlkpIGSGAQGIVcaaYDAILERNVAIK--KLSRPFQNQTHAKRayRELVLMKCV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 320 RHVNILLFMGYMTKD-------NLAIVTQWCEgSSLYKHLHVQETKFQMFQLIdiaRQTAQGMDYLHAKNIIHRDMKSNN 392
Cdd:cd07875    81 NHKNIIGLLNVFTPQksleefqDVYIVMELMD-ANLCQVIQMELDHERMSYLL---YQMLCGIKHLHSAGIIHRDLKPSN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 393 IFLHEGLTVKIGDFGLAtvksRWSGSQQVEQP-TGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYA--- 468
Cdd:cd07875   157 IVVKSDCTLKILDFGLA----RTAGTSFMMTPyVVTRYYRAPEVILGMG---YKENVDIWSVGCIMGEMIKGGVLFPgtd 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 469 HINNRDQIIFMVGrgyaSPdlsrlyknCPKAMKRLvADCVKKVKEERP---------LFPQIL 522
Cdd:cd07875   230 HIDQWNKVIEQLG----TP--------CPEFMKKL-QPTVRTYVENRPkyagysfekLFPDVL 279
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
273-476 1.35e-12

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 68.45  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRnEVAVLRK-TRHVNILLFMGYM---TKDNLAIVTQWCEG 345
Cdd:cd07831     6 KIGEGTFSEVLKAQSRKTgkyYAIKCMKKHFKSLEQVNNLR-EIQALRRlSPHPNILRLIEVLfdrKTGRLALVFELMDM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SsLY-------KHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGlTVKIGDFG-LATVKSRwsg 417
Cdd:cd07831    85 N-LYelikgrkRPLPEKRVKNYMYQLL-------KSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGsCRGIYSK--- 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 418 sqqveQPTG---SVLWM-APEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQI 476
Cdd:cd07831   153 -----PPYTeyiSTRWYrAPEC--LLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQI 208
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-467 1.57e-12

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 68.79  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY---------KGKWHgdvAVKILK--VVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY--MTKDNLAIVT 340
Cdd:cd05614     8 LGTGAYGKVFlvrkvsghdANKLY---AMKVLRkaALVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYafQTDAKLHLIL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLatvkSRWSGSQQ 420
Cdd:cd05614    85 DYVSGGELFTHLY-QRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGL----SKEFLTEE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQP---TGSVLWMAPEVIRMQDDNPFSFqsDVYSYGIVLYELMAGELPY 467
Cdd:cd05614   160 KERTysfCGTIEYMAPEIIRGKSGHGKAV--DWWSLGILMFELLTGASPF 207
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
261-467 1.65e-12

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 67.69  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVmlsTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIV 339
Cdd:cd14113     5 FDSFYSEV---AELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQHPQLVgLLDTFETPTSYILV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEGSSLYKHL----HVQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL---TVKIGDFGLATvk 412
Cdd:cd14113    82 LEMADQGRLLDYVvrwgNLTEEKIRFY-----LREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAV-- 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 413 sRWSGSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14113   155 -QLNTTYYIHQLLGSPEFAAPEIIL---GNPVSLTSDLWSIGVLTYVLLSGVSPF 205
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
311-530 1.92e-12

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 67.65  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 311 NEVAVLRKTRHVN--ILLFMGYMTKDNLAIVTQWCEGSSLYKH-LHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRD 387
Cdd:cd14197    57 HEIAVLELAQANPwvINLHEVYETASEMILVLEYAAGGEIFNQcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLD 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 388 MKSNNIFLHEGL---TVKIGDFGLATVksrWSGSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGE 464
Cdd:cd14197   137 LKPQNILLTSESplgDIKIVDFGLSRI---LKNSEELREIMGTPEYVAPEILSYE---PISTATDMWSIGVLAYVMLTGI 210
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 465 LPYahINNRDQIIFM----VGRGYASPDLSRLYKNCPKAMKRLVadcVKKvKEERPlfpqilSSIELLQH 530
Cdd:cd14197   211 SPF--LGDDKQETFLnisqMNVSYSEEEFEHLSESAIDFIKTLL---IKK-PENRA------TAEDCLKH 268
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
58-103 2.32e-12

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 61.76  E-value: 2.32e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759  58 HNFARKTFLKLAFCDICQKFLL----NGFRCQTCGYKFHEHCSTKVPTMC 103
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWglfkQGLKCSDCGLVCHKKCLDKAPSPC 50
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
274-474 2.67e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 68.01  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGDV-AVKILKV-VDPTPEQLQAFRNEVAVLRKTRHVNIL--LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05590     3 LGKGSFGKVMlaRLKESGRLyAVKVLKKdVILQDDDVECTMTEKRILSLARNHPFLtqLYCCFQTPDRLFFVMEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYkhLHVQETK-FQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGlTVKIGDFGLAtvKSRWSGSQQVEQPT 425
Cdd:cd05590    83 LM--FHIQKSRrFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLdHEG-HCKLADFGMC--KEGIFNGKTTSTFC 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 426 GSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHINNRD 474
Cdd:cd05590   158 GTPDYIAPEILQEMLYGP---SVDWWAMGVLLYEMLCGHAPFEAENEDD 203
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
270-474 2.75e-12

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 69.13  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDN--------LA 337
Cdd:PTZ00283   36 ISRVLGSGATGTVLCAKRVSDgepFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVkCHEDFAKKDPrnpenvlmIA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 338 IVTQWCEGSSLYKHLHVQETKFQMFQ-----LIDIarQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVK 412
Cdd:PTZ00283  116 LVLDYANAGDLRQEIKSRAKTNRTFReheagLLFI--QVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMY 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 413 SRWSGSQQVEQPTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPYAHINNRD 474
Cdd:PTZ00283  194 AATVSDDVGRTFCGTPYYVAPEIWRRK---PYSKKADMFSLGVLLYELLTLKRPFDGENMEE 252
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
330-475 2.80e-12

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 67.46  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 YMTKDNLAIVTQWCEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd05606    67 FQTPDKLCFILDLMNGGDLHYHL-SQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 410 TVKSRwsgsqqvEQPTGSV---LWMAPEVIrmQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQ 475
Cdd:cd05606   146 CDFSK-------KKPHASVgthGYMAPEVL--QKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDK 205
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
274-475 2.92e-12

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 67.65  E-value: 2.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPtpEQLQAfRNEVA-------VLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05574     9 LGKGDVGRVYLVRLKGTGKLFAMKVLDK--EEMIK-RNKVKrvltereILATLDHPFLPtLYASFQTSTHLCFVMDYCPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKfqMFQlIDIARQTAQ----GMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT----------- 410
Cdd:cd05574    86 GELFRLLQKQPGK--RLP-EEVARFYAAevllALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtpppvrk 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 411 -VKSRWSGSQQ--------VEQPT-------GSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHiNNRD 474
Cdd:cd05574   163 sLRKGSRRSSVksieketfVAEPSarsnsfvGTEEYIAPEVIK---GDGHGSAVDWWTLGILLYEMLYGTTPFKG-SNRD 238

                  .
gi 1720416759 475 Q 475
Cdd:cd05574   239 E 239
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
346-459 3.66e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 68.77  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT-VKSRWSgSQQVEQP 424
Cdd:PHA03211  244 SDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACfARGSWS-TPFHYGI 322
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720416759 425 TGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYE 459
Cdd:PHA03211  323 AGTVDTNAPEVLA---GDPYTPSVDIWSAGLVIFE 354
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
274-467 3.93e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 67.71  E-value: 3.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV----YKGKwhGDV-AVKILKVVDPTP----EQLQAFRNEVAVLRKTRH---VNilLFMGYMTKDNLAIVTQ 341
Cdd:cd05589     7 LGRGHFGKVllaeYKPT--GELfAIKALKKGDIIArdevESLMCEKRIFETVNSARHpflVN--LFACFQTPEHVCFVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHvqETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGLtVKIGDFGLAtvKSRWSGSQQ 420
Cdd:cd05589    83 YAAGGDLMMHIH--EDVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLdTEGY-VKIADFGLC--KEGMGFGDR 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 421 VEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05589   158 TSTFCGTPEFLAPEVLT---DTSYTRAVDWWGLGVLIYEMLVGESPF 201
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
269-483 4.58e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 66.96  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 269 MLSTRIGSGSFGT----VYKGKwHGDVAVKILKVVDPTPEQlqafrnEVAVL-RKTRHVNILLFMG-YMTKDNLAIVTQW 342
Cdd:cd14178     6 EIKEDIGIGSYSVckrcVHKAT-STEYAVKIIDKSKRDPSE------EIEILlRYGQHPNIITLKDvYDDGKFVYLVMEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 343 CEGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL----TVKIGDFGLAtvKSRWSGS 418
Cdd:cd14178    79 MRGGELLDRI-LRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFA--KQLRAEN 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 419 QQVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAH--INNRDQIIFMVGRG 483
Cdd:cd14178   156 GLLMTPCYTANFVAPEVLKRQG---YDAACDIWSLGILLYTMLAGFTPFANgpDDTPEEILARIGSG 219
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
326-518 4.91e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 66.66  E-value: 4.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 326 LFMGYMTKDNLAIVTQWCEG---SSLYKHlhvqetkfqMFQL-IDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHE 397
Cdd:cd05609    65 MYCSFETKRHLCMVMEYVEGgdcATLLKN---------IGPLpVDMARmyfaETVLALEYLHSYGIVHRDLKPDNLLITS 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 398 GLTVKIGDFGLATV------KSRWSGSQQVE-------QPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGE 464
Cdd:cd05609   136 MGHIKLTDFGLSKIglmsltTNLYEGHIEKDtrefldkQVCGTPEYIAPEVILRQG---YGKPVDWWAMGIILYEFLVGC 212
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 465 LP---------YAHINNrDQIIFMVGRGYASPD----LSRLYKNCPkaMKRLVADCVKKVKEErPLF 518
Cdd:cd05609   213 VPffgdtpeelFGQVIS-DEIEWPEGDDALPDDaqdlITRLLQQNP--LERLGTGGAEEVKQH-PFF 275
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
287-531 5.23e-12

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 66.23  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 287 WHGDVAVKILKVVDPTP--------EQLQAFRNEVAVLRKTRHVNILLFMGY----MTKDN---LAIVTQWCEGSSLYKH 351
Cdd:cd14012    15 VVLDNSKKPGKFLTSQEyfktsngkKQIQLLEKELESLKKLRHPNLVSYLAFsierRGRSDgwkVYLLTEYAPGGSLSEL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 352 LHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL----HEGlTVKIGDFGLATVKSR--WSGSQQVEQPT 425
Cdd:cd14012    95 LD-SVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLdrdaGTG-IVKLTDYSLGKTLLDmcSRGSLDEFKQT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 gsvLWMAPEVIRMqdDNPFSFQSDVYSYGIVLYELMAGelpyAHINNRdqiifmvgrgYASPDLSRLYKNCPKAMKRLVA 505
Cdd:cd14012   173 ---YWLPPELAQG--SKSPTRKTDVWDLGLLFLQMLFG----LDVLEK----------YTSPNPVLVSLDLSASLQDFLS 233
                         250       260
                  ....*....|....*....|....*.
gi 1720416759 506 DCVKKVKEERPlfpqilSSIELLQHS 531
Cdd:cd14012   234 KCLSLDPKKRP------TALELLPHE 253
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
265-475 5.32e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 66.58  E-value: 5.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 265 ASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILK-----VVDPTPEQlQAFRnEV---AVLRKTRHVnILLFMGYMTKDNL 336
Cdd:cd14138     4 ATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKrskkpLAGSVDEQ-NALR-EVyahAVLGQHSHV-VRYYSAWAEDDHM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGSSL-------YKHLHVqetkFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL----------HEG- 398
Cdd:cd14138    81 LIQNEYCNGGSLadaisenYRIMSY----FTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaasEEGd 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 399 --------LTVKIGDFGLATVKSrwsgSQQVEQptGSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGE-LPyah 469
Cdd:cd14138   157 edewasnkVIFKIGDLGHVTRVS----SPQVEE--GDSRFLANEV--LQENYTHLPKADIFALALTVVCAAGAEpLP--- 225

                  ....*.
gi 1720416759 470 iNNRDQ 475
Cdd:cd14138   226 -TNGDQ 230
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
274-483 5.35e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 66.59  E-value: 5.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGT----VYKGKwHGDVAVKILKVVDPTPEQlqafrnEVAVLRK-TRHVNILLFMG-YMTKDNLAIVTQWCEGSS 347
Cdd:cd14175     9 IGVGSYSVckrcVHKAT-NMEYAVKVIDKSKRDPSE------EIEILLRyGQHPNIITLKDvYDDGKHVYLVTELMRGGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI-FLHEG---LTVKIGDFGLAtvKSRWSGSQQVEQ 423
Cdd:cd14175    82 LLDKI-LRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNIlYVDESgnpESLRICDFGFA--KQLRAENGLLMT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 424 PTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAH--INNRDQIIFMVGRG 483
Cdd:cd14175   159 PCYTANFVAPEVLKRQG---YDEGCDIWSLGILLYTMLAGYTPFANgpSDTPEEILTRIGSG 217
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
274-519 5.48e-12

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 66.08  E-value: 5.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSL---Y 349
Cdd:cd14108    10 IGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRvVIIVTELCHEELLeriT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQmfqliDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT--VKIGDFGLAtvKSRWSGSQQVEQpTGS 427
Cdd:cd14108    90 KRPTVCESEVR-----SYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNA--QELTPNEPQYCK-YGT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 428 VLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIifMVGRGYASPDLSRLYKN-CPKA----MKR 502
Cdd:cd14108   162 PEFVAPEIV---NQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTL--MNIRNYNVAFEESMFKDlCREAkgfiIKV 236
                         250
                  ....*....|....*..
gi 1720416759 503 LVADCVKKVKEERPLFP 519
Cdd:cd14108   237 LVSDRLRPDAEETLEHP 253
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
270-483 6.22e-12

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 66.58  E-value: 6.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFgTVYKGKWHG----DVAVKILKVVDPTPEQlqafrnEVAVL-RKTRHVNILLFMG-YMTKDNLAIVTQWC 343
Cdd:cd14177     8 LKEDIGVGSY-SVCKRCIHRatnmEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDvYDDGRYVYLVTELM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL----TVKIGDFGLAtvKSRWSGSQ 419
Cdd:cd14177    81 KGGELLDRI-LRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFA--KQLRGENG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720416759 420 QVEQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNR--DQIIFMVGRG 483
Cdd:cd14177   158 LLLTPCYTANFVAPEVLMRQG---YDAACDIWSLGVLLYTMLAGYTPFANGPNDtpEEILLRIGSG 220
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
274-467 7.23e-12

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 67.34  E-value: 7.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTpEQLQafRNEVAVLRKTRHVNI--------LLFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05624    80 IGRGAFGEVAVVKMKNTERIYAMKILNKW-EMLK--RAETACFREERNVLVngdcqwitTLHYAFQDENYLYLVMDYYVG 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLhvqeTKFQMFQLIDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlATVKSRWSGSQQV 421
Cdd:cd05624   157 GDLLTLL----SKFEDKLPEDMARfyigEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG-SCLKMNDDGTVQS 231
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720416759 422 EQPTGSVLWMAPEVIRMQDD--NPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05624   232 SVAVGTPDYISPEILQAMEDgmGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
274-475 8.36e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 66.61  E-value: 8.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM--TKDNLAIVTQWCEG 345
Cdd:cd14223     8 IGRGGFGEVYgcrkadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAfhTPDKLSFILDLMNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsgsQQVEQPT 425
Cdd:cd14223    88 GDLHYHLS-QHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSK----KKPHASV 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 GSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQ 475
Cdd:cd14223   163 GTHGYMAPEV--LQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 210
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
274-530 1.11e-11

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 65.52  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwHGD----VAVKI-LKVVDPTPEQLQAFRnEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd07846     9 VGEGSYGMVMKCR-HKEtgqiVAIKKfLESEDDKMVKKIAMR-EIKMLKQLRHENLVnLIEVFRRKKRWYLVFEFVDHTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 L-----YKH-LHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAT----------- 410
Cdd:cd07846    87 LddlekYPNgLDESRVRKYLFQIL-------RGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlaapgevytd 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 411 -VKSRWsgsqqveqptgsvlWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGElPY----------AHINN------- 472
Cdd:cd07846   160 yVATRW--------------YRAPEL--LVGDTKYGKAVDVWAVGCLVTEMLTGE-PLfpgdsdidqlYHIIKclgnlip 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720416759 473 RDQIIFM---VGRGYASPD------LSRLYKNCPKAMKRLVADCVKKVKEERPlfpqilSSIELLQH 530
Cdd:cd07846   223 RHQELFQknpLFAGVRLPEvkevepLERRYPKLSGVVIDLAKKCLHIDPDKRP------SCSELLHH 283
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
274-467 1.14e-11

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 66.96  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTpEQLQafRNEVAVLRKTRHVNI--------LLFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05623    80 IGRGAFGEVAVVKLKNADKVFAMKILNKW-EMLK--RAETACFREERDVLVngdsqwitTLHYAFQDDNNLYLVMDYYVG 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLhvqeTKFQMFQLIDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlATVKSRWSGSQQV 421
Cdd:cd05623   157 GDLLTLL----SKFEDRLPEDMARfylaEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFG-SCLKLMEDGTVQS 231
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720416759 422 EQPTGSVLWMAPEVIRMQDDNPFSF--QSDVYSYGIVLYELMAGELPY 467
Cdd:cd05623   232 SVAVGTPDYISPEILQAMEDGKGKYgpECDWWSLGVCMYEMLYGETPF 279
pknD PRK13184
serine/threonine-protein kinase PknD;
329-506 1.36e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 67.49  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 329 GYMTKDNLAIVTQwCEgsSLYKHLHVQETkfqMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL 408
Cdd:PRK13184   86 GYTLKSLLKSVWQ-KE--SLSKELAEKTS---VGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 409 ATVKS-------------RWSGSQQVEQP---TGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAH--- 469
Cdd:PRK13184  160 AIFKKleeedlldidvdeRNICYSSMTIPgkiVGTPDYMAPERLL---GVPASESTDIYALGVILYQMLTLSFPYRRkkg 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720416759 470 --INNRDQIIF---MVGRGYASPDLSRLykncpkAMKRLVAD 506
Cdd:PRK13184  237 rkISYRDVILSpieVAPYREIPPFLSQI------AMKALAVD 272
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
270-520 1.42e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 66.60  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 270 LSTRIGSGSFGTVYKG---KWHGDVAVKilKVV-DPtpeqlQAFRNEVAVLRKTRHVNILLFMGYM----TKDN-----L 336
Cdd:PTZ00036   70 LGNIIGNGSFGVVYEAiciDTSEKVAIK--KVLqDP-----QYKNRELLIMKNLNHINIIFLKDYYytecFKKNeknifL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 337 AIVTQWCEGS--SLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL-TVKIGDFGLAtvKS 413
Cdd:PTZ00036  143 NVVMEFIPQTvhKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNThTLKLCDFGSA--KN 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RWSGSQQVEQpTGSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVgRGYASPDLSRLy 493
Cdd:PTZ00036  221 LLAGQRSVSY-ICSRFYRAPEL--MLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRII-QVLGTPTEDQL- 295
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720416759 494 kncpKAMKRLVADcVK----KVKEERPLFPQ 520
Cdd:PTZ00036  296 ----KEMNPNYAD-IKfpdvKPKDLKKVFPK 321
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
274-460 1.49e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 65.44  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK--WHGDVAVKILKVVDPTPEQ---LQAFRnEVAVLRKTR---HVNILLFMGYMT------KDNLAIV 339
Cdd:cd07862     9 IGEGAYGKVFKARdlKNGGRFVALKRVRVQTGEEgmpLSTIR-EVAVLRHLEtfeHPNVVRLFDVCTvsrtdrETKLTLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 340 TQWCEgSSLYKHLH-VQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgS 418
Cdd:cd07862    88 FEHVD-QDLTTYLDkVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYS----F 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 419 QQVEQPTGSVLWM-APEVIrMQddNPFSFQSDVYSYGIVLYEL 460
Cdd:cd07862   163 QMALTSVVVTLWYrAPEVL-LQ--SSYATPVDLWSVGCIFAEM 202
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
274-407 1.51e-11

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 62.07  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK--GKWHG-DVAVKILKVVdpTPEQLQAFRNEVAVLRKTR--HVNILLFMGYMTKDN-LAIVTQWCEGSS 347
Cdd:cd13968     1 MGEGASAKVFWaeGECTTiGVAVKIGDDV--NNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGpNILLMELVKGGT 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLhvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG 407
Cdd:cd13968    79 LIAYT--QEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
276-467 1.51e-11

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 64.88  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 276 SGSFGTVYKGKWHGDVAVKILKVVDPtpeqlQAFRN-EVAV---LRKTRHVnILLFMGYMTKDNLAIVTQWCEGSSLY-- 349
Cdd:PHA03390   26 DGKFGKVSVLKHKPTQKLFVQKIIKA-----KNFNAiEPMVhqlMKDNPNF-IKLYYSVTTLKGHVLIMDYIKDGDLFdl 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 ----KHLHVQETKFQMFQLIDiarqtaqGMDYLHAKNIIHRDMKSNNIFLHEGLT-VKIGDFGLatvksrwsgSQQVEQP 424
Cdd:PHA03390  100 lkkeGKLSEAEVKKIIRQLVE-------ALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGL---------CKIIGTP 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759 425 T---GSVLWMAPEVIRMQdDNPFSFqsDVYSYGIVLYELMAGELPY 467
Cdd:PHA03390  164 ScydGTLDYFSPEKIKGH-NYDVSF--DWWAVGVLTYELLTGKHPF 206
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
274-475 1.67e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 65.85  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY------KGKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM--TKDNLAIVTQWCEG 345
Cdd:cd05633    13 IGRGGFGEVYgcrkadTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAfhTPDKLCFILDLMNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwsgsQQVEQPT 425
Cdd:cd05633    93 GDLHYHLS-QHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK----KKPHASV 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 426 GSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQ 475
Cdd:cd05633   168 GTHGYMAPEV--LQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 215
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
272-467 1.84e-11

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 65.77  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVY--KGKWHGDV-AVKILK---VVDPtpEQLQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCE 344
Cdd:cd05573     7 KVIGRGAFGEVWlvRDKDTGQVyAMKILRksdMLKR--EQIAHVRAERDILADADSPWIVrLHYAFQDEDHLYLVMEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLhvqeTKFQMFQlIDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRWSGSQQ 420
Cdd:cd05573    85 GGDLMNLL----IKYDVFP-EETARfyiaELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCT-KMNKSGDRE 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 421 VEQ----------------------------PTGSVLWMAPEVIRMQddnPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05573   159 SYLndsvntlfqdnvlarrrphkqrrvraysAVGTPDYIAPEVLRGT---GYGPECDWWSLGVILYEMLYGFPPF 230
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-467 1.85e-11

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 65.28  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWH---GDVAVKILKvvdptpEQLQAF-RNEVAVLRKTR-HVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd14180    14 LGEGSFSVCRKCRHRqsgQEYAVKIIS------RRMEANtQREVAALRLCQsHPNIVaLHEVLHDQYHTYLVMELLRGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLAtvKSRWSGSQQVEQP 424
Cdd:cd14180    88 LLDRIKKKA-RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFA--RLRPQGSRPLQTP 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 425 TGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14180   165 CFTLQYAAPELFSNQG---YDESCDLWSLGVILYTMLSGQVPF 204
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
274-463 2.16e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 64.86  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDV-AVKILKVVDPT-PEQLQAF-RNEVAVLRKTRHVNILLFMGYMTKDNL-AIVTQWCEGSSLY 349
Cdd:cd14157     1 ISEGTFADIYKGYRHGKQyVIKRLKETECEsPKSTERFfQTEVQICFRCCHPNILPLLGFCVESDChCLIYPYMPNGSLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 350 KHLHVQETKFQM--FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL----ATVKSRWSGSQ---- 419
Cdd:cd14157    81 DRLQQQGGSHPLpwEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGLrlcpVDKKSVYTMMKtkvl 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 420 QVEQPtgsvlWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAG 463
Cdd:cd14157   161 QISLA-----YLPEDFVR---HGQLTEKVDIFSCGVVLAEILTG 196
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
273-529 2.22e-11

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 64.62  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKilKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGY------MTKDNLAIVTQWC 343
Cdd:cd13986     7 LLGEGGFSFVYLVedlSTGRLYALK--KILCHSKEDVKEAMREIENYRLFNHPNILRLLDSqivkeaGGKKEVYLLLPYY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLH---VQETKFQMFQLIDIARQTAQGMDYLHAKNII---HRDMKSNNIFLHEGLTVKIGDFGlATVKSRW-- 415
Cdd:cd13986    85 KRGSLQDEIErrlVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLG-SMNPARIei 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 416 SGSQQVEQ------PTGSVLWMAPEVIRMQDDNPFSFQSDVYSYGIVLYELMAGELPYAHINNR-DQIIFMVGRGYASPD 488
Cdd:cd13986   164 EGRREALAlqdwaaEHCTMPYRAPELFDVKSHCTIDEKTDIWSLGCTLYALMYGESPFERIFQKgDSLALAVLSGNYSFP 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720416759 489 LSRLYkncPKAMKRLVADCVKKVKEERPLFPQILSSIELLQ 529
Cdd:cd13986   244 DNSRY---SEELHQLVKSMLVVNPAERPSIDDLLSRVHDLI 281
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
274-467 2.57e-11

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 65.28  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDptpEQLQAFRNEVAVLRKTRhvNIL-------------LFMGYMTKDNLAIVT 340
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLS---KKVIVAKKEVAHTIGER--NILvrtaldespfivgLKFSFQTPTDLYLVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLH------VQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSR 414
Cdd:cd05586    76 DYMSGGELFWHLQkegrfsEDRAKFYIAELV-------LALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS--KAD 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05586   147 LTDNKTTNTFCGTTEYLAPEV--LLDEKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
274-474 2.60e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 65.44  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPT----PEQLQAFRNEVAVLRKTRHVNIL--LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05618    28 IGRGSYAKVLLVRLKKTERIYAMKVVKKElvndDEDIDWVQTEKHVFEQASNHPFLvgLHSCFQTESRLFFVIEYVNGGD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS 427
Cdd:cd05618   108 LMFHMQRQR-KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMC--KEGLRPGDTTSTFCGT 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 428 VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRD 474
Cdd:cd05618   185 PNYIAPEILRGED---YGFSVDWWALGVLMFEMMAGRSPFDIVGSSD 228
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
273-469 2.63e-11

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 64.56  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKGKWHGDVAVKILK-----VVDPTPEQLqAFRnEV---AVLRKTRHVnILLFMGYMTKDNLAIVTQWCE 344
Cdd:cd14139     7 KIGVGEFGSVYKCIKRLDGCVYAIKrsmrpFAGSSNEQL-ALH-EVyahAVLGHHPHV-VRYYSAWAEDDHMIIQNEYCN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQETKFQMF---QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTV-------------------- 401
Cdd:cd14139    84 GGSLQDAISENTKSGNHFeepELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKMQSssgvgeevsneedeflsanv 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 402 --KIGDFGLATVKSrwsgSQQVEQptGSVLWMAPEVirMQDDNPFSFQSDVYSYGIVLyELMAGELPYAH 469
Cdd:cd14139   164 vyKIGDLGHVTSIN----KPQVEE--GDSRFLANEI--LQEDYRHLPKADIFALGLTV-ALAAGAEPLPT 224
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
274-506 2.84e-11

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 64.73  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK-----GKWHGDV-AVKILKVVDPTPEQ-----LQAFRNevaVLRKTRHVNIL-LFMGYMTKDNLAIVTQ 341
Cdd:cd05584     4 LGKGGYGKVFQvrkttGSDKGKIfAMKVLKKASIVRNQkdtahTKAERN---ILEAVKHPFIVdLHYAFQTGGKLYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEGSSLYKHLHVQ------ETKFQMFQlIDIArqtaqgMDYLHAKNIIHRDMKSNNIFL-HEGlTVKIGDFGLAtvKSR 414
Cdd:cd05584    81 YLSGGELFMHLEREgifmedTACFYLAE-ITLA------LGHLHSLGIIYRDLKPENILLdAQG-HVKLTDFGLC--KES 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSQQVEQPTGSVLWMAPEVIRMQDDNPfsfQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRG------YASPD 488
Cdd:cd05584   151 IHDGTVTHTFCGTIEYMAPEILTRSGHGK---AVDWWSLGALMYDMLTGAPPFTA-ENRKKTIDKILKGklnlppYLTNE 226
                         250
                  ....*....|....*...
gi 1720416759 489 LSRLYKncpKAMKRLVAD 506
Cdd:cd05584   227 ARDLLK---KLLKRNVSS 241
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
274-467 3.35e-11

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 64.68  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYK---GKWHGDVAVKILKvvdptpEQLQA-FRNEVAVLRKTR-HVNIL-LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd14179    15 LGEGSFSICRKclhKKTNQEYAVKIVS------KRMEAnTQREIAALKLCEgHPNIVkLHEVYHDQLHTFLVMELLKGGE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLATVKSrwSGSQQVEQP 424
Cdd:cd14179    89 LLERIK-KKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKP--PDNQPLKTP 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720416759 425 TGSVLWMAPEVIrmqDDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14179   166 CFTLHYAAPELL---NYNGYDESCDLWSLGVILYTMLSGQVPF 205
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
274-474 4.49e-11

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 64.44  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILK----VVDPTPEQLQAFRNEVAVLRKTRHVNILlFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05591     3 LGKGSFGKVMLAERKGTdevYAIKVLKkdviLQDDDVDCTMTEKRILALAAKHPFLTAL-HSCFQTKDRLFFVMEYVNGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 347 SLYkhLHVQET-KFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPT 425
Cdd:cd05591    82 DLM--FQIQRArKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMC--KEGILNGKTTTTFC 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720416759 426 GSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHINNRD 474
Cdd:cd05591   158 GTPDYIAPEILQELE---YGPSVDWWALGVLMYEMMAGQPPFEADNEDD 203
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
261-476 5.26e-11

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 64.15  E-value: 5.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 261 WEIEASEVMLsTRIGSGSFGTVYKG---KWHGDVAVKilKVVDPTPEQL---QAFRnEVAVLRKTRHVNIL--------- 325
Cdd:cd07879    11 WELPERYTSL-KQVGSGAYGSVCSAidkRTGEKVAIK--KLSRPFQSEIfakRAYR-ELTLLKHMQHENVIglldvftsa 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 326 ----------LFMGYMTKDNLAIVTqwcegsslykhLHVQETKFQMfqlidIARQTAQGMDYLHAKNIIHRDMKSNNIFL 395
Cdd:cd07879    87 vsgdefqdfyLVMPYMQTDLQKIMG-----------HPLSEDKVQY-----LVYQMLCGLKYIHSAGIIHRDLKPGNLAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 396 HEGLTVKIGDFGLAtvksRWSGSQQveqpTGSVL---WMAPEVIR--MQddnpFSFQSDVYSYGIVLYELMAGELPYAHI 470
Cdd:cd07879   151 NEDCELKILDFGLA----RHADAEM----TGYVVtrwYRAPEVILnwMH----YNQTVDIWSVGCIMAEMLTGKTLFKGK 218

                  ....*.
gi 1720416759 471 NNRDQI 476
Cdd:cd07879   219 DYLDQL 224
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
274-550 5.56e-11

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 63.93  E-value: 5.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKV----VDPTPEQLQAFR-NEVAVLRKTRHVNILLFMGYMT--KDNLAIVTQWC 343
Cdd:cd14041    14 LGRGGFSEVYKAfdlTEQRYVAVKIHQLnknwRDEKKENYHKHAcREYRIHKELDHPRIVKLYDYFSldTDSFCTVLEYC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLT---VKIGDFGLATVK-----S 413
Cdd:cd14041    94 EGNDLDFYLK-QHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTAcgeIKITDFGLSKIMdddsyN 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 414 RWSGSQQVEQPTGSVLWMAPEVIRMQDDNP-FSFQSDVYSYGIVLYELMAGELPYAHiNNRDQIIFMVGRGYASPDLSRL 492
Cdd:cd14041   173 SVDGMELTSQGAGTYWYLPPECFVVGKEPPkISNKVDVWSVGVIFYQCLYGRKPFGH-NQSQQDILQENTILKATEVQFP 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 493 YKN--CPKAmKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKInrSASEPSLHRAAHT 550
Cdd:cd14041   252 PKPvvTPEA-KAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSV--STSSPAGAAVAST 308
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
264-436 6.15e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 63.54  E-value: 6.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 264 EASEVMLSTRIGSGSFGTVYKG--KWHGD-VAVKILKVVDPT---PeqLQAFRnEVAVLRKTRHVNILLF---------M 328
Cdd:cd07865    10 EVSKYEKLAKIGQGTFGEVFKArhRKTGQiVALKKVLMENEKegfP--ITALR-EIKILQLLKHENVVNLieicrtkatP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 329 GYMTKDNLAIVTQWCEgSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGL 408
Cdd:cd07865    87 YNRYKGSIYLVFEFCE-HDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGL 165
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720416759 409 ATVKSRwSGSQQVEQPTGSV--LWM-APEVI 436
Cdd:cd07865   166 ARAFSL-AKNSQPNRYTNRVvtLWYrPPELL 195
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
273-466 6.93e-11

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 62.62  E-value: 6.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG--KWHGDVAVKI-----LKVVDPT--PEQLQafrNEVAVLRKTR-HVNIllfMGYMT----KDNLAI 338
Cdd:cd14019     8 KIGEGTFSSVYKAedKLHDLYDRNKgrlvaLKHIYPTssPSRIL---NELECLERLGgSNNV---SGLITafrnEDQVVA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 339 VTQWCEGSS---LYKHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNiFLH-----EGLTVkigDFGLAt 410
Cdd:cd14019    82 VLPYIEHDDfrdFYRKMSLTDIRIYLRNLF-------KALKHVHSFGIIHRDVKPGN-FLYnretgKGVLV---DFGLA- 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720416759 411 vkSRWSGSQQVEQP-TGSVLWMAPEVI-RMQDdnpfsfQS---DVYSYGIVLYELMAGELP 466
Cdd:cd14019   150 --QREEDRPEQRAPrAGTRGFRAPEVLfKCPH------QTtaiDIWSAGVILLSILSGRFP 202
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
58-103 8.62e-11

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 57.33  E-value: 8.62e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720416759  58 HNFARKTFLkLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMC 103
Cdd:cd20812     3 HRFSKKLFM-RQTCDYCHKQMFFGLKCKDCKYKCHKKCAKKAPPSC 47
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
274-480 9.73e-11

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 63.54  E-value: 9.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV------YKGKwhgDVAVKilKVVDPTPEQLQAFRN--EVAVLRKTRHVNILLFMG-YMTKDNLAivtqwcE 344
Cdd:cd07855    13 IGSGAYGVVcsaidtKSGQ---KVAIK--KIPNAFDVVTTAKRTlrELKILRHFKHDNIIAIRDiLRPKVPYA------D 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHLHVQET-----------------KFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFG 407
Cdd:cd07855    82 FKDVYVVLDLMESdlhhiihsdqpltlehiRYFLYQLL-------RGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 408 LAtvksRWSGSQQVEQP---TGSV--LWM-APEVIrmqddnpFSFQS-----DVYSYGIVLYElMAGE---LPYAHINNR 473
Cdd:cd07855   155 MA----RGLCTSPEEHKyfmTEYVatRWYrAPELM-------LSLPEytqaiDMWSVGCIFAE-MLGRrqlFPGKNYVHQ 222

                  ....*..
gi 1720416759 474 DQIIFMV 480
Cdd:cd07855   223 LQLILTV 229
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
274-480 1.01e-10

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 63.50  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPT----PEQLQAFRNEVAVLRKTRHVNIL--LFMGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05617    23 IGRGSYAKVLLVRLKKNDQIYAMKVVKKElvhdDEDIDWVQTEKHVFEQASSNPFLvgLHSCFQTTSRLFLVIEYVNGGD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQEtKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS 427
Cdd:cd05617   103 LMFHMQRQR-KLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMC--KEGLGPGDTTSTFCGT 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 428 VLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYAHIN-----NRDQIIFMV 480
Cdd:cd05617   180 PNYIAPEILRGEE---YGFSVDWWALGVLMFEMMAGRSPFDIITdnpdmNTEDYLFQV 234
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
274-464 1.02e-10

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 63.48  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKwHGDVAVKI-LKVVDPTPEQLQAFRN--EVAVLRKTRHVNILLFMGYMTKDNLA------IVTQWCE 344
Cdd:cd07849    13 IGEGAYGMVCSAV-HKPTGQKVaIKKISPFEHQTYCLRTlrEIKILLRFKHENIIGILDIQRPPTFEsfkdvyIVQELME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 gSSLYKHLHVQETKFQMFQLIdiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqQVEQP 424
Cdd:cd07849    92 -TDLYKLIKTQHLSNDHIQYF--LYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIAD------PEHDH 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 425 TG------SVLWM-APEVirMQDDNPFSFQSDVYSYGIVLYELMAGE 464
Cdd:cd07849   163 TGflteyvATRWYrAPEI--MLNSKGYTKAIDIWSVGCILAEMLSNR 207
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
295-522 1.18e-10

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 62.62  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 295 ILKVVDPTPEQLQ-AFRNEVAVLRKTRHVNILLFMGYMTKDNLAI-VTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTA 372
Cdd:cd05076    47 VLKVLDPSHHDIAlAFFETASLMSQVSHTHLVFVHGVCVRGSENImVEEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 373 QGMDYLHAKNIIHRDMKSNNIF-----LHEGLT--VKIGDFGLA-TVKSRwsgSQQVEQptgsVLWMAPEVIRmqDDNPF 444
Cdd:cd05076   127 SALSYLENKNLVHGNVCAKNILlarlgLEEGTSpfIKLSDPGVGlGVLSR---EERVER----IPWIAPECVP--GGNSL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 445 SFQSDVYSYGIVLYEL-MAGELPYahinnrdqiifmvgRGYASPDLSRLYK--------NCPKaMKRLVADCVKKVKEER 515
Cdd:cd05076   198 STAADKWGFGATLLEIcFNGEAPL--------------QSRTPSEKERFYQrqhrlpepSCPE-LATLISQCLTYEPTQR 262

                  ....*..
gi 1720416759 516 PLFPQIL 522
Cdd:cd05076   263 PSFRTIL 269
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
273-466 1.63e-10

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 62.65  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG---KWHGDVAVKILKvvdPTPEQLQAFRNEVAVLR--------KTRHVNILLFMGYMTKDNLAIVTQ 341
Cdd:cd14212     6 LLGQGTFGQVVKCqdlKTNKLVAVKVLK---NKPAYFRQAMLEIAILTllntkydpEDKHHIVRLLDHFMHHGHLCIVFE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 wCEGSSLYKHLhvQETKFQMFQLIDI---ARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT--VKIGDFGLATVKsrws 416
Cdd:cd14212    83 -LLGVNLYELL--KQNQFRGLSLQLIrkfLQQLLDALSVLKDARIIHCDLKPENILLVNLDSpeIKLIDFGSACFE---- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 417 gSQQVEQPTGSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGeLP 466
Cdd:cd14212   156 -NYTLYTYIQSRFYRSPEVLL---GLPYSTAIDMWSLGCIAAELFLG-LP 200
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
291-501 1.64e-10

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 62.58  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 291 VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGSSLYKHLHVQETKFQMFQLI-DIA 368
Cdd:cd08226    28 VTVKITNLDNCSEEHLKALQNEVVLSHFFRHPNIMTHWTVFTEGSwLWVISPFMAYGSARGLLKTYFPEGMNEALIgNIL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 369 RQTAQGMDYLHAKNIIHRDMKSNNIFLH-EGLTVKIGDFGLATVKSRWSGSQQV---EQPTGSVL-WMAPEVIRmQDDNP 443
Cdd:cd08226   108 YGAIKALNYLHQNGCIHRSVKASHILISgDGLVSLSGLSHLYSMVTNGQRSKVVydfPQFSTSVLpWLSPELLR-QDLHG 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720416759 444 FSFQSDVYSYGIVLYELMAGELPYAHInNRDQIIFMVGRGYA-SPDLSRLYKNCPKAMK 501
Cdd:cd08226   187 YNVKSDIYSVGITACELARGQVPFQDM-RRTQMLLQKLKGPPySPLDIFPFPELESRMK 244
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
304-510 1.65e-10

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 62.34  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 304 EQLQAFRNEVAVLRKTRHVNILLFMGYM--TKDNLAIVT------------QWCEGSSLYKH-----LHVQETKFQMFQL 364
Cdd:cd14011    44 QILELLKRGVKQLTRLRHPRILTVQHPLeeSRESLAFATepvfaslanvlgERDNMPSPPPElqdykLYDVEIKYGLLQI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 365 IDiarqtaqGMDYLH-AKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtVKSRWSGSQQ------------VEQPTGSvlWM 431
Cdd:cd14011   124 SE-------ALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFC-ISSEQATDQFpyfreydpnlppLAQPNLN--YL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 432 APEVIRmqdDNPFSFQSDVYSYGIVLYelmagelpyaHINNRDQIIFMVGRGYASPD-----LSRLYKNCPKAMKRLVAD 506
Cdd:cd14011   194 APEYIL---SKTCDPASDMFSLGVLIY----------AIYNKGKPLFDCVNNLLSYKknsnqLRQLSLSLLEKVPEELRD 260

                  ....
gi 1720416759 507 CVKK 510
Cdd:cd14011   261 HVKT 264
PHA02988 PHA02988
hypothetical protein; Provisional
282-527 1.69e-10

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 62.07  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 282 VYKGKWHG-DVAVKILKVVDPTPEQL-QAFRNEVAVLRKTRHVNILLFMGYMTK--DNL---AIVTQWCEGSSLYKHLHv 354
Cdd:PHA02988   36 IYKGIFNNkEVIIRTFKKFHKGHKVLiDITENEIKNLRRIDSNNILKIYGFIIDivDDLprlSLILEYCTRGYLREVLD- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 355 QETKFQMFQLIDIARQTAQGMDYLHAK-NIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrwsgsqqvEQPTGSVLWMAP 433
Cdd:PHA02988  115 KEKDLSFKTKLDMAIDCCKGLYNLYKYtNKPYKNLTSVSFLVTENYKLKIICHGLEKILS--------SPPFKNVNFMVY 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 434 EVIRMQDD--NPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFMVGRGYASPdlsrLYKNCPKAMKRLVADCVKKV 511
Cdd:PHA02988  187 FSYKMLNDifSEYTIKDDIYSLGVVLWEIFTGKIPFENLTTKEIYDLIINKNNSLK----LPLDCPLEIKCIVEACTSHD 262
                         250
                  ....*....|....*.
gi 1720416759 512 KEERPLFPQILSSIEL 527
Cdd:PHA02988  263 SIKRPNIKEILYNLSL 278
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
273-488 2.12e-10

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 61.75  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 273 RIGSGSFGTVYKG--KWHGD-VAVKILKVvDPTPEQL--QAFRnEVAVLRKTRHVNIL-------------LFMGYMTKD 334
Cdd:cd07860     7 KIGEGTYGVVYKArnKLTGEvVALKKIRL-DTETEGVpsTAIR-EISLLKELNHPNIVklldvihtenklyLVFEFLHQD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 335 nLAIVTQWCEGSSLYKHLhvqeTKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksR 414
Cdd:cd07860    85 -LKKFMDASALTGIPLPL----IKSYLFQLL-------QGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLA----R 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 415 WSGSqQVEQPTGSV--LWM-APEVI---RMqddnpFSFQSDVYSYGIVLYELMAGELPYAHINNRDQiIFMVGRGYASPD 488
Cdd:cd07860   149 AFGV-PVRTYTHEVvtLWYrAPEILlgcKY-----YSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQ-LFRIFRTLGTPD 221
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
274-465 2.18e-10

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 62.20  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWH---GDVAVKILKVVDPTPEqlqAFRNEVAVLRKTRHVN-------ILLFMGYMTKDNLAIVTQWC 343
Cdd:cd14134    20 LGEGTFGKVLECWDRkrkRYVAVKIIRNVEKYRE---AAKIEIDVLETLAEKDpngkshcVQLRDWFDYRGHMCIVFELL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 eGSSLYKHLhvQETKFQMF---QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLT-------------------V 401
Cdd:cd14134    97 -GPSLYDFL--KKNNYGPFpleHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYvkvynpkkkrqirvpkstdI 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 402 KIGDFGLATVKsrwsgsqqvEQPTGSVL----WMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGEL 465
Cdd:cd14134   174 KLIDFGSATFD---------DEYHSSIVstrhYRAPEVIL---GLGWSYPCDVWSIGCILVELYTGEL 229
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
274-468 2.45e-10

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 61.94  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY--KGKWHGDV-AVKILKVVDPTPEQLQAFRNE---VAVLRKTRHVNILLFmGYMTKDNLAIVTQWCEGSS 347
Cdd:cd05601     9 IGRGHFGEVQvvKEKATGDIyAMKVLKKSETLAQEEVSFFEEerdIMAKANSPWITKLQY-AFQDSENLYLVMEYHPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 348 LYKHLHVQETKFQMfqliDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRwSGSQQVEQ 423
Cdd:cd05601    88 LLSLLSRYDDIFEE----SMARfylaELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSS-DKTVTSKM 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720416759 424 PTGSVLWMAPEVIRMQDDNP---FSFQSDVYSYGIVLYELMAGELPYA 468
Cdd:cd05601   163 PVGTPDYIAPEVLTSMNGGSkgtYGVECDWWSLGIVAYEMLYGKTPFT 210
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
274-522 2.58e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 62.41  E-value: 2.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFR--NEVAVLRKTRHVNILLFMGYMTKDNLAIvtqwcEGSSL 348
Cdd:cd07874    25 IGSGAQGIVcaaYDAVLDRNVAIK--KLSRPFQNQTHAKRayRELVLMKCVNHKNIISLLNVFTPQKSLE-----EFQDV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLHVQETKF-QMFQL-IDIAR------QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGSQQ 420
Cdd:cd07874    98 YLVMELMDANLcQVIQMeLDHERmsyllyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA----RTAGTSF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 421 VEQP-TGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMagelpyahinnRDQIIFmVGRGYA---SPDLSRLYKNC 496
Cdd:cd07874   174 MMTPyVVTRYYRAPEVILGMG---YKENVDIWSVGCIMGEMV-----------RHKILF-PGRDYIdqwNKVIEQLGTPC 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720416759 497 PKAMKRLvADCVKKVKEERP-----LFPQIL 522
Cdd:cd07874   239 PEFMKKL-QPTVRNYVENRPkyaglTFPKLF 268
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
274-464 4.28e-10

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 61.23  E-value: 4.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGK---WHGDVAVK-ILKVVDPTPEQLQAFRnEVAVLRKTRHVNILLFMGYMT---KDN---LAIVTQWC 343
Cdd:cd07858    13 IGRGAYGIVCSAKnseTNEKVAIKkIANAFDNRIDAKRTLR-EIKLLRHLDHENVIAIKDIMPpphREAfndVYIVYELM 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EgSSLYKHLHVQET------KFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKsrwsg 417
Cdd:cd07858    92 D-TDLHQIIRSSQTlsddhcQYFLYQLL-------RGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTT----- 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 SQQVEQPTGSVL---WMAPEVIRMQDDnpFSFQSDVYSYGIVLYELMAGE 464
Cdd:cd07858   159 SEKGDFMTEYVVtrwYRAPELLLNCSE--YTTAIDVWSVGCIFAELLGRK 206
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
274-414 5.22e-10

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 61.43  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVD----PTPEQLQAFRNEVAVLRKTRHVNilLFMGYMTKDNLAIVTQWCEGS 346
Cdd:cd05610    12 ISRGAFGKVYLGRKKNNsklYAVKVVKKADminkNMVHQVQAERDALALSKSPFIVH--LYYSLQSANNVYLVMEYLIGG 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 347 SLYKHLHVqetkFQMFQLiDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSR 414
Cdd:cd05610    90 DVKSLLHI----YGYFDE-EMAVkyisEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLN 156
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
274-525 5.38e-10

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 60.30  E-value: 5.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVK------ILKVVDPTPEQLQ-AFRNEVAVLRKTRHVNILLFMGY-MTKDNLAIVTQWCEG 345
Cdd:cd14208     7 LGKGSFTKIYRGLRTDEEDDErcetevLLKVMDPTHGNCQeSFLEAASIMSQISHKHLVLLHGVcVGKDSIMVQEFVCHG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 S-SLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL-HEGLT-----VKIGDFGLA-TVKSRwsg 417
Cdd:cd14208    87 AlDLYLKKQQQKGPVAISWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLsREGDKgsppfIKLSDPGVSiKVLDE--- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 418 sqqvEQPTGSVLWMAPEVIRmqDDNPFSFQSDVYSYGIVLYELMA-GELPYAHINNRDQIIFMVGR-GYASPDLSRLykn 495
Cdd:cd14208   164 ----ELLAERIPWVAPECLS--DPQNLALEADKWGFGATLWEIFSgGHMPLSALDPSKKLQFYNDRkQLPAPHWIEL--- 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 1720416759 496 cpkamKRLVADCVKKVKEERPLFPQILSSI 525
Cdd:cd14208   235 -----ASLIQQCMSYNPLLRPSFRAIIRDL 259
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
274-477 7.80e-10

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 60.46  E-value: 7.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKG---KWHGDVAVKILKV----VDPTPEQLQAFR-NEVAVLRKTRHVNILLFMGYMT--KDNLAIVTQWC 343
Cdd:cd14040    14 LGRGGFSEVYKAfdlYEQRYAAVKIHQLnkswRDEKKENYHKHAcREYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 344 EGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKN--IIHRDMKSNNIFLHEGLT---VKIGDFGLATVKSRWS-- 416
Cdd:cd14040    94 EGNDLDFYLK-QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKIMDDDSyg 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 417 --GSQQVEQPTGSVLWMAPEVIRMQDDNP-FSFQSDVYSYGIVLYELMAGELPYAHINNRDQII 477
Cdd:cd14040   173 vdGMDLTSQGAGTYWYLPPECFVVGKEPPkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIL 236
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
272-466 1.02e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 60.07  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 272 TRIGSGSFGTVYK--GKWHGDVAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKD-NLAIVTQWCEGSSL 348
Cdd:cd06650    11 SELGAGNGGVVFKvsHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDgEISICMEHMDGGSL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLH-VQETKFQMFQLIDIArqTAQGMDYLHAKN-IIHRDMKSNNIFLHEGLTVKIGDFGLAtvksrwsgSQQVEQPTG 426
Cdd:cd06650    91 DQVLKkAGRIPEQILGKVSIA--VIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVS--------GQLIDSMAN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720416759 427 SVL----WMAPEviRMQDDNpFSFQSDVYSYGIVLYELMAGELP 466
Cdd:cd06650   161 SFVgtrsYMSPE--RLQGTH-YSVQSDIWSMGLSLVEMAVGRYP 201
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
274-468 1.10e-09

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 60.05  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTpEQLQafRNEVAVLRKTRHVNIL--------LFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05597     9 IGRGAFGEVAVVKLKSTEKVYAMKILNKW-EMLK--RAETACFREERDVLVNgdrrwitkLHYAFQDENYLYLVMDYYCG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLhvqeTKFQMFQLIDIARQTAQGM----DYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlATVKSRWSGSQQV 421
Cdd:cd05597    86 GDLLTLL----SKFEDRLPEEMARFYLAEMvlaiDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-SCLKLREDGTVQS 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQPTGSVLWMAPEVIRMQDDNPFSF--QSDVYSYGIVLYELMAGELP-YA 468
Cdd:cd05597   161 SVAVGTPDYISPEILQAMEDGKGRYgpECDWWSLGVCMYEMLYGETPfYA 210
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
294-465 1.50e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 60.48  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 294 KILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYM-TKDNLAIVTQWCEgSSLYKHLHVQETKFQ----MFQLIDIA 368
Cdd:PHA03210  195 LIAKRVKAGSRAAIQLENEILALGRLNHENILKIEEILrSEANTYMITQKYD-FDLYSFMYDEAFDWKdrplLKQTRAIM 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 369 RQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvksrwsgsqQVEQP--------TGSVLWMAPEVIRmqd 440
Cdd:PHA03210  274 KQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAM---------PFEKEreafdygwVGTVATNSPEILA--- 341
                         170       180
                  ....*....|....*....|....*
gi 1720416759 441 DNPFSFQSDVYSYGIVLYELMAGEL 465
Cdd:PHA03210  342 GDGYCEITDIWSCGLILLDMLSHDF 366
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
275-468 1.52e-09

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 59.62  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 275 GSGSFGTVYKGKWHGD-VAVKILKVVDPTPEQLQAFRNEVAVLRKTRHVNILLFMGYMTKDN-LAIVTQWCE-GSS---L 348
Cdd:cd08216    11 KGGGVVHLAKHKPTNTlVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNdLYVVTPLMAyGSCrdlL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 349 YKHLhvqETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGdfGLATVKSRWSGSQQV----EQP 424
Cdd:cd08216    91 KTHF---PEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLS--GLRYAYSMVKHGKRQrvvhDFP 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 425 TGSV---LWMAPEVIRmQDDNPFSFQSDVYSYGIVLYELMAGELPYA 468
Cdd:cd08216   166 KSSEknlPWLSPEVLQ-QNLLGYNEKSDIYSVGITACELANGVVPFS 211
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
274-521 1.63e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 59.66  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFR--NEVAVLRKTRHVNILLFMGYMTKD-------NLAIVTQ 341
Cdd:cd07876    29 IGSGAQGIVcaaFDTVLGINVAVK--KLSRPFQNQTHAKRayRELVLLKCVNHKNIISLLNVFTPQksleefqDVYLVME 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 342 WCEgSSLYKHLHVQETKFQMFQLIdiaRQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSGSQQV 421
Cdd:cd07876   107 LMD-ANLCQVIHMELDHERMSYLL---YQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA----RTACTNFM 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 422 EQP-TGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPYA---HINNRDQIIFMVGrgyaSPDLsrlykncp 497
Cdd:cd07876   179 MTPyVVTRYYRAPEVILGMG---YKENVDIWSVGCIMGELVKGSVIFQgtdHIDQWNKVIEQLG----TPSA-------- 243
                         250       260
                  ....*....|....*....|....
gi 1720416759 498 KAMKRLVaDCVKKVKEERPLFPQI 521
Cdd:cd07876   244 EFMNRLQ-PTVRNYVENRPQYPGI 266
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
367-465 1.68e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 59.51  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 367 IARQTAQGMDYLHAK-NIIHRDMKSNNIFL-HEGLTVKIGDFGLAT-VKSRWSGSQQVEQptgsvlWMAPEVIRmqdDNP 443
Cdd:cd14136   124 IARQVLQGLDYLHTKcGIIHTDIKPENVLLcISKIEVKIADLGNACwTDKHFTEDIQTRQ------YRSPEVIL---GAG 194
                          90       100
                  ....*....|....*....|..
gi 1720416759 444 FSFQSDVYSYGIVLYELMAGEL 465
Cdd:cd14136   195 YGTPADIWSTACMAFELATGDY 216
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
274-463 1.75e-09

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 59.34  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV----YKGKWHGD-VAVK-ILKVVDPTPEQLQAFRnEVAVLRKTR-HVNI--LLFMGYMTKDNLaivtqwcE 344
Cdd:cd07857     8 LGQGAYGIVcsarNAETSEEEtVAIKkITNVFSKKILAKRALR-ELKLLRHFRgHKNItcLYDMDIVFPGNF-------N 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 GSSLYKHL-------------HVQETKFQMFqlidiARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtv 411
Cdd:cd07857    80 ELYLYEELmeadlhqiirsgqPLTDAHFQSF-----IYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLA-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416759 412 ksRWSGSQQVEQP---TGSV--LWM-APEVirMQDDNPFSFQSDVYSYGIVLYELMAG 463
Cdd:cd07857   153 --RGFSENPGENAgfmTEYVatRWYrAPEI--MLSFQSYTKAIDVWSVGCILAELLGR 206
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
374-467 2.07e-09

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 59.63  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 374 GMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQ-DDNPFSFQSDVYS 452
Cdd:cd05622   184 ALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG-TCMKMNKEGMVRCDTAVGTPDYISPEVLKSQgGDGYYGRECDWWS 262
                          90
                  ....*....|....*
gi 1720416759 453 YGIVLYELMAGELPY 467
Cdd:cd05622   263 VGVFLYEMLVGDTPF 277
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
274-479 2.30e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 59.27  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGD---VAVKILKVVDPTPEQLQAfrnEVAVLRKTRHVN------ILLFMGYMTKDNLAIVTQWCE 344
Cdd:cd14229     8 LGRGTFGQVVKCWKRGTneiVAVKILKNHPSYARQGQI---EVGILARLSNENadefnfVRAYECFQHRNHTCLVFEMLE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 345 gSSLYKHLhvQETKFQMFQLI---DIARQTAQGMDYLHAKNIIHRDMKSNNIFL----HEGLTVKIGDFGLATVKSRWSG 417
Cdd:cd14229    85 -QNLYDFL--KQNKFSPLPLKvirPILQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFGSASHVSKTVC 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416759 418 SQQVEqptgSVLWMAPEVIRmqdDNPFSFQSDVYSYGIVLYELMAGELPYAHINNRDQIIFM 479
Cdd:cd14229   162 STYLQ----SRYYRAPEIIL---GLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYI 216
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
274-467 2.60e-09

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 59.24  E-value: 2.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVYKGKWHGDVAVKILKVVDPTpEQLQafRNEVAVLRKTRHVN--------ILLFMGYMTKDNLAIVTQWCEG 345
Cdd:cd05621    60 IGRGAFGEVQLVRHKASQKVYAMKLLSKF-EMIK--RSDSAFFWEERDIMafanspwvVQLFCAFQDDKYLYMVMEYMPG 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 346 SSLYKHLHVQET--KFQMFQLIDIArqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlATVKSRWSGSQQVEQ 423
Cdd:cd05621   137 GDLVNLMSNYDVpeKWAKFYTAEVV----LALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFG-TCMKMDETGMVHCDT 211
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720416759 424 PTGSVLWMAPEVIRMQ-DDNPFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd05621   212 AVGTPDYISPEVLKSQgGDGYYGRECDWWSVGVFLFEMLVGDTPF 256
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
330-467 3.66e-09

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 57.69  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 YMTKDNLAIVTQWCEGSSLYKHlhVQETKFQMF---QLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKI 403
Cdd:cd14172    70 HHGKRCLLIIMECMEGGELFSR--IQERGDQAFterEASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKL 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416759 404 GDFGLATVKSRWSGSQqveQPTGSVLWMAPEVIRMQDdnpFSFQSDVYSYGIVLYELMAGELPY 467
Cdd:cd14172   148 TDFGFAKETTVQNALQ---TPCYTPYYVAPEVLGPEK---YDKSCDMWSLGVIMYILLCGFPPF 205
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
274-467 3.68e-09

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 58.48  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTVY---KGKWHGDVAVKILKVVDptpeQLQafRNEVAVLRKTRhvNIL----------LFMGYMTKDNLAIVT 340
Cdd:cd05598     9 IGVGAFGEVSlvrKKDTNALYAMKTLRKKD----VLK--RNQVAHVKAER--DILaeadnewvvkLYYSFQDKENLYFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 341 QWCEGSSLYKHLhvqeTKFQMFQLiDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATvKSRW- 415
Cdd:cd05598    81 DYIPGGDLMSLL----IKKGIFEE-DLARfyiaELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCT-GFRWt 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720416759 416 --SGSQQVEQPTGSVLWMAPEVIRMQDDNpfsfQS-DVYSYGIVLYELMAGELPY 467
Cdd:cd05598   155 hdSKYYLAHSLVGTPNYIAPEVLLRTGYT----QLcDWWSVGVILYEMLVGQPPF 205
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
274-522 3.71e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 58.58  E-value: 3.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 274 IGSGSFGTV---YKGKWHGDVAVKilKVVDPTPEQLQAFR--NEVAVLRKTRHVNIL-------------------LFMG 329
Cdd:cd07850     8 IGSGAQGIVcaaYDTVTGQNVAIK--KLSRPFQNVTHAKRayRELVLMKLVNHKNIIgllnvftpqksleefqdvyLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 330 YMTKdNLAIVTQwcegsslyKHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLA 409
Cdd:cd07850    86 LMDA-NLCQVIQ--------MDLDHERMSYLLYQML-------CGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416759 410 tvksRWSGSQQVEQP-TGSVLWMAPEVIR-MqddnPFSFQSDVYSYGIVLYELMAGELPYA---HINNRDQIIFMVGrgy 484
Cdd:cd07850   150 ----RTAGTSFMMTPyVVTRYYRAPEVILgM----GYKENVDIWSVGCIMGEMIRGTVLFPgtdHIDQWNKIIEQLG--- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720416759 485 aSPdlsrlyknCPKAMKRLvADCVKKVKEERP---------LFPQIL 522
Cdd:cd07850   219 -TP--------SDEFMSRL-QPTVRNYVENRPkyagysfeeLFPDVL 255
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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