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Conserved domains on  [gi|656985050|ref|NP_001280645|]
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phosphatidylinositol 4-kinase beta isoform 3 [Mus musculus]

Protein Classification

phosphatidylinositol 4-kinase( domain architecture ID 10142440)

phosphatidylinositol 4-kinase (PI4K) catalyzes the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides

CATH:  1.10.510.10
Gene Ontology:  GO:0004430|GO:0016310|GO:0005524
PubMed:  16244704|16793271
SCOP:  3000066

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 197-484 0e+00

Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIbeta (also called Pik1p in yeast) is a 110 kDa protein that is localized to the Golgi and the nucleus. It is required for maintaining the structural integrity of the Golgi complex (GC), and is a key regulator of protein transport from the GC to the plasma membrane. PI4KIIIbeta also functions in the genesis, transport, and exocytosis of synaptic vesicles. The Drosophila PI4KIIIbeta is essential for cytokinesis during spermatogenesis. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


:

Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 547.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 197 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd05168    1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 277 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 354
Cdd:cd05168   81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 355 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCF--H 432
Cdd:cd05168  161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSKLPCFfgG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 656985050 433 GSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 484
Cdd:cd05168  241 GEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
 
Name Accession Description Interval E-value
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 197-484 0e+00

Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIbeta (also called Pik1p in yeast) is a 110 kDa protein that is localized to the Golgi and the nucleus. It is required for maintaining the structural integrity of the Golgi complex (GC), and is a key regulator of protein transport from the GC to the plasma membrane. PI4KIIIbeta also functions in the genesis, transport, and exocytosis of synaptic vesicles. The Drosophila PI4KIIIbeta is essential for cytokinesis during spermatogenesis. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 547.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 197 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd05168    1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 277 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 354
Cdd:cd05168   81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 355 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCF--H 432
Cdd:cd05168  161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSKLPCFfgG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 656985050 433 GSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 484
Cdd:cd05168  241 GEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 229-434 1.77e-69

Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in a variety of processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, and apoptosis. These homologues may be either lipid kinases and/or protein kinases: the former phosphorylate the 3-position in the inositol ring of inositol phospholipids. The ataxia telangiectesia-mutated gene produced, the targets of rapamycin (TOR) and the DNA-dependent kinase have not been found to possess lipid kinase activity. Some of this family possess PI-4 kinase activities.


Pssm-ID: 214538 [Multi-domain]  Cd Length: 240  Bit Score: 221.40  E-value: 1.77e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050   229 VIVKCGDDLRQELLAFQVLKQLQSIWEQE----RVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS---------- 294
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYrkqkgkvldl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050   295 ----------------------QLSLLDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGH 352
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPDPS-EDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGH 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050   353 IIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCF 431
Cdd:smart00146 160 LFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELM-LYDGLPDW 236


                   ...
gi 656985050   432 HGS 434
Cdd:smart00146 237 RSG 239
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
211-483 1.02e-59

Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 212.72  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  211 RIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIW----EQERVPLWIKPYKILVISADSGMIEPVVNAVS 286
Cdd:COG5032  1781 LQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDT 1860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  287 IHQVKK------------QSQL-------------------------SLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYC 329
Cdd:COG5032  1861 LHSILReyhkrknisidqEKKLaarldnlklllkdefftkatlksppVLYDWFSESFPNP--EDWLTARTNFARSLAVYS 1938

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  330 LVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGGLNGDMFnyYKMLMLQGLIA 407
Cdd:COG5032  1939 VIGYILGLGDRHPGNILIDrSSGHVIHIDFGFILFNAPGRFPFpEKVPFRLTRNIVEAMGVSGVEGS--FRELCETAFRA 2016

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  408 ARKHMDKVVQIVEIMQ-----QGSQLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLT 480
Cdd:COG5032  2017 LRKNADSLMNVLELFVrdpliEWRRLPCFREIQnnEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLAT 2096


                  ...
gi 656985050  481 NGI 483
Cdd:COG5032  2097 MYI 2099
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 228-422 4.84e-40

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 144.39  E-value: 4.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  228 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLW-IKPYKILVISADSGMIEPVVNAVSIHQ----------------- 289
Cdd:pfam00454   3 GGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPNSETLAYildeygengvpptamvk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  290 ------------VKKQSQLS------LLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 350
Cdd:pfam00454  83 ilhsalnypklkLEFESRISlppkvgLLQWFVKKSPDA--EEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTt 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 656985050  351 GHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:pfam00454 161 GKLFHIDFGLCLPDAGKDLPFpEKVPFRLTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLM 231
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 266-363 7.07e-08

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 55.48  E-value: 7.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  266 YKILVISADSGMIEPVvnavsihqvkKQSQLSLLDYFlqEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNI 345
Cdd:PTZ00303 1090 YSVLPLSCDSGLIEKA----------EGRELSNLDNM--DIASYVLYRGTRSCINFLASAKLFLLLNYIFSIGDRHKGNV 1157

                          90
                  ....*....|....*...
gi 656985050  346 LLDAEGHIIHIDFGFILS 363
Cdd:PTZ00303 1158 LIGTNGALLHIDFRFIFS 1175
 
Name Accession Description Interval E-value
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 197-484 0e+00

Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIbeta (also called Pik1p in yeast) is a 110 kDa protein that is localized to the Golgi and the nucleus. It is required for maintaining the structural integrity of the Golgi complex (GC), and is a key regulator of protein transport from the GC to the plasma membrane. PI4KIIIbeta also functions in the genesis, transport, and exocytosis of synaptic vesicles. The Drosophila PI4KIIIbeta is essential for cytokinesis during spermatogenesis. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 547.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 197 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd05168    1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 277 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 354
Cdd:cd05168   81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 355 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCF--H 432
Cdd:cd05168  161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSKLPCFfgG 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 656985050 433 GSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 484
Cdd:cd05168  241 GEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
 201-484 1.35e-153

Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. There are two types of PI4Ks, types II and III. Type II PI4Ks lack the characteristic catalytic kinase domain present in PI3Ks and type III PI4Ks, and are excluded from this family. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270626 [Multi-domain]  Cd Length: 286  Bit Score: 438.23  E-value: 1.35e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 201 LKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEP 280
Cdd:cd00893    2 FGEDWTDKTERIREKSPYGNLKGWKLVSLIVKTGDDLKQEQLALQLISQFDQIFKEEGLPLWLRPYEILSLGPDSGIIEM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 281 VVNAVSIHQVKKQSQ-----LSLLDYFLQEHGSyttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIH 355
Cdd:cd00893   82 IKNAVSIDSLKKKLDsfnkfVSLSDFFDDNFGD---EAIQKARDNFLQSLVAYSLVCYFLQIKDRHNGNILLDKEGHIIH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 356 IDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFhGSS 435
Cdd:cd00893  159 IDFGFFLSSHPGFYGFEGAPFKLSSEYIEVLGGVDSELFKEFRKLFLKGFMALRKHSDKILSLVEMMYSGHGITCF-GKK 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 656985050 436 TIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 484
Cdd:cd00893  238 TIQQLKQRFNPELTEGELEVYVLSLINKSLDNWRTRWYDKYQYFSQGIF 286
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
 227-484 2.33e-104

Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 4-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) to generate PtdIns(4)P, the major precursor in the synthesis of other phosphoinositides including PtdIns(4,5)P2, PtdIns(3,4)P2, and PtdIns(3,4,5)P3. Two isoforms of type III PI4K, alpha and beta, exist in most eukaryotes. PI4KIIIalpha is a 220 kDa protein found in the plasma membrane and the endoplasmic reticulum (ER). The role of PI4KIIIalpha in the ER remains unclear. In the plasma membrane, it provides PtdIns(4)P, which is then converted by PI5Ks to PtdIns(4,5)P2, an important signaling molecule. Vertebrate PI4KIIIalpha is also part of a signaling complex associated with P2X7 ion channels. The yeast homolog, Stt4p, is also important in regulating the conversion of phosphatidylserine to phosphatidylethanolamine at the ER and Golgi interface. Mammalian PI4KIIIalpha is highly expressed in the nervous system. The PI4K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270711 [Multi-domain]  Cd Length: 307  Bit Score: 313.76  E-value: 2.33e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEH 306
Cdd:cd05167   50 QAAIFKVGDDCRQDMLALQLISLFKNIFEEVGLDLYLFPYRVVATGPGCGVIEVIPNSKSRDQIGRETDNGLYEYFLSKY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 307 GSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSP-RNLGFETSAFKLTTEFVDV 385
Cdd:cd05167  130 GDESTPAFQKARRNFIKSMAGYSLVSYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFEISPgGNLGFESAPFKLTKEMVDL 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 386 MGG-LNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGsSTIRNLKERFHMSMTEEQLQLLVEQMVDGS 464
Cdd:cd05167  210 MGGsMESEPFKWFVELCVRGYLAVRPYAEAIVSLVELM-LDSGLPCFRG-QTIKNLRERFALEMSEREAANFMIKLIADS 287

                        250       260
                 ....*....|....*....|
gi 656985050 465 MRSITTKLYDGFQYLTNGIM 484
Cdd:cd05167  288 YLKIRTKGYDMFQYYQNGIP 307
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
 200-425 6.98e-81

Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family include PI3K, phosphoinositide 4-kinase (PI4K), PI3K-related protein kinases (PIKKs), and TRansformation/tRanscription domain-Associated Protein (TRAPP). PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives, while PI4K catalyze the phosphorylation of the 4-hydroxyl of PtdIns. PIKKs are protein kinases that catalyze the phosphorylation of serine/threonine residues, especially those that are followed by a glutamine. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI4Ks produce PtdIns(4)P, the major precursor to important signaling phosphoinositides. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PI3K-like catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270621 [Multi-domain]  Cd Length: 216  Bit Score: 249.94  E-value: 6.98e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 200 ALKEPWQEKVRRIReGSPYGHLPNWR---LLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd00142    1 NALDVGILKVIHSK-QRPKKITLIGAdgkTYSFLLKRRDDLRKDERSFQFMRLIQSILEKESVNLVLPPYKVIPLSENSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 277 MIEPVVNAVSIHqvkkqsqlSLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHI 356
Cdd:cd00142   80 LIEIVKDAQTIE--------DLLKSLWRKSPSS--QSWLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIMIEPSGNIFHI 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 656985050 357 DFGFILSSSPRNLGFETSAFKLTTEFVDVMGGlnGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQG 425
Cdd:cd00142  150 DFGFIFSGRKLAEGVETVPFRLTPMLENAMGT--AGVNGPFQISMVKIMEILREHADLIVPILEHSLRD 216
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 229-434 1.77e-69

Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in a variety of processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, and apoptosis. These homologues may be either lipid kinases and/or protein kinases: the former phosphorylate the 3-position in the inositol ring of inositol phospholipids. The ataxia telangiectesia-mutated gene produced, the targets of rapamycin (TOR) and the DNA-dependent kinase have not been found to possess lipid kinase activity. Some of this family possess PI-4 kinase activities.


Pssm-ID: 214538 [Multi-domain]  Cd Length: 240  Bit Score: 221.40  E-value: 1.77e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050   229 VIVKCGDDLRQELLAFQVLKQLQSIWEQE----RVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS---------- 294
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYrkqkgkvldl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050   295 ----------------------QLSLLDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGH 352
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPDPS-EDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGH 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050   353 IIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCF 431
Cdd:smart00146 160 LFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELM-LYDGLPDW 236


                   ...
gi 656985050   432 HGS 434
Cdd:smart00146 237 RSG 239
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
211-483 1.02e-59

Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 212.72  E-value: 1.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  211 RIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIW----EQERVPLWIKPYKILVISADSGMIEPVVNAVS 286
Cdd:COG5032  1781 LQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDT 1860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  287 IHQVKK------------QSQL-------------------------SLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYC 329
Cdd:COG5032  1861 LHSILReyhkrknisidqEKKLaarldnlklllkdefftkatlksppVLYDWFSESFPNP--EDWLTARTNFARSLAVYS 1938

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  330 LVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGGLNGDMFnyYKMLMLQGLIA 407
Cdd:COG5032  1939 VIGYILGLGDRHPGNILIDrSSGHVIHIDFGFILFNAPGRFPFpEKVPFRLTRNIVEAMGVSGVEGS--FRELCETAFRA 2016

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  408 ARKHMDKVVQIVEIMQ-----QGSQLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLT 480
Cdd:COG5032  2017 LRKNADSLMNVLELFVrdpliEWRRLPCFREIQnnEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLAT 2096


                  ...
gi 656985050  481 NGI 483
Cdd:COG5032  2097 MYI 2099
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 228-474 2.48e-47

Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. Class III PI3Ks, also called Vps34 (vacuolar protein sorting 34), contain an N-terminal lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They phosphorylate only the substrate PtdIns. They interact with a regulatory subunit, Vps15, to form a membrane-associated complex. Class III PI3Ks are involved in protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270628 [Multi-domain]  Cd Length: 346  Bit Score: 166.94  E-value: 2.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 228 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQsQLSLLDYFLQEHG 307
Cdd:cd00896   94 KVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPNDGLVEFVPNSKALADILKK-YGSILNFLRKHNP 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 308 SYTTEAFLSAQ--RNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLgfeTSAFKLTTEFVDV 385
Cdd:cd00896  173 DESGPYGIKPEvmDNFVKSCAGYCVITYILGVGDRHLDNLLLTKDGHLFHIDFGYILGRDPKPF---PPPMKLCKEMVEA 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 386 MGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDG 463
Cdd:cd00896  250 MGGANSEGYKEFKKYCCTAYNILRKHANLILNLFSLM-VDANIPDIALEPdkAVLKVQEKFRLDLSDEEAEQYFQNLIDE 328

                        250
                 ....*....|.
gi 656985050 464 SMRSITTKLYD 474
Cdd:cd00896  329 SVNALFPAVVE 339
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 229-452 1.14e-46

Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class II PI3Ks comprise three catalytic isoforms that do not associate with any regulatory subunits. They selectively use PtdIns as a susbtrate to produce PtsIns(3)P. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270624 [Multi-domain]  Cd Length: 334  Bit Score: 164.67  E-value: 1.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 229 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAV---SIHQVKKQ-----SQLSLLD 300
Cdd:cd00891   90 VIFKAGDDLRQDQLTLQLLRIMDKLWKKEGLDLRMTPYKCIATGDEVGMIEVVPNSEttaAIQKKYGGfgaafKDTPISN 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 301 YFLQEHGsyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd00891  170 WLKKHNP--TEEEYEEAVENFIRSCAGYCVATYVLGIGDRHNDNIMVTKSGHLFHIDFGHFLGNFKKKFGIkrERAPFVF 247

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 656985050 379 TTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSSTIRNLKERFHMSMTEEQ 452
Cdd:cd00891  248 TPEMAYVMGGEDSENFQKFEDLCCKAYNILRKHGNLLINLFSLM-LSAGIPELQSIEDIEYLRDALQLDLSDEE 320
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 228-422 4.84e-40

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 144.39  E-value: 4.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  228 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLW-IKPYKILVISADSGMIEPVVNAVSIHQ----------------- 289
Cdd:pfam00454   3 GGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPNSETLAYildeygengvpptamvk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  290 ------------VKKQSQLS------LLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 350
Cdd:pfam00454  83 ilhsalnypklkLEFESRISlppkvgLLQWFVKKSPDA--EEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTt 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 656985050  351 GHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:pfam00454 161 GKLFHIDFGLCLPDAGKDLPFpEKVPFRLTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLM 231
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 229-411 9.12e-35

Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. In vitro, they can also phosphorylate the substrates PtdIns and PtdIns(4)P. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270709 [Multi-domain]  Cd Length: 363  Bit Score: 133.53  E-value: 9.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 229 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL--------SLLD 300
Cdd:cd05165   98 IIFKNGDDLRQDMLTLQIIRIMDNIWKEEGLDLRMLPYGCLSTGDNVGLIEVVRNAKTIANIQKKKGKvatlafnkDSLH 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 301 YFLQEHgSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd05165  178 KWLKEK-NKTGEKYDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVKENGQLFHIDFGHFLGNFKKKFGIkrERVPFVL 256

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 656985050 379 TTEFVDVM----GGLNGDMFNYYKMLMLQGLIAARKH 411
Cdd:cd05165  257 THDFVYVIargqDNTKSEEFQEFQELCEKAYLILRRH 293
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 227-472 4.88e-33

Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. They are activated by a variety of stimuli including chemokines, cytokines, lysophosphatidic acid (LPA), insulin, and tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270710 [Multi-domain]  Cd Length: 352  Bit Score: 128.18  E-value: 4.88e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL------SLLD 300
Cdd:cd05166   91 ISVIFKVGDDLRQDMLTLQLIRIMDKIWLQEGLDLKMITFRCVPTGNKRGMVELVPEAETLREIQTEHGLtgsfkdRPLA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 301 YFLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd05166  171 DWLQKHNP-SELEYEKAVENFIRSCAGYCVATYVLGICDRHNDNIMLKTSGHLFHIDFGKFLGDAQMFGNFkrDRVPFVL 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 379 TTEFVDVMGGlnGDM----FNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFhGSSTIRNLKERFHMSMTEEQLQ 454
Cdd:cd05166  250 TSDMAYVING--GDKpssrFQLFVDLCCQAFNIIRKNSNLLLNLLSLMLS-SGIPGV-TQDDLRYVQDALLPELTDAEAT 325

                        250
                 ....*....|....*...
gi 656985050 455 LLVEQMVDGSMRSITTKL 472
Cdd:cd05166  326 AHFTRMIEESLSSKFTQL 343
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 227-452 5.68e-32

Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kgamma signaling controls diverse immune and vascular functions including cell recruitment, mast cell activation, platelet aggregation, and smooth muscle contractility. It associates with one of two regulatory subunits, p101 and p84, and is activated by G-protein-coupled receptors (GPCRs) by direct binding to their betagamma subunits. It contains an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270627 [Multi-domain]  Cd Length: 367  Bit Score: 125.75  E-value: 5.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKkQSQL--------SL 298
Cdd:cd00894  100 IGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQ-QSTVgntgafkdEV 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 299 LDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAF 376
Cdd:cd00894  179 LNHWLKEKCPIE-EKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGInkERVPF 257

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 656985050 377 KLTTEFVDVMGGLNGDM---FNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFHGSSTIRNLKERFHMSMTEEQ 452
Cdd:cd00894  258 VLTPDFLFVMGTSGKKTslhFQKFQDVCVKAYLALRHHTNLLIILFSMMLM-TGMPQLTSKEDIEYIRDALTVGKSEED 335
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 227-422 1.32e-29

Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II gamma isoform, PI3K-C2gamma, is expressed in the liver, breast, and prostate. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. It's biological function remains unknown. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270721 [Multi-domain]  Cd Length: 354  Bit Score: 118.84  E-value: 1.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL-------SLL 299
Cdd:cd05177   92 ISIIFKTGDDLRQDMLVLQIVRVMDNIWLQEGLDMQMIIYRCLSTGKTQGLVQMVPDAVTLAKIHRESGLigplkenTIE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 300 DYFLQEHgsYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFK 377
Cdd:cd05177  172 KWFHMHN--KLKEDYDKAVRNFFHSCAGWCVVTFILGVCDRHNDNIMLTHSGHMFHIDFGKFLGHAQTFGSIkrDRAPFI 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 656985050 378 LTTE--FVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:cd05177  250 FTSEmeYFITEGGKKPQRFQRFVELCCRAYNIVRKHSQLLLNLLEMM 296
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 226-472 5.66e-29

Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kbeta can be activated by G-protein-coupled receptors. Deletion of PI3Kbeta in mice results in early lethality at around day three of development. PI3Kbeta plays an important role in regulating sustained integrin activation and stable platelet agrregation, especially under conditions of high shear stress. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270717 [Multi-domain]  Cd Length: 362  Bit Score: 117.37  E-value: 5.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 226 LLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS----------Q 295
Cdd:cd05173   94 SLGIIFKNGDDLRQDMLTLQILRLMDTLWKEAGLDLRIVPYGCLATGDRSGLIEVVSSAETIADIQLNSsnvaaaaafnK 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 296 LSLLDYfLQEHGSytTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ET 373
Cdd:cd05173  174 DALLNW-LKEYNS--GDDLERAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVRKNGQLFHIDFGHILGNFKSKFGIkrER 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 374 SAFKLTTEFVDVM---GGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSqLPCFHGSSTIRNLKERFHMSMTE 450
Cdd:cd05173  251 VPFILTYDFIHVIqqgKTGNTEKFGRFRQYCEDAYLILRKNGNLFITLFALMLTAG-LPELTSVKDIQYLKDSLALGKSE 329

                        250       260
                 ....*....|....*....|...
gi 656985050 451 EQLQLLVEQMVDGSMR-SITTKL 472
Cdd:cd05173  330 EEALKQFRQKFDEALReSWTTKV 352
PI3Kc_C2_alpha cd05176
Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 227-472 1.31e-28

Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II alpha isoform, PI3K-C2alpha, plays key roles in clathrin assembly and clathrin-mediated membrane trafficking, insulin signaling, vascular smooth muscle contraction, and the priming of neurosecretory granule exocytosis. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270720 [Multi-domain]  Cd Length: 353  Bit Score: 116.23  E-value: 1.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL--SLLDYFLQ 304
Cdd:cd05176   91 INVMFKVGEDLRQDMLALQMIKIMDKIWLQEGLDLRMVIFKCLSTGKDRGMVELVPSSDTLRKIQVEYGVtgSFKDKPLA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 305 E---HGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKLT 379
Cdd:cd05176  171 EwlrKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFkrDRAPFVLT 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 380 TEFVDVMGGlnGDM----FNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFHGSSTIRNLKERFHMSMTEEQLQL 455
Cdd:cd05176  251 SDMAYVING--GEKptirFQLFVDLCCQAYNLIRKHTNLFLNLLSLMLS-SGLPELTGIQDLKYVFDALQPQTTDAEATI 327

                        250
                 ....*....|....*..
gi 656985050 456 LVEQMVDGSMRSITTKL 472
Cdd:cd05176  328 FFTRLIESSLGSVATKF 344
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 229-472 2.77e-28

Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kalpha plays an important role in insulin signaling. It also mediates physiologic heart growth and provides protection from stress. Activating mutations of PI3Kalpha is associated with diverse forms of cancer at high frequency. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270719 [Multi-domain]  Cd Length: 370  Bit Score: 115.54  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 229 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLS--------LLD 300
Cdd:cd05175  105 IIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKgalqfnshTLH 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 301 YFLQEHGSytTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd05175  185 QWLKDKNK--GEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYkrERVPFVL 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 379 TTEFVDVMGG-----LNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSSTIRNLKERFHMSMTE-EQ 452
Cdd:cd05175  263 TQDFLIVISKgaqecTKTREFERFQEMCYKAYLAIRQHANLFINLFSMM-LGSGMPELQSFDDIAYIRKTLALDKTEqEA 341

                        250       260
                 ....*....|....*....|
gi 656985050 453 LQLLVEQMVDGSMRSITTKL 472
Cdd:cd05175  342 LEYFMKQMNDAHHGGWTTKM 361
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
 227-452 5.82e-28

Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. PI3Kdelta is mainly expressed in immune cells and plays an important role in cellular and humoral immunity. It plays a major role in antigen receptor signaling in B-cells, T-cells, and mast cells. It regulates the differentiation of peripheral helper T-cells and controls the development and function of regulatory T-cells. PI3Ks can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class I PI3Ks are the only enzymes capable of converting PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. Class I enzymes are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. They are further classified into class IA (alpha, beta and delta) and IB (gamma). Class IA enzymes contain an N-terminal p85 binding domain, a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding cataytic domain. They associate with a regulatory subunit of the p85 family and are activated by tyrosine kinase receptors. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270718 [Multi-domain]  Cd Length: 366  Bit Score: 114.38  E-value: 5.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQ----------SQL 296
Cdd:cd05174   98 VGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLSTGDKTGLIEVVLHSDTIANIQLNksnmaataafNKD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 297 SLLDYFLQEHGSyttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETS 374
Cdd:cd05174  178 ALLNWLKSKNPG---DALDQAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGInrERV 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 375 AFKLTTEFVDVM---GGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSSTIRNLKERFHMSMTEE 451
Cdd:cd05174  255 PFILTYDFVHVIqqgKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALM-KAAGLPELSCSKDIQYLKDSLALGKTEE 333


                 .
gi 656985050 452 Q 452
Cdd:cd05174  334 E 334
PI3Kc_C2_beta cd00895
Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 227-472 6.51e-26

Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. The class II beta isoform, PI3K-C2beta, contributes to the migration and survival of cancer cells. It regulates Rac activity and impacts membrane ruffling, cell motility, and cadherin-mediated cell-cell adhesion. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They can be divided into three main classes (I, II, and III), defined by their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PtdIns as a substrate to produce PtdIns(3)P, but can also phosphorylate PtdIns(4)P. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a Phox homology (PX) domain, and a second C2 domain at the C-terminus. The PI3K catalytic domain family is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 119421 [Multi-domain]  Cd Length: 354  Bit Score: 108.55  E-value: 6.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLS-------LL 299
Cdd:cd00895   92 IRVIFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHGVTgsfkdrpLA 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 300 DYfLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPR--NLGFETSAFK 377
Cdd:cd00895  172 DW-LQKHNP-TEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMfgNIKRDRAPFV 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 378 LTTEFVDVMGGlnGD----MFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFHGSSTIRNLKERFHMSMTEEQL 453
Cdd:cd00895  250 FTSDMAYVING--GDkpssRFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLS-CGIPELSDLEDLKYVYDALRPQDTEADA 326

                        250
                 ....*....|....*....
gi 656985050 454 QLLVEQMVDGSMRSITTKL 472
Cdd:cd00895  327 TTYFTRLIESSLGSVATKL 345
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
 230-422 1.61e-21

Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members include ATM (Ataxia telangiectasia mutated), ATR (Ataxia telangiectasia and Rad3-related), TOR (Target of rapamycin), SMG-1 (Suppressor of morphogenetic effect on genitalia-1), and DNA-PK (DNA-dependent protein kinase). PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). They show strong preference for phosphorylating serine/threonine residues followed by a glutamine and are also referred to as (S/T)-Q-directed kinases. They all contain a FATC (FRAP, ATM and TRRAP, C-terminal) domain. PIKKs have diverse functions including cell-cycle checkpoints, genome surveillance, mRNA surveillance, and translation control. The PIKK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270708 [Multi-domain]  Cd Length: 222  Bit Score: 92.72  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 230 IVKCGDDLRQE---LLAFQVL-KQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVkkqsqlsLLDYFLqe 305
Cdd:cd05164   33 LVKGDDDLRKDervMQLFQLLnTLLEKDKETRKRNLTIRTYSVVPLSSQSGLIEWVDNTTTLKPV-------LKKWFN-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 306 HGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVD 384
Cdd:cd05164  104 ETFPDPTQWYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKtGEVVHIDFGMIFNKGKTLPVPEIVPFRLTRNIIN 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 656985050 385 VMG--GLNGdmfNYYKMlMLQGLIAARKHMDKVVQIVEIM 422
Cdd:cd05164  184 GMGptGVEG---LFRKS-CEQVLRVFRKHKDKLITFLDTF 219
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
 230-411 3.55e-21

Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, containing the Ku70/80 subunit, and a catalytic subunit, which contains a NUC194 domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. It is part of a multi-component system involved in non-homologous end joining (NHEJ), a process of repairing double strand breaks (DSBs) by joining together two free DNA ends of little homology. DNA-PK functions as a molecular sensor for DNA damage that enhances the signal via phosphorylation of downstream targets. It may also act as a protein scaffold that aids the localization of DNA repair proteins to the site of DNA damage. DNA-PK also plays a role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. DNA-PK is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The DNA-PK catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270716 [Multi-domain]  Cd Length: 235  Bit Score: 92.25  E-value: 3.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 230 IVKCGDDLR-----QELLAF--QVLKQLQSIWEQErvpLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSqlsLLDYF 302
Cdd:cd05172   33 LVKGGEDLRqdqriQQLFDVmnNILASDPACRQRR---LRIRTYQVIPMTSRLGLIEWVDNTTPLKEILEND---LLRRA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 303 LQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTT 380
Cdd:cd05172  107 LLSLAS-SPEAFLALRSNFARSLAAMSICGYILGIGDRHLSNFLVDlSTGRLIGIDFGHAFGSATQFLPIpELVPFRLTR 185

                        170       180       190
                 ....*....|....*....|....*....|.
gi 656985050 381 EFVDVMGGLNGDmfNYYKMLMLQGLIAARKH 411
Cdd:cd05172  186 QLLNLLQPLDAR--GLLRSDMVHVLRALRAG 214
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 230-391 1.27e-16

Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA double strand breaks (DSBs) caused by radiation. It is activated at the site of a DSB and phosphorylates key substrates that trigger pathways that regulate DNA repair and cell cycle checkpoints at the G1/S, S phase, and G2/M transition. Patients with the human genetic disorder Ataxia telangiectasia (A-T), caused by truncating mutations in ATM, show genome instability, increased cancer risk, immunodeficiency, compromised mobility, and neurodegeneration. A-T displays clinical heterogeneity, which is correlated to the degree of retained ATM activity. ATM contains a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. It is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The ATM catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270715 [Multi-domain]  Cd Length: 282  Bit Score: 79.89  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 230 IVKCGDDLRQELLAFQVLKQLQSIWEQERVP----LWIKPYKILVISADSGMIEPVVNAVSIHQV--------------- 290
Cdd:cd05171   33 LVKGGDDLRQDAVMEQVFELVNQLLKRDKETrkrkLRIRTYKVVPLSPRSGVLEFVENTIPLGEYlvgassksgaharyr 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 291 ----------KKQSQLSLLD--------------------YFLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDR 340
Cdd:cd05171  113 pkdwtastcrKKMREKAKASaeerlkvfdeicknfkpvfrHFFLEKFP-DPSDWFERRLAYTRSVATSSIVGYILGLGDR 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 656985050 341 HNGNILLDAE-GHIIHIDFGFI-----LSSSPrnlgfETSAFKLTTEFVDVMG--GLNG 391
Cdd:cd05171  192 HLNNILIDQKtGELVHIDLGIAfeqgkLLPIP-----ETVPFRLTRDIVDGMGitGVEG 245
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 225-387 2.76e-11

Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to as Mei-41 (Drosophila), Esr1/Mec1p (Saccharomyces cerevisiae), Rad3 (Schizosaccharomyces pombe), and FRAP-related protein (human). ATR contains a UME domain of unknown function, a FAT (FRAP, ATM and TRRAP) domain, a catalytic domain, and a FATC domain at the C-terminus. Together with its downstream effector kinase, Chk1, ATR plays a central role in regulating the replication checkpoint. ATR stabilizes replication forks by promoting the association of DNA polymerases with the fork. Preventing fork collapse is essential in preserving genomic integrity. ATR also plays a role in normal cell growth and in response to DNA damage. ATR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The ATR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270625 [Multi-domain]  Cd Length: 237  Bit Score: 63.29  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 225 RLLSVIVKCGDDLRQEL----LAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSI-HQVKKQSQLSLL 299
Cdd:cd00892   28 KKYPFLCKPKDDLRKDArmmeFNTLINRLLSKDPESRRRNLHIRTYAVIPLNEECGIIEWVPNTVTLrSILSTLYPPVLH 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 300 DYFLQEHGSYTteAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDF------GFILsSSPrnlgfE 372
Cdd:cd00892  108 EWFLKNFPDPT--AWYEARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTtGDVVHVDFdclfdkGLTL-EVP-----E 179

                        170
                 ....*....|....*
gi 656985050 373 TSAFKLTTEFVDVMG 387
Cdd:cd00892  180 RVPFRLTQNMVDAMG 194
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 266-363 7.07e-08

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 55.48  E-value: 7.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050  266 YKILVISADSGMIEPVvnavsihqvkKQSQLSLLDYFlqEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNI 345
Cdd:PTZ00303 1090 YSVLPLSCDSGLIEKA----------EGRELSNLDNM--DIASYVLYRGTRSCINFLASAKLFLLLNYIFSIGDRHKGNV 1157

                          90
                  ....*....|....*...
gi 656985050  346 LLDAEGHIIHIDFGFILS 363
Cdd:PTZ00303 1158 LIGTNGALLHIDFRFIFS 1175
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 236-421 1.84e-07

Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic domain, and a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. It is also called FRAP (FK506 binding protein 12-rapamycin associated protein). TOR is a central component of the eukaryotic growth regulatory network. It controls the expression of many genes transcribed by all three RNA polymerases. It associates with other proteins to form two distinct complexes, TORC1 and TORC2. TORC1 is involved in diverse growth-related functions including protein synthesis, nutrient use and transport, autophagy and stress responses. TORC2 is involved in organizing cytoskeletal structures. TOR is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The TOR catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270713 [Multi-domain]  Cd Length: 279  Bit Score: 52.48  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 236 DLRQELLAFQVLKQLQSIWEQERVP----LWIKPYKILVISADSGMIEPVVNAVSIHQVKKQ------------------ 293
Cdd:cd05169   39 DLRLDERVMQLFGLVNTLLKNDSETsrrnLSIQRYSVIPLSPNSGLIGWVPGCDTLHSLIRDyrekrkiplniehrlmlq 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 294 -----SQLSLLD-YFLQEHG----------------SYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 350
Cdd:cd05169  119 mapdyDNLTLIQkVEVFEYAlentpgddlrrvlwlkSPSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLt 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 351 GHIIHIDFGFIlsssprnlgFETSA----------FKLTTEFVDVMG--GLNGdmfNYYK-----MLMLqgliaaRKHMD 413
Cdd:cd05169  199 GKVIHIDFGDC---------FEVAMhrekfpekvpFRLTRMLVNAMEvsGVEG---TFRStcedvMRVL------RENKD 260


                 ....*...
gi 656985050 414 KVVQIVEI 421
Cdd:cd05169  261 SLMAVLEA 268
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
 307-391 1.91e-06

Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical role in the mRNA surveillance mechanism known as non-sense mediated mRNA decay (NMD). NMD protects the cells from the accumulation of aberrant mRNAs with premature termination codons (PTCs) generated by genome mutations and by errors during transcription and splicing. SMG-1 phosphorylates Upf1, another central component of NMD, at the C-terminus upon recognition of PTCs. The phosphorylation/dephosphorylation cycle of Upf1 is essential for promoting NMD. In addition to its catalytic domain, SMG-1 contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain at the C-terminus. SMG-1 is a member of the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K, and their large molecular weight (240-470 kDa). The SMG-1 catalytic domain subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and RIO kinases.


Pssm-ID: 270714  Cd Length: 304  Bit Score: 49.56  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656985050 307 GSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDFgfilsssprNLGF---------ETSAF 376
Cdd:cd05170  180 SSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLStGEVVHIDY---------NVCFekgkrlrvpEKVPF 250

                         90
                 ....*....|....*..
gi 656985050 377 KLTTEFVDVMG--GLNG 391
Cdd:cd05170  251 RLTQNIEHALGptGVEG 267
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 309-359 3.86e-03

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: 37.81  E-value: 3.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 656985050 309 YTTEAFLSAQRN--FVQSCAGYCLVCYLLQV--KDRHNGNILLDAEGHIIHIDFG 359
Cdd:cd13968   82 YTQEEELDEKDVesIMYQLAECMRLLHSFHLihRDLNNDNILLSEDGNVKLIDFG 136
 
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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