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Conserved domains on  [gi|81885714|sp|Q6PF93|]
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RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3; Short=PI3-kinase type 3; Short=PI3K type 3; Short=PtdIns-3-kinase type 3; AltName: Full=Phosphoinositide-3-kinase class 3

Protein Classification

phosphatidylinositol 3-kinase( domain architecture ID 10170542)

phosphatidylinositol 3-kinase catalyzes 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 539-883 0e+00

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: 621.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 539 RSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMP 618
Cdd:cd00896   1 REALKRQQEFVDRLRSLMKEVKNEKGSRDKKIERLRELLSDSELGLLLFFEPLPLPLDPSVKVTGIIPEKSTVFKSALMP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 619 AQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFI-QSVPVAEVLDTE 697
Cdd:cd00896  81 LKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPNDGLVEFVpNSKALADILKKY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 698 GSIQNFFRKYAPSETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPM 777
Cdd:cd00896 161 GSILNFLRKHNPDESGPYGIKPEVMDNFVKSCAGYCVITYILGVGDRHLDNLLLTKDGHLFHIDFGYILGRDPKPFPPPM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 778 KLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVH 857
Cdd:cd00896 241 KLCKEMVEAMGGANSEGYKEFKKYCCTAYNILRKHANLILNLFSLMVDANIPDIALEPDKAVLKVQEKFRLDLSDEEAEQ 320

                       330       340
                ....*....|....*....|....*.
gi 81885714 858 YMQSLIDESVHALFAAVVEQIHKFAQ 883
Cdd:cd00896 321 YFQNLIDESVNALFPAVVETIHKIAQ 346
PI3Ka_III cd00870
Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is ...
 283-503 1.90e-86

Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3Ks class III phosphorylate phosphoinositol (PtdIns) only. The prototypical PI3K class III, yeast Vps34, is involved in trafficking proteins from Golgi to the vacuole.


:

Pssm-ID: 238442  Cd Length: 166  Bit Score: 272.67  E-value: 1.90e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 283 DHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVED 362
Cdd:cd00870   1 DKDLKPNSKERKELNKILKYPPTTKLTDEEKDLIWKFRFYLTNNKKALTKFLKSVNWSDEQEVKQALELMPKWAKIDIED 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 363 SLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKngleptkkdsqtsaseslsnsgvssgdids 442
Cdd:cd00870  81 ALELLSPYFTNPVVRKYAVSRLKLASDEELLLYLLQLVQALKYENLDLSP------------------------------ 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81885714 443 sqiitnplppvaspppaskakevsdGENLEQDLCTFLISRACKNSTLANYLYWYVIVECED 503
Cdd:cd00870 131 -------------------------LPRLDSPLADFLIERALKNPKLANFLYWYLKVELED 166
C2_PI3K_class_III cd08397
C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 26-186 1.75e-85

C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. These are the only domains identified in the class III PI3Ks present in this cd. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


:

Pssm-ID: 176042  Cd Length: 159  Bit Score: 269.89  E-value: 1.75e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  26 LEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQ 105
Cdd:cd08397   1 LEGKVPLLSLSEKLEDPVLRFSGSNVSPNSDLFVTCQVFDDGKPLTLPVQTSYKPFKNRRNWNEWLTLPIKYSDLPRNSQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 106 VALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPgrTSSTLSEDQMSRLAKLTKAHRQG 185
Cdd:cd08397  81 LAITIWDVSGTGKAVPFGGTTLSLFNKDGTLRRGRQKLRVWPDVEADGSIPTSTG--KSPDSERDELDRLEKLLKKYERG 158


                .
gi 81885714 186 H 186
Cdd:cd08397 159 E 159
 
Name Accession Description Interval E-value
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 539-883 0e+00

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: 621.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 539 RSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMP 618
Cdd:cd00896   1 REALKRQQEFVDRLRSLMKEVKNEKGSRDKKIERLRELLSDSELGLLLFFEPLPLPLDPSVKVTGIIPEKSTVFKSALMP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 619 AQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFI-QSVPVAEVLDTE 697
Cdd:cd00896  81 LKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPNDGLVEFVpNSKALADILKKY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 698 GSIQNFFRKYAPSETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPM 777
Cdd:cd00896 161 GSILNFLRKHNPDESGPYGIKPEVMDNFVKSCAGYCVITYILGVGDRHLDNLLLTKDGHLFHIDFGYILGRDPKPFPPPM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 778 KLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVH 857
Cdd:cd00896 241 KLCKEMVEAMGGANSEGYKEFKKYCCTAYNILRKHANLILNLFSLMVDANIPDIALEPDKAVLKVQEKFRLDLSDEEAEQ 320

                       330       340
                ....*....|....*....|....*.
gi 81885714 858 YMQSLIDESVHALFAAVVEQIHKFAQ 883
Cdd:cd00896 321 YFQNLIDESVNALFPAVVETIHKIAQ 346
PI3Ka_III cd00870
Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is ...
 283-503 1.90e-86

Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3Ks class III phosphorylate phosphoinositol (PtdIns) only. The prototypical PI3K class III, yeast Vps34, is involved in trafficking proteins from Golgi to the vacuole.


Pssm-ID: 238442  Cd Length: 166  Bit Score: 272.67  E-value: 1.90e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 283 DHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVED 362
Cdd:cd00870   1 DKDLKPNSKERKELNKILKYPPTTKLTDEEKDLIWKFRFYLTNNKKALTKFLKSVNWSDEQEVKQALELMPKWAKIDIED 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 363 SLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKngleptkkdsqtsaseslsnsgvssgdids 442
Cdd:cd00870  81 ALELLSPYFTNPVVRKYAVSRLKLASDEELLLYLLQLVQALKYENLDLSP------------------------------ 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81885714 443 sqiitnplppvaspppaskakevsdGENLEQDLCTFLISRACKNSTLANYLYWYVIVECED 503
Cdd:cd00870 131 -------------------------LPRLDSPLADFLIERALKNPKLANFLYWYLKVELED 166
C2_PI3K_class_III cd08397
C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 26-186 1.75e-85

C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. These are the only domains identified in the class III PI3Ks present in this cd. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176042  Cd Length: 159  Bit Score: 269.89  E-value: 1.75e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  26 LEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQ 105
Cdd:cd08397   1 LEGKVPLLSLSEKLEDPVLRFSGSNVSPNSDLFVTCQVFDDGKPLTLPVQTSYKPFKNRRNWNEWLTLPIKYSDLPRNSQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 106 VALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPgrTSSTLSEDQMSRLAKLTKAHRQG 185
Cdd:cd08397  81 LAITIWDVSGTGKAVPFGGTTLSLFNKDGTLRRGRQKLRVWPDVEADGSIPTSTG--KSPDSERDELDRLEKLLKKYERG 158


                .
gi 81885714 186 H 186
Cdd:cd08397 159 E 159
PI3Ka smart00145
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 289-530 3.06e-69

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 214537  Cd Length: 184  Bit Score: 227.14  E-value: 3.06e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    289 NATTRDQLNIIVSYPPTKQLTYEEQDLVWKFR-YYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELL 367
Cdd:smart00145   4 DIEEREQLEAILKLDPTYELTEEEKDLIWKFRhYYLTNNPKALPKFLLSVKWSDADEVAQALSLLLSWAPLDPEDALELL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    368 SSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDikngleptkkdsqtsaseslsnsgvssgdidssqiit 447
Cdd:smart00145  84 DPKFPDPFVRAYAVKRLESASDEELLLYLLQLVQALKYEPYLD------------------------------------- 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    448 nplppvaspppaskakevsdgenleQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQA 527
Cdd:smart00145 127 -------------------------SALARFLLERALANQRLGHFFYWYLKSELHDPHVSIRFGLLLEAYLRGCGTHLKE 181


                   ...
gi 81885714    528 LLK 530
Cdd:smart00145 182 LLK 184
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 633-835 4.47e-67

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: 223.71  E-value: 4.47e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    633 VIFKHGDDLRQDQLILQIISLMDKLLRKE----NLDLKLTPYKVLATSTKHGFMQFI-QSVPVAEVLDT----------- 696
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVpNSTTLHEILKEyrkqkgkvldl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    697 ----------------------EGSIQNFFRKYAPSetgPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKT 754
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPD---PSEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    755 GKLFHIDFGYILGRDPKPLPPPMKL----NKEMVEGMGgtQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPD 830
Cdd:smart00146 158 GHLFHIDFGFILGNGPKLFGFPERVpfrlTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPD 235


                   ....*
gi 81885714    831 IALEP 835
Cdd:smart00146 236 WRSGK 240
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 631-831 6.80e-60

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: 204.10  E-value: 6.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   631 YPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLK-LTPYKVLATSTKHGFMQFIQ-SVPVAEVLD------------- 695
Cdd:pfam00454   2 YGGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPnSETLAYILDeygengvpptamv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   696 -----------------------TEGSIQNFFRKYAPSETGPYgisaEVMDTYVKSCAGYCVITYILGVGDRHLDNLLL- 751
Cdd:pfam00454  82 kilhsalnypklklefesrislpPKVGLLQWFVKKSPDAEEWG----EARKNFVRSCAGYSVLDYILGNGDRHLDNILVd 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   752 TKTGKLFHIDFGYILGRDPKPLPPPMKL----NKEMVEGMGgtQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDAN 827
Cdd:pfam00454 158 KTTGKLFHIDFGLCLPDAGKDLPFPEKVpfrlTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADG 235


                  ....
gi 81885714   828 IPDI 831
Cdd:pfam00454 236 LPDW 239
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
285-884 8.47e-56

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 210.41  E-value: 8.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  285 DLKPNATTRDQLNII--VSYPPTKQLTYEEQDLVWKFR---YYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMD 359
Cdd:COG5032 1445 YLLLCRLGRRELKAGlnVWNLTNLELFSDIQESEFFEWgknLKLLSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELLG 1524

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  360 VEDSLELLSSHYTNPTVRRYAvarlrqadDEDLLMYLLQLVQALKYENFDDI-----KNGLEPTKKDSQTSASESLSNSG 434
Cdd:COG5032 1525 SLLSAKDAAGSYYKNFHIFDL--------EISVIPFIPQLLSSLSLLDLNSAqsllsKIGKEHPQALVFTLRSAIESTAL 1596

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  435 VSSGDIDSSQIITNPLPPVASPPPASKAKEVSDGENLEQDLCT------FLISRACKNSTLANYL--YWYVIVECEDQDT 506
Cdd:COG5032 1597 SKESVALSLENKSRTHDPSLVKEALELSDENIRIAYPLLHLLFepilaqLLSRLSSENNKISVALliDKPLHEERENFPS 1676

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  507 QQRDPKTHEM----YLNVMRRFSQALLKGDKSvrvMRSLLAAqqTFVDRLVHLMKAVQResgnrkKKNERLQalLGDNEK 582
Cdd:COG5032 1677 GLSLSSFQSSflkeLIKKSPRKIRKKFKIDIS---LLNLSRK--LYISVLRSIRKRLKR------LLELRLK--KVSPKL 1743

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  583 MNLSDVELIPLPLE-----PQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKL 657
Cdd:COG5032 1744 LLFHAFLEIKLPGQylldkPFVLIERFEPEVSVVKSHLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKI 1823

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  658 LRKENL----DLKLTPYKVLATSTKHGFMQFIQSV-PVAEVLDT------------------------EGSIQNFF---R 705
Cdd:COG5032 1824 LKKDKEtrrrDLWIRPYKVIPLSPGSGIIEWVPNSdTLHSILREyhkrknisidqekklaarldnlklLLKDEFFTkatL 1903

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  706 KYAP------SETGPYGISAEV-MDTYVKSCAGYCVITYILGVGDRHLDNLLLTK-TGKLFHIDFGYILGRDPKPLPPPM 777
Cdd:COG5032 1904 KSPPvlydwfSESFPNPEDWLTaRTNFARSLAVYSVIGYILGLGDRHPGNILIDRsSGHVIHIDFGFILFNAPGRFPFPE 1983

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  778 KL----NKEMVEGMGGTQSEQYqeFRKQCYTAFLHLRRYSNLILNLFSLMVD------ANIPDIALEPDKTVKKVQDKFR 847
Cdd:COG5032 1984 KVpfrlTRNIVEAMGVSGVEGS--FRELCETAFRALRKNADSLMNVLELFVRdpliewRRLPCFREIQNNEIVNVLERFR 2061

                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 81885714  848 LDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQY 884
Cdd:COG5032 2062 LKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMY 2098
PI3K_C2 pfam00792
Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 ...
 53-198 2.60e-53

Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 domain. Outlier of pfam00168 family.


Pssm-ID: 395640  Cd Length: 136  Bit Score: 181.80  E-value: 2.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    53 TCSDLYVTCQVFAEGKPLALPVRTSYKAFST-RWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGP-GSAVPVGGTTVSLF 130
Cdd:pfam00792   1 RQEDLYVECQLYHGGKPLCLPVSTRYVPFSNsSIKWNEWITFPIQISDLPRSARLCITIWDVSGPeKSFVPIGWVNTSLF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81885714   131 GKYGMFRQGMHDLKVWPnveadgsePTRTPGRtsstLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTF 198
Cdd:pfam00792  81 DKKGILRQGKQKLRLWP--------SKSTPGR----SNVDEMNRLEKLLKKYERGQVSSVDWLDFLTF 136
PI3Ka pfam00613
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 285-529 3.01e-51

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 395488  Cd Length: 185  Bit Score: 177.91  E-value: 3.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   285 DLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSL 364
Cdd:pfam00613   2 DLKPNEKERKELEAILAYDPLSKLTAEEKDLIWKFRYYLMLVPKALTKLLLSVKWSDLSEVAEALSLLLKWAPIDPVDAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   365 ELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDikngleptkkdsqtsaseslsnsgvssgdidssq 444
Cdd:pfam00613  82 ELLDPKFPDPEVRQYAVKCLESASDDELLFYLLQLVQALKYEPFHD---------------------------------- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   445 iitnplppvaspppaskakevsdgenleQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLnvmRRF 524
Cdd:pfam00613 128 ----------------------------SYLSRFLLQRALKNRRIGHFFFWYLKSEIHDEEVSPRFGSLLELYL---RSC 176


                  ....*
gi 81885714   525 SQALL 529
Cdd:pfam00613 177 GTSLL 181
PI3K_C2 smart00142
Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.
 21-123 6.29e-33

Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.


Pssm-ID: 214536  Cd Length: 100  Bit Score: 122.46  E-value: 6.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714     21 LKIGSLEG-KREQKSYKAVLEDPMLKFSGLYqetcSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPD 99
Cdd:smart00142   1 VKIESLWDcDRNLVITIALIHGIPLNWSRDY----SDLYVEIQLYHGGKLLCLPVSTSYKPFFPSVKWNEWLTFPIQISD 76

                           90       100
                   ....*....|....*....|....
gi 81885714    100 LPRNAQVALTIWDVYGPGSAVPVG 123
Cdd:smart00142  77 LPREARLCITIYAVKNPSKGSEFG 100
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 597-766 4.08e-04

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 44.31  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   597 PQVKIRGIIPETatLFKSalMPAQLFFktedggkypvIFKHgDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATS 676
Cdd:PTZ00303 1032 PVTAVNGVSPES--LHDS--LPQECMF----------LYKR-ENVERDQLMCISSRLLQMLLSSEIGNAEMLDYSVLPLS 1096

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   677 TKHGFMQFIQSVPVAEVLDTEGSIQNFFRkyapsetgpyGISAEVmdTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGK 756
Cdd:PTZ00303 1097 CDSGLIEKAEGRELSNLDNMDIASYVLYR----------GTRSCI--NFLASAKLFLLLNYIFSIGDRHKGNVLIGTNGA 1164

                         170
                  ....*....|
gi 81885714   757 LFHIDFGYIL 766
Cdd:PTZ00303 1165 LLHIDFRFIF 1174
 
Name Accession Description Interval E-value
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 539-883 0e+00

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: 621.47  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 539 RSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMP 618
Cdd:cd00896   1 REALKRQQEFVDRLRSLMKEVKNEKGSRDKKIERLRELLSDSELGLLLFFEPLPLPLDPSVKVTGIIPEKSTVFKSALMP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 619 AQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFI-QSVPVAEVLDTE 697
Cdd:cd00896  81 LKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPNDGLVEFVpNSKALADILKKY 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 698 GSIQNFFRKYAPSETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPM 777
Cdd:cd00896 161 GSILNFLRKHNPDESGPYGIKPEVMDNFVKSCAGYCVITYILGVGDRHLDNLLLTKDGHLFHIDFGYILGRDPKPFPPPM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 778 KLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVH 857
Cdd:cd00896 241 KLCKEMVEAMGGANSEGYKEFKKYCCTAYNILRKHANLILNLFSLMVDANIPDIALEPDKAVLKVQEKFRLDLSDEEAEQ 320

                       330       340
                ....*....|....*....|....*.
gi 81885714 858 YMQSLIDESVHALFAAVVEQIHKFAQ 883
Cdd:cd00896 321 YFQNLIDESVNALFPAVVETIHKIAQ 346
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 539-868 1.49e-106

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: 332.23  E-value: 1.49e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 539 RSLLAAQQTFVDRLVHLMKAVQRESGNRKKknERLQALLGdnekmNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMP 618
Cdd:cd00891   1 REELLKQVKVLDELKEIAKKIKEEPSEERK--EVLEKLLQ-----KLELPKKFTLPLDPRMEVKGLIVEKCKVMDSKKLP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 619 AQLFFKTED--GGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQ-SVPVAEVLD 695
Cdd:cd00891  74 LWLVFKNADpgGDPIKVIFKAGDDLRQDQLTLQLLRIMDKLWKKEGLDLRMTPYKCIATGDEVGMIEVVPnSETTAAIQK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 696 TEG---------SIQNFFRKYAPSETgpygISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYIL 766
Cdd:cd00891 154 KYGgfgaafkdtPISNWLKKHNPTEE----EYEEAVENFIRSCAGYCVATYVLGIGDRHNDNIMVTKSGHLFHIDFGHFL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 767 GRDPKPLPPPMKL-----NKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDiaLEPDKTVKK 841
Cdd:cd00891 230 GNFKKKFGIKRERapfvfTPEMAYVMGGEDSENFQKFEDLCCKAYNILRKHGNLLINLFSLMLSAGIPE--LQSIEDIEY 307

                       330       340
                ....*....|....*....|....*..
gi 81885714 842 VQDKFRLDLSDEEAVHYMQSLIDESVH 868
Cdd:cd00891 308 LRDALQLDLSDEEAAEHFRKLIHESLN 334
PI3Ka_III cd00870
Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is ...
 283-503 1.90e-86

Phosphoinositide 3-kinase (PI3K) class III, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3Ks class III phosphorylate phosphoinositol (PtdIns) only. The prototypical PI3K class III, yeast Vps34, is involved in trafficking proteins from Golgi to the vacuole.


Pssm-ID: 238442  Cd Length: 166  Bit Score: 272.67  E-value: 1.90e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 283 DHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVED 362
Cdd:cd00870   1 DKDLKPNSKERKELNKILKYPPTTKLTDEEKDLIWKFRFYLTNNKKALTKFLKSVNWSDEQEVKQALELMPKWAKIDIED 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 363 SLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKngleptkkdsqtsaseslsnsgvssgdids 442
Cdd:cd00870  81 ALELLSPYFTNPVVRKYAVSRLKLASDEELLLYLLQLVQALKYENLDLSP------------------------------ 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81885714 443 sqiitnplppvaspppaskakevsdGENLEQDLCTFLISRACKNSTLANYLYWYVIVECED 503
Cdd:cd00870 131 -------------------------LPRLDSPLADFLIERALKNPKLANFLYWYLKVELED 166
C2_PI3K_class_III cd08397
C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 26-186 1.75e-85

C2 domain present in class III phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. These are the only domains identified in the class III PI3Ks present in this cd. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176042  Cd Length: 159  Bit Score: 269.89  E-value: 1.75e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  26 LEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQ 105
Cdd:cd08397   1 LEGKVPLLSLSEKLEDPVLRFSGSNVSPNSDLFVTCQVFDDGKPLTLPVQTSYKPFKNRRNWNEWLTLPIKYSDLPRNSQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 106 VALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPgrTSSTLSEDQMSRLAKLTKAHRQG 185
Cdd:cd08397  81 LAITIWDVSGTGKAVPFGGTTLSLFNKDGTLRRGRQKLRVWPDVEADGSIPTSTG--KSPDSERDELDRLEKLLKKYERG 158


                .
gi 81885714 186 H 186
Cdd:cd08397 159 E 159
PI3Ka smart00145
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 289-530 3.06e-69

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 214537  Cd Length: 184  Bit Score: 227.14  E-value: 3.06e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    289 NATTRDQLNIIVSYPPTKQLTYEEQDLVWKFR-YYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELL 367
Cdd:smart00145   4 DIEEREQLEAILKLDPTYELTEEEKDLIWKFRhYYLTNNPKALPKFLLSVKWSDADEVAQALSLLLSWAPLDPEDALELL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    368 SSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDikngleptkkdsqtsaseslsnsgvssgdidssqiit 447
Cdd:smart00145  84 DPKFPDPFVRAYAVKRLESASDEELLLYLLQLVQALKYEPYLD------------------------------------- 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    448 nplppvaspppaskakevsdgenleQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQA 527
Cdd:smart00145 127 -------------------------SALARFLLERALANQRLGHFFYWYLKSELHDPHVSIRFGLLLEAYLRGCGTHLKE 181


                   ...
gi 81885714    528 LLK 530
Cdd:smart00145 182 LLK 184
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 541-868 6.78e-68

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: 230.21  E-value: 6.78e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 541 LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMN-LSDvelIPLPLEPQVKIRGIIPETATLFKSALMPA 619
Cdd:cd05165   3 SLSRQVEALNKLKKLSDILKEKKKSKEKVKKLLKECLKQKFYDEaLQN---FQSPLNPSHKLGELIIEKCKVMDSKKRPL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 620 QLFFKTED-----GGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQ-SVPVAEV 693
Cdd:cd05165  80 WLVFENADplalsGEDIKIIFKNGDDLRQDMLTLQIIRIMDNIWKEEGLDLRMLPYGCLSTGDNVGLIEVVRnAKTIANI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 694 LDTEG----------SIQNFFRKYAPSETgpygISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFG 763
Cdd:cd05165 160 QKKKGkvatlafnkdSLHKWLKEKNKTGE----KYDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVKENGQLFHIDFG 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 764 YILGRdpkpLPPPMKLNKEMV-------------EGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPD 830
Cdd:cd05165 236 HFLGN----FKKKFGIKRERVpfvlthdfvyviaRGQDNTKSEEFQEFQELCEKAYLILRRHGNLFISLFSMMLSTGIPE 311

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 81885714 831 IALEPDktVKKVQDKFRLDLSDEEAVHYMQSLIDESVH 868
Cdd:cd05165 312 LTSVKD--IEYLRKTLALDKTEEEALKYFRKKFNEALK 347
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 548-883 8.29e-68

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: 229.48  E-value: 8.29e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 548 FVDRLVHLMKAVQRESgNRKKKNERLQALLGDNEKMNlSDVELIP--LPLEPQVKIRGIIPETATLFKSALMPAQLFFKT 625
Cdd:cd05166   6 KQHVLVQALTSIAEKV-KSAKDSARENALRRELEQLA-SFLLENSfrLPLDPALEVTGVDVRSCSYFNSNALPLKLVFRN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 626 ED--GGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFmqfIQSVPVAEVL---DTE--- 697
Cdd:cd05166  84 ADprAEPISVIFKVGDDLRQDMLTLQLIRIMDKIWLQEGLDLKMITFRCVPTGNKRGM---VELVPEAETLreiQTEhgl 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 698 -GS-----IQNFFRKYAPSETgPYGISaevMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILG---- 767
Cdd:cd05166 161 tGSfkdrpLADWLQKHNPSEL-EYEKA---VENFIRSCAGYCVATYVLGICDRHNDNIMLKTSGHLFHIDFGKFLGdaqm 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 768 -----RDPKPLPPPMklnkEM--VEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEpdkTVK 840
Cdd:cd05166 237 fgnfkRDRVPFVLTS----DMayVINGGDKPSSRFQLFVDLCCQAFNIIRKNSNLLLNLLSLMLSSGIPGVTQD---DLR 309

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 81885714 841 KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQ 883
Cdd:cd05166 310 YVQDALLPELTDAEATAHFTRMIEESLSSKFTQLNFFIHNLAQ 352
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 633-835 4.47e-67

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: 223.71  E-value: 4.47e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    633 VIFKHGDDLRQDQLILQIISLMDKLLRKE----NLDLKLTPYKVLATSTKHGFMQFI-QSVPVAEVLDT----------- 696
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVpNSTTLHEILKEyrkqkgkvldl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    697 ----------------------EGSIQNFFRKYAPSetgPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKT 754
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPD---PSEDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    755 GKLFHIDFGYILGRDPKPLPPPMKL----NKEMVEGMGgtQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPD 830
Cdd:smart00146 158 GHLFHIDFGFILGNGPKLFGFPERVpfrlTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPD 235


                   ....*
gi 81885714    831 IALEP 835
Cdd:smart00146 236 WRSGK 240
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 631-831 6.80e-60

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: 204.10  E-value: 6.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   631 YPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLK-LTPYKVLATSTKHGFMQFIQ-SVPVAEVLD------------- 695
Cdd:pfam00454   2 YGGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPnSETLAYILDeygengvpptamv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   696 -----------------------TEGSIQNFFRKYAPSETGPYgisaEVMDTYVKSCAGYCVITYILGVGDRHLDNLLL- 751
Cdd:pfam00454  82 kilhsalnypklklefesrislpPKVGLLQWFVKKSPDAEEWG----EARKNFVRSCAGYSVLDYILGNGDRHLDNILVd 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   752 TKTGKLFHIDFGYILGRDPKPLPPPMKL----NKEMVEGMGgtQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDAN 827
Cdd:pfam00454 158 KTTGKLFHIDFGLCLPDAGKDLPFPEKVpfrlTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADG 235


                  ....
gi 81885714   828 IPDI 831
Cdd:pfam00454 236 LPDW 239
PI3Ka cd00864
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 290-503 6.42e-57

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in PI3 and PI4-kinases. Its role is unclear, but it has been suggested to be involved in substrate presentation. Phosphoinositide 3-kinases play an important role in a variety of fundamental cellular processes and can be divided into three main classes, defined by their substrate specificity and domain architecture.


Pssm-ID: 238440  Cd Length: 152  Bit Score: 192.43  E-value: 6.42e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 290 ATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSS 369
Cdd:cd00864   1 AWERKPLLAILLYPPFSTLTEEEKELLWKFRYYLLNVPKALPKLLKSVNWNDDEEVSELYQLLKWWAPLSPEDALELLSP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 370 HYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDikngleptkkdsqtsaseslsnsgvssgdidssqiitnp 449
Cdd:cd00864  81 KYPDPVVRQYAVRVLESASDDELLLYLPQLVQALKYEPYLD--------------------------------------- 121

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 81885714 450 lppvaspppaskakevsdgenleQDLCTFLISRACKNSTLANYLYWYVIVECED 503
Cdd:cd00864 122 -----------------------SYLARFLLERALKSQRLGHQLYWNLKSEIHD 152
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
 600-885 2.40e-56

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: 196.66  E-value: 2.40e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 600 KIRGIIPETATLFKSAL-MPAQLFFKTEDGGK-----------------YPVIFKHGDDLRQDQLILQIISLMDKLLRKE 661
Cdd:cd05167   1 VVLGIDYKSGKPLQSAAkAPFLVTFKVKDCGVdelehegteseatkevwQAAIFKVGDDCRQDMLALQLISLFKNIFEEV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 662 NLDLKLTPYKVLATSTKHGfmqFIQSVPVAEVLD-----TEGSIQNFFR-KYAPSETGPYgISAEvmDTYVKSCAGYCVI 735
Cdd:cd05167  81 GLDLYLFPYRVVATGPGCG---VIEVIPNSKSRDqigreTDNGLYEYFLsKYGDESTPAF-QKAR--RNFIKSMAGYSLV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 736 TYILGVGDRHLDNLLLTKTGKLFHIDFGYIL----GRDPKPLPPPMKLNKEMVEGMGGT-QSEQYQEFRKQCYTAFLHLR 810
Cdd:cd05167 155 SYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFeispGGNLGFESAPFKLTKEMVDLMGGSmESEPFKWFVELCVRGYLAVR 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81885714 811 RYSNLILNLFSLMVDANIPDIAlepDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIhkfaQYW 885
Cdd:cd05167 235 PYAEAIVSLVELMLDSGLPCFR---GQTIKNLRERFALEMSEREAANFMIKLIADSYLKIRTKGYDMF----QYY 302
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
285-884 8.47e-56

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 210.41  E-value: 8.47e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  285 DLKPNATTRDQLNII--VSYPPTKQLTYEEQDLVWKFR---YYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMD 359
Cdd:COG5032 1445 YLLLCRLGRRELKAGlnVWNLTNLELFSDIQESEFFEWgknLKLLSIIPPIEEIFLSNALSCYLQVKDLLKKLNLFELLG 1524

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  360 VEDSLELLSSHYTNPTVRRYAvarlrqadDEDLLMYLLQLVQALKYENFDDI-----KNGLEPTKKDSQTSASESLSNSG 434
Cdd:COG5032 1525 SLLSAKDAAGSYYKNFHIFDL--------EISVIPFIPQLLSSLSLLDLNSAqsllsKIGKEHPQALVFTLRSAIESTAL 1596

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  435 VSSGDIDSSQIITNPLPPVASPPPASKAKEVSDGENLEQDLCT------FLISRACKNSTLANYL--YWYVIVECEDQDT 506
Cdd:COG5032 1597 SKESVALSLENKSRTHDPSLVKEALELSDENIRIAYPLLHLLFepilaqLLSRLSSENNKISVALliDKPLHEERENFPS 1676

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  507 QQRDPKTHEM----YLNVMRRFSQALLKGDKSvrvMRSLLAAqqTFVDRLVHLMKAVQResgnrkKKNERLQalLGDNEK 582
Cdd:COG5032 1677 GLSLSSFQSSflkeLIKKSPRKIRKKFKIDIS---LLNLSRK--LYISVLRSIRKRLKR------LLELRLK--KVSPKL 1743

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  583 MNLSDVELIPLPLE-----PQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKL 657
Cdd:COG5032 1744 LLFHAFLEIKLPGQylldkPFVLIERFEPEVSVVKSHLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKI 1823

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  658 LRKENL----DLKLTPYKVLATSTKHGFMQFIQSV-PVAEVLDT------------------------EGSIQNFF---R 705
Cdd:COG5032 1824 LKKDKEtrrrDLWIRPYKVIPLSPGSGIIEWVPNSdTLHSILREyhkrknisidqekklaarldnlklLLKDEFFTkatL 1903

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  706 KYAP------SETGPYGISAEV-MDTYVKSCAGYCVITYILGVGDRHLDNLLLTK-TGKLFHIDFGYILGRDPKPLPPPM 777
Cdd:COG5032 1904 KSPPvlydwfSESFPNPEDWLTaRTNFARSLAVYSVIGYILGLGDRHPGNILIDRsSGHVIHIDFGFILFNAPGRFPFPE 1983

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  778 KL----NKEMVEGMGGTQSEQYqeFRKQCYTAFLHLRRYSNLILNLFSLMVD------ANIPDIALEPDKTVKKVQDKFR 847
Cdd:COG5032 1984 KVpfrlTRNIVEAMGVSGVEGS--FRELCETAFRALRKNADSLMNVLELFVRdpliewRRLPCFREIQNNEIVNVLERFR 2061

                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 81885714  848 LDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQY 884
Cdd:COG5032 2062 LKLSEKDAEKFVDLLINKSVESLITQATDPFQLATMY 2098
PI3K_C2 pfam00792
Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 ...
 53-198 2.60e-53

Phosphoinositide 3-kinase C2; Phosphoinositide 3-kinase region postulated to contain a C2 domain. Outlier of pfam00168 family.


Pssm-ID: 395640  Cd Length: 136  Bit Score: 181.80  E-value: 2.60e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714    53 TCSDLYVTCQVFAEGKPLALPVRTSYKAFST-RWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGP-GSAVPVGGTTVSLF 130
Cdd:pfam00792   1 RQEDLYVECQLYHGGKPLCLPVSTRYVPFSNsSIKWNEWITFPIQISDLPRSARLCITIWDVSGPeKSFVPIGWVNTSLF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81885714   131 GKYGMFRQGMHDLKVWPnveadgsePTRTPGRtsstLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTF 198
Cdd:pfam00792  81 DKKGILRQGKQKLRLWP--------SKSTPGR----SNVDEMNRLEKLLKKYERGQVSSVDWLDFLTF 136
PI3Ka pfam00613
Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in ...
 285-529 3.01e-51

Phosphoinositide 3-kinase family, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation.


Pssm-ID: 395488  Cd Length: 185  Bit Score: 177.91  E-value: 3.01e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   285 DLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSL 364
Cdd:pfam00613   2 DLKPNEKERKELEAILAYDPLSKLTAEEKDLIWKFRYYLMLVPKALTKLLLSVKWSDLSEVAEALSLLLKWAPIDPVDAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   365 ELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDikngleptkkdsqtsaseslsnsgvssgdidssq 444
Cdd:pfam00613  82 ELLDPKFPDPEVRQYAVKCLESASDDELLFYLLQLVQALKYEPFHD---------------------------------- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   445 iitnplppvaspppaskakevsdgenleQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLnvmRRF 524
Cdd:pfam00613 128 ----------------------------SYLSRFLLQRALKNRRIGHFFFWYLKSEIHDEEVSPRFGSLLELYL---RSC 176


                  ....*
gi 81885714   525 SQALL 529
Cdd:pfam00613 177 GTSLL 181
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
 585-883 8.18e-51

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: 182.94  E-value: 8.18e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 585 LSDVELiplPLEPQVKIRGIIPETATLFKSALMPAQLFFKTED--GGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKEN 662
Cdd:cd05174  53 LSHLQS---PLDPSIILEEVCVDQCTFMDSKMKPLWIMYSSEEagAGNVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEG 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 663 LDLKLTPYKVLATSTKHGFMQFI------------QSVPVAEVLDTEGSIQNFFRKYAPSETGPYGIsaevmDTYVKSCA 730
Cdd:cd05174 130 LDLRMTPYGCLSTGDKTGLIEVVlhsdtianiqlnKSNMAATAAFNKDALLNWLKSKNPGDALDQAI-----EEFTLSCA 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 731 GYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRdpkpLPPPMKLNKEMVEGM-----------GGT-QSEQYQEF 798
Cdd:cd05174 205 GYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGN----FKTKFGINRERVPFIltydfvhviqqGKTnNSEKFERF 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 799 RKQCYTAFLHLRRYSNLILNLFSLMVDANIPDiaLEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQI 878
Cdd:cd05174 281 RGYCERAYTILRRHGLLFLHLFALMKAAGLPE--LSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWL 358


                ....*.
gi 81885714 879 -HKFAQ 883
Cdd:cd05174 359 aHNVSK 364
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 632-870 2.54e-49

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: 176.13  E-value: 2.54e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 632 PVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIqsvPVAEVLDT-------EGSIQNFF 704
Cdd:cd05168  32 SVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSGLIETI---PDTVSIDSlkkrfpnFTSLLDYF 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 705 RKYAPSETGPYGISAevMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGrdpkplpppmklN---- 780
Cdd:cd05168 109 ERTFGDPNSERFKEA--QRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHIIHIDFGFMLS------------Nspgg 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 781 -----------KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDAN-IPDIALEPDKTVKKVQDKFRL 848
Cdd:cd05168 175 lgfetapfkltQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSkLPCFFGGGEFTIEQLRERFKL 254

                       250       260
                ....*....|....*....|..
gi 81885714 849 DLSDEEAVHYMQSLIDESVHAL 870
Cdd:cd05168 255 NLTEEECAQFVDSLIDKSLNNW 276
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 562-883 3.55e-49

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: 177.78  E-value: 3.55e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 562 ESGNRKKKNERLQALLGDNEKMnLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTED--GGKYPVIFKHGD 639
Cdd:cd05177  22 KTASDTRRKEVLKREASRLEDF-FQDVVSCCLPLNPALRVKGIDADACSYFTSNAAPLKISFINANplAKNISIIFKTGD 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 640 DLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFmqfIQSVPVAEVLDT------------EGSIQNFFRKY 707
Cdd:cd05177 101 DLRQDMLVLQIVRVMDNIWLQEGLDMQMIIYRCLSTGKTQGL---VQMVPDAVTLAKihresgligplkENTIEKWFHMH 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 708 APSETGpygiSAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILG---------RDPKPLPPPMK 778
Cdd:cd05177 178 NKLKED----YDKAVRNFFHSCAGWCVVTFILGVCDRHNDNIMLTHSGHMFHIDFGKFLGhaqtfgsikRDRAPFIFTSE 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 779 LNKEMVEgmGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDiaLEPDKTVKKVQDKFRLDLSDEEAVHY 858
Cdd:cd05177 254 MEYFITE--GGKKPQRFQRFVELCCRAYNIVRKHSQLLLNLLEMMLHAGLPE--LKDIQDLKYVYNNLRPQDTDLEATSY 329

                       330       340
                ....*....|....*....|....*
gi 81885714 859 MQSLIDESVHALFAAVVEQIHKFAQ 883
Cdd:cd05177 330 FTKKIKESLECFPVKLNNLIHTLAQ 354
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 565-867 4.79e-49

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: 177.85  E-value: 4.79e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 565 NRKKKNERLQALLGDNE-KMNLSDVELiplPLEPQVKIRGIIPETATLFKSALMPAQLFFKTE--DGGKYPVIFKHGDDL 641
Cdd:cd05173  29 SKAKGKEAMHTCLRQSAyREALSDLQS---PLNPSIILSELNVEKCKYMDSKMKPLWIVYNNKlfGGDSLGIIFKNGDDL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 642 RQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSV-PVAEV-LDTEG----------SIQNFFRKYAP 709
Cdd:cd05173 106 RQDMLTLQILRLMDTLWKEAGLDLRIVPYGCLATGDRSGLIEVVSSAeTIADIqLNSSNvaaaaafnkdALLNWLKEYNS 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 710 SETGPYGIsaevmDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILG---------RDPKPLPPPMKLN 780
Cdd:cd05173 186 GDDLERAI-----EEFTLSCAGYCVATYVLGIGDRHSDNIMVRKNGQLFHIDFGHILGnfkskfgikRERVPFILTYDFI 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 781 KEMVEGMGGtQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDiaLEPDKTVKKVQDKFRLDLSDEEAVHYMQ 860
Cdd:cd05173 261 HVIQQGKTG-NTEKFGRFRQYCEDAYLILRKNGNLFITLFALMLTAGLPE--LTSVKDIQYLKDSLALGKSEEEALKQFR 337


                ....*..
gi 81885714 861 SLIDESV 867
Cdd:cd05173 338 QKFDEAL 344
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 593-862 6.89e-47

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: 171.97  E-value: 6.89e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 593 LPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYP-----VIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKL 667
Cdd:cd00894  57 VPYDPGLRAGALVIEKCKVMASKKKPLWLEFKCADPTALSnetigIIFKHGDDLRQDMLILQILRIMESIWETESLDLCL 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 668 TPYKVLATSTKHGFMQFIQ-SVPVAEVLDTEGSIQNFFRKYAPS----ETGPYGIS-AEVMDTYVKSCAGYCVITYILGV 741
Cdd:cd00894 137 LPYGCISTGDKIGMIEIVKdATTIAKIQQSTVGNTGAFKDEVLNhwlkEKCPIEEKfQAAVERFVYSCAGYCVATFVLGI 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 742 GDRHLDNLLLTKTGKLFHIDFGYILGRdpkpLPPPMKLNKEMVE------------GMGGTQSEQYQEFRKQCYTAFLHL 809
Cdd:cd00894 217 GDRHNDNIMITETGNLFHIDFGHILGN----YKSFLGINKERVPfvltpdflfvmgTSGKKTSLHFQKFQDVCVKAYLAL 292

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 81885714 810 RRYSNLILNLFSLMVDANIPDIALEPDktVKKVQDKFRLDLSDEEAV-HYMQSL 862
Cdd:cd00894 293 RHHTNLLIILFSMMLMTGMPQLTSKED--IEYIRDALTVGKSEEDAKkHFLDQI 344
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
 632-867 1.25e-46

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: 168.59  E-value: 1.25e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 632 PVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSV----PVAEVLDTEG---SIQNFF 704
Cdd:cd00893  29 SLIVKTGDDLKQEQLALQLISQFDQIFKEEGLPLWLRPYEILSLGPDSGIIEMIKNAvsidSLKKKLDSFNkfvSLSDFF 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 705 RKYAPSETGPYGIsaevmDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNK--- 781
Cdd:cd00893 109 DDNFGDEAIQKAR-----DNFLQSLVAYSLVCYFLQIKDRHNGNILLDKEGHIIHIDFGFFLSSHPGFYGFEGAPFKlss 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 782 EMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEpdKTVKKVQDKFRLDLSDEEAVHYMQS 861
Cdd:cd00893 184 EYIEVLGGVDSELFKEFRKLFLKGFMALRKHSDKILSLVEMMYSGHGITCFGK--KTIQQLKQRFNPELTEGELEVYVLS 261


                ....*.
gi 81885714 862 LIDESV 867
Cdd:cd00893 262 LINKSL 267
PI3Kc_C2_alpha cd05176
Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 539-883 1.40e-43

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: 162.07  E-value: 1.40e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 539 RSLLAAQQTFVDRLVHLMKAVQRESGNRKKKN-----ERLQALLGDNEkmnlsdvelIPLPLEPQVKIRGIIPETATLFK 613
Cdd:cd05176   1 REELEKQTRLVQLLGRVAEKVRQASGSARQVAlqdgmERVQSFFQKNK---------CRLPLSPSLVAKELNIKACSFFS 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 614 SALMPAQLFFKTED--GGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVA 691
Cdd:cd05176  72 SNAVPLKVALVNADplGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLQEGLDLRMVIFKCLSTGKDRGMVELVPSSDTL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 692 EVLDTE----GSIQN-----FFRKYAPSETgPYGISAEvmdTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDF 762
Cdd:cd05176 152 RKIQVEygvtGSFKDkplaeWLRKYNPSEE-EYEKASE---NFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDF 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 763 GYILG---------RDpkPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIAL 833
Cdd:cd05176 228 GKFLGhaqmfgsfkRD--RAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNLIRKHTNLFLNLLSLMLSSGLPELTG 305

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 81885714 834 EPDktVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQ 883
Cdd:cd05176 306 IQD--LKYVFDALQPQTTDAEATIFFTRLIESSLGSVATKFNFFIHNLAQ 353
PI3Kc_C2_beta cd00895
Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 593-883 5.84e-43

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: 160.17  E-value: 5.84e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 593 LPLEPQVKIRGIIPETATLFKSALMPAQLFFKTED--GGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPY 670
Cdd:cd00895  52 LPLSPSLLVKGIVPRDCSYFNSNAVPLKLSFQNVDplGENIRVIFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIF 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 671 KVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFR---------KYAPSETGpygiSAEVMDTYVKSCAGYCVITYILGV 741
Cdd:cd00895 132 RCFSTGRGRGMVEMIPNAETLRKIQVEHGVTGSFKdrpladwlqKHNPTEDE----YEKAVENFIYSCAGCCVATYVLGI 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 742 GDRHLDNLLLTKTGKLFHIDFGYILG---------RDpkPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRY 812
Cdd:cd00895 208 CDRHNDNIMLKTTGHMFHIDFGRFLGhaqmfgnikRD--RAPFVFTSDMAYVINGGDKPSSRFHDFVDLCCQAYNLIRKH 285

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81885714 813 SNLILNLFSLMVDANIPDIALEPDktVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQ 883
Cdd:cd00895 286 THLFLNLLGLMLSCGIPELSDLED--LKYVYDALRPQDTEADATTYFTRLIESSLGSVATKLNFFIHNLAQ 354
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 542-869 1.71e-36

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: 141.73  E-value: 1.71e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 542 LAAQQTFVDRLVHLMKAVQRESGNRKKKNErLQALLGDNEKMNLSD-VELIPLPLEPQVKIRGIIPETATLFKSALMP-- 618
Cdd:cd05175   8 LSRQVEAMEKLINLTDILKQEKKDETQKVQ-MKFLVEQMRRPDFMDaLQGFLSPLNPAHQLGNLRLEECRIMSSAKRPlw 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 619 ---------AQLFFKTEDggkypVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVP 689
Cdd:cd05175  87 lnwenpdimSELLFQNNE-----IIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSH 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 690 VAEVLDTEGSIQNFFRKYAPS------ETGPYGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFG 763
Cdd:cd05175 162 TIMQIQCKGGLKGALQFNSHTlhqwlkDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFG 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 764 YIL-------GRDPKPLPPPMKLNKEMVEGMGG---TQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDiaL 833
Cdd:cd05175 242 HFLdhkkkkfGYKRERVPFVLTQDFLIVISKGAqecTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPE--L 319

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 81885714 834 EPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHA 869
Cdd:cd05175 320 QSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHG 355
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
 618-825 7.46e-36

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: 135.15  E-value: 7.46e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 618 PAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFmqfIQSVPVAEVLdtE 697
Cdd:cd00142  17 PKKITLIGADGKTYSFLLKRRDDLRKDERSFQFMRLIQSILEKESVNLVLPPYKVIPLSENSGL---IEIVKDAQTI--E 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 698 GSIQNFFRKyAPSETGpygiSAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPM 777
Cdd:cd00142  92 DLLKSLWRK-SPSSQS----WLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIMIEPSGNIFHIDFGFIFSGRKLAEGVET 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 81885714 778 KL---NKEMVEGMGGTQSEQYqeFRKQCYTAFLHLRRYSNLILNLFSLMVD 825
Cdd:cd00142 167 VPfrlTPMLENAMGTAGVNGP--FQISMVKIMEILREHADLIVPILEHSLR 215
C2_PI3K_like cd08380
C2 domain present in phosphatidylinositol 3-kinases (PI3Ks); C2 domain present in all classes ...
 34-186 8.35e-34

C2 domain present in phosphatidylinositol 3-kinases (PI3Ks); C2 domain present in all classes of PI3Ks. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. In addition some PI3Ks contain a Ras-binding domain and/or a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains members with the first C2 repeat, C2A, and a type-I topology, as well as some with a single C2 repeat.


Pssm-ID: 176026  Cd Length: 156  Bit Score: 127.09  E-value: 8.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  34 SYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLaLPVRTSYKA-FSTRWNWNEWLKLPVKYPDLPRNAQVALTIWD 112
Cdd:cd08380   7 NFNLRIKIHGITNINLLDSEDLKLYVRVQLYHGGEPL-CPPQSTKKVpFSTSVTWNEWLTFDILISDLPREARLCLSIYA 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81885714 113 VYGPGS--AVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTrtpgrTSSTLSEDQMSRLAKLTKAHRQGH 186
Cdd:cd08380  86 VSEPGSkkEVPLGWVNVPLFDYKGKLRQGMITLNLWPGKKTDPRIAC-----TPCNNSNENSTRLLIELPEFSKPV 156
PI3K_C2 smart00142
Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.
 21-123 6.29e-33

Phosphoinositide 3-kinase, region postulated to contain C2 domain; Outlier of C2 family.


Pssm-ID: 214536  Cd Length: 100  Bit Score: 122.46  E-value: 6.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714     21 LKIGSLEG-KREQKSYKAVLEDPMLKFSGLYqetcSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPD 99
Cdd:smart00142   1 VKIESLWDcDRNLVITIALIHGIPLNWSRDY----SDLYVEIQLYHGGKLLCLPVSTSYKPFFPSVKWNEWLTFPIQISD 76

                           90       100
                   ....*....|....*....|....
gi 81885714    100 LPRNAQVALTIWDVYGPGSAVPVG 123
Cdd:smart00142  77 LPREARLCITIYAVKNPSKGSEFG 100
PI3Ka_I cd00872
Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all ...
 293-410 6.77e-33

Phosphoinositide 3-kinase (PI3K) class I, accessory domain ; PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, PI3K class I prefer phosphoinositol (4,5)-bisphosphate as a substrate. Mammalian members interact with active Ras. They form heterodimers with adapter molecules linking them to different signaling pathways.


Pssm-ID: 238444  Cd Length: 171  Bit Score: 125.12  E-value: 6.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 293 RDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYT 372
Cdd:cd00872   4 REQLEAIIARDPLSELTEEDKELLWKLRHECRKKPQALPKLLLSVKWNKRDDVAQMYQLLKRWPKLKPEQALELLDCNFP 83

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 81885714 373 NPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDD 410
Cdd:cd00872  84 DEHVREFAVRCLEKLSDDELLQYLLQLVQVLKYEPYHD 121
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
 601-824 3.46e-28

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: 113.14  E-value: 3.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 601 IRGIIPETaTLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKEN----LDLKLTPYKVLATS 676
Cdd:cd05164   1 IASFDPRV-RILASLQKPKKITILGSDGKEYPFLVKGDDDLRKDERVMQLFQLLNTLLEKDKetrkRNLTIRTYSVVPLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 677 TKHGFMQFI-QSVPVAEVLdtegsiQNFFRKYAPSETGPYgisaEVMDTYVKSCAGYCVITYILGVGDRHLDNLLL-TKT 754
Cdd:cd05164  80 SQSGLIEWVdNTTTLKPVL------KKWFNETFPDPTQWY----EARSNYTKSTAVMSMVGYIIGLGDRHLENILIdTKT 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81885714 755 GKLFHIDFGYILGRDPKPLPPPMK---LNKEMVEGMGGTQSEqyQEFRKQCYTAFLHLRRYSNLILNLFSLMV 824
Cdd:cd05164 150 GEVVHIDFGMIFNKGKTLPVPEIVpfrLTRNIINGMGPTGVE--GLFRKSCEQVLRVFRKHKDKLITFLDTFL 220
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
 607-767 7.67e-28

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: 112.67  E-value: 7.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 607 ETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKE----NLDLKLTPYKVLATSTKHGFM 682
Cdd:cd05172   6 PRVLVLSSKRRPKRITIRGSDEKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDpacrQRRLRIRTYQVIPMTSRLGLI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 683 QFIQ-SVPVAEVLdTEGSIQNFFRKYAPSETGPYGISaevmDTYVKSCAGYCVITYILGVGDRHLDNLLL-TKTGKLFHI 760
Cdd:cd05172  86 EWVDnTTPLKEIL-ENDLLRRALLSLASSPEAFLALR----SNFARSLAAMSICGYILGIGDRHLSNFLVdLSTGRLIGI 160


                ....*..
gi 81885714 761 DFGYILG 767
Cdd:cd05172 161 DFGHAFG 167
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 627-817 2.29e-22

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: 98.00  E-value: 2.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 627 DGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKE----NLDLKLTPYKVLATSTKHGFMQFIQ-SVPVAEVLDTEGSIQ 701
Cdd:cd05171  26 DGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLKRDketrKRKLRIRTYKVVPLSPRSGVLEFVEnTIPLGEYLVGASSKS 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 702 NFFRKYAPSETGPYGISAEVMD-------------------------------------------TYVKSCAGYCVITYI 738
Cdd:cd05171 106 GAHARYRPKDWTASTCRKKMREkakasaeerlkvfdeicknfkpvfrhfflekfpdpsdwferrlAYTRSVATSSIVGYI 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 739 LGVGDRHLDNLLL-TKTGKLFHIDFGYI----------------LGRDpkplpppmklnkeMVEGMGGTQSEqyQEFRKQ 801
Cdd:cd05171 186 LGLGDRHLNNILIdQKTGELVHIDLGIAfeqgkllpipetvpfrLTRD-------------IVDGMGITGVE--GVFRRC 250

                       250
                ....*....|....*.
gi 81885714 802 CYTAFLHLRRYSNLIL 817
Cdd:cd05171 251 CEETLRVLRENKEALL 266
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 607-825 9.16e-21

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: 92.18  E-value: 9.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 607 ETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK----ENLDLKLTPYKVLATSTKHGFM 682
Cdd:cd00892   6 DEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKdpesRRRNLHIRTYAVIPLNEECGII 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 683 QFIQ-SVPVAEVLDTEGS--IQNFFRKYAPSETGPYgisaEVMDTYVKSCAGYCVITYILGVGDRHLDNLLL-TKTGKLF 758
Cdd:cd00892  86 EWVPnTVTLRSILSTLYPpvLHEWFLKNFPDPTAWY----EARNNYTRSTAVMSMVGYILGLGDRHGENILFdSTTGDVV 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81885714 759 HIDFGYILGRDPKPLPppmklnKE---------MVEGMGGTQSEqyQEFRKQCYTAFLHLRRYSNLILN-LFSLMVD 825
Cdd:cd00892 162 HVDFDCLFDKGLTLEV------PErvpfrltqnMVDAMGVTGVE--GTFRRTCEVTLRVLRENRETLMSvLETFVHD 230
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 601-763 4.23e-16

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: 79.45  E-value: 4.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 601 IRGIIPeTATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENL----DLKLTPYKVLATS 676
Cdd:cd05169   1 ISSFDP-TLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDERVMQLFGLVNTLLKNDSEtsrrNLSIQRYSVIPLS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 677 TKHGFMQFIQ----------------SVPV-AEVLDTEGSIQNFFR----------KYAPSETGPYGI---------SAE 720
Cdd:cd05169  80 PNSGLIGWVPgcdtlhslirdyrekrKIPLnIEHRLMLQMAPDYDNltliqkvevfEYALENTPGDDLrrvlwlkspSSE 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 81885714 721 V----MDTYVKSCAGYCVITYILGVGDRHLDNLLL-TKTGKLFHIDFG 763
Cdd:cd05169 160 AwlerRTNFTRSLAVMSMVGYILGLGDRHPSNIMLdRLTGKVIHIDFG 207
PI3Ka_II cd00869
Phosphoinositide 3-kinase (PI3K) class II, accessory domain (PIK domain); PIK domain is ...
 305-406 1.24e-15

Phosphoinositide 3-kinase (PI3K) class II, accessory domain (PIK domain); PIK domain is conserved in all PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. In general, class II PI3-kinases phosphorylate phosphoinositol (PtdIns), PtdIns(4)-phosphate, but not PtdIns(4,5)-bisphosphate. They are larger, having a C2 domain at the C-terminus.


Pssm-ID: 238441  Cd Length: 169  Bit Score: 75.57  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 305 TKQLTY----EEQDLVWKFRYYLTNQEKALTKFLKCV-NWDLPQEAKqALELLGKWKPMDVEDSLELLSSHYTNPTVRRY 379
Cdd:cd00869  12 QKQSTYtlstEDKDLLWEKRLYCTNEPNALPLVLASApSWDWANLMD-VYQLLHQWAPLRPLIALELLLPKFPDQEVRAH 90

                        90       100
                ....*....|....*....|....*..
gi 81885714 380 AVARLRQADDEDLLMYLLQLVQALKYE 406
Cdd:cd00869  91 AVQWLARLSNDELLDYLPQLVQALKFE 117
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
 618-762 1.75e-10

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: 63.04  E-value: 1.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 618 PAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENL----DLKLTPYKVLATSTKHGFMQFIQ-SVPV-- 690
Cdd:cd05170  17 PKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEhrrrRYRARHYSVTPLGPRSGLIQWVDgATPLfs 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 691 ---------AEVLDTEGSIQN------------FFRKYAP-----------------------------SETGPYGISAE 720
Cdd:cd05170  97 lykrwqqrrAAAQAQKNQDSGstpppvprpselFYNKLKPalkaagirkstsrrewplevlrqvleelvAETPRDLLARE 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 81885714 721 -------------VMDTYVKSCAGYCVITYILGVGDRHLDNLLLT-KTGKLFHIDF 762
Cdd:cd05170 177 lwcsspssaewwrVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDlSTGEVVHIDY 232
C2A_PI3K_class_II cd04012
C2 domain first repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 ...
 55-160 1.47e-09

C2 domain first repeat present in class II phosphatidylinositol 3-kinases (PI3Ks); There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a N-terminal C2 domain, a PIK domain, and a kinase catalytic domain. Unlike class I and class III, class II PI3Ks have additionally a PX domain and a C-terminal C2 domain containing a nuclear localization signal both of which bind phospholipids though in a slightly different fashion. Class II PIK3s act downstream of receptors for growth factors, integrins, and chemokines. PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175979  Cd Length: 171  Bit Score: 57.75  E-value: 1.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  55 SDLYVTCQVFAEGKPLALPV----RTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTiwdVYG------------PGS 118
Cdd:cd04012  29 EDFYLSCSLYHGGRLLCSPVttkpVKITKSFFPRVVWDEWIEFPIPVCQLPRESRLVLT---LYGttsspdggsnkqRMG 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 81885714 119 AVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTP 160
Cdd:cd04012 106 PEELGWVSLPLFDFRGVLRQGSLLLGLWPPSKDNPLGPAPPP 147
C2_PI3K_class_I_alpha cd08398
C2 domain present in class I alpha phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 57-147 1.67e-08

C2 domain present in class I alpha phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, alpha isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology.


Pssm-ID: 176043  Cd Length: 158  Bit Score: 54.41  E-value: 1.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  57 LYVTCQVFAEGKPLALPVRTSYKAFSTRWnWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGSA----VPVGGTTVSLFGK 132
Cdd:cd08398  28 IYVRTGIYHGGEPLCDNVNTQRVPCSNPR-WNEWLDYDIYIPDLPRSARLCLSICSVKGRKGAkeehCPLAWGNINLFDY 106

                        90
                ....*....|....*
gi 81885714 133 YGMFRQGMHDLKVWP 147
Cdd:cd08398 107 TDTLVSGKMALNLWP 121
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 617-763 2.33e-08

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: 53.60  E-value: 2.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 617 MPAQLFFKTEDGGKYPVIFKHGDDlRQDQLILQIISLMDKLLRKENLDLklTPYKVLATSTKHGF----MQFIQSVPVAE 692
Cdd:cd13968   5 ASAKVFWAEGECTTIGVAVKIGDD-VNNEEGEDLESEMDILRRLKGLEL--NIPKVLVTEDVDGPnillMELVKGGTLIA 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81885714 693 VLDTEGSiqnffrkyapSETGPYGIsaevmdtyVKSCAGYCVITYILGV--GDRHLDNLLLTKTGKLFHIDFG 763
Cdd:cd13968  82 YTQEEEL----------DEKDVESI--------MYQLAECMRLLHSFHLihRDLNNDNILLSEDGNVKLIDFG 136
PI4Ka cd00871
Phosphoinositide 4-kinase(PI4K), accessory domain (PIK domain); PIK domain is conserved in PI3 ...
 297-423 8.32e-06

Phosphoinositide 4-kinase(PI4K), accessory domain (PIK domain); PIK domain is conserved in PI3 and PI4-kinases. Its role is unclear but it has been suggested to be involved in substrate presentation. PI4K phosphorylates hydroxylgroup at position 4 on the inositol ring of phosphoinositide, the first commited step in the phosphatidylinositol cycle.


Pssm-ID: 238443  Cd Length: 175  Bit Score: 46.97  E-value: 8.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714 297 NIIVSYP---PTKQLTYEEQDLVWKFRYYLTNQEKALtKFLkcVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHY-T 372
Cdd:cd00871   7 RLAIHLPsrfPNSKLKSEVTRLVRKHPLAVVKIPEAL-PFL--VTGKSVDENSPDLKYLLYWAPVSPVQALSLFTPQYpG 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 81885714 373 NPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQ 423
Cdd:cd00871  84 HPLVLQYAVRVLESYPVETVFFYIPQIVQALRYDKMGYVEEYILETAKRSQ 134
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 597-766 4.08e-04

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 44.31  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   597 PQVKIRGIIPETatLFKSalMPAQLFFktedggkypvIFKHgDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATS 676
Cdd:PTZ00303 1032 PVTAVNGVSPES--LHDS--LPQECMF----------LYKR-ENVERDQLMCISSRLLQMLLSSEIGNAEMLDYSVLPLS 1096

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714   677 TKHGFMQFIQSVPVAEVLDTEGSIQNFFRkyapsetgpyGISAEVmdTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGK 756
Cdd:PTZ00303 1097 CDSGLIEKAEGRELSNLDNMDIASYVLYR----------GTRSCI--NFLASAKLFLLLNYIFSIGDRHKGNVLIGTNGA 1164

                         170
                  ....*....|
gi 81885714   757 LFHIDFGYIL 766
Cdd:PTZ00303 1165 LLHIDFRFIF 1174
C2_PI3K_class_I_gamma cd08399
C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA ...
 57-147 4.32e-04

C2 domain present in class I gamma phosphatidylinositol 3-kinases (PI3Ks); PI3Ks (AKA phosphatidylinositol (PtdIns) 3-kinases) regulate cell processes such as cell growth, differentiation, proliferation, and motility. PI3Ks work on phosphorylation of phosphatidylinositol, phosphatidylinositide (4)P (PtdIns (4)P),2 or PtdIns(4,5)P2. Specifically they phosphorylate the D3 hydroxyl group of phosphoinositol lipids on the inositol ring. There are 3 classes of PI3Ks based on structure, regulation, and specificity. All classes contain a C2 domain, a PIK domain, and a kinase catalytic domain. The members here are class I, gamma isoform PI3Ks and contain both a Ras-binding domain and a p85-binding domain. Class II PI3Ks contain both of these as well as a PX domain, and a C-terminal C2 domain containing a nuclear localization signal. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members have a type-I topology.


Pssm-ID: 176044  Cd Length: 178  Bit Score: 42.21  E-value: 4.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81885714  57 LYVTCQVFaEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPG-SAVPVGGTTVS------- 128
Cdd:cd08399  32 VFVEANIQ-HGQQVLCQRRTSPKPFTEEVLWNTWLEFDIKIKDLPKGALLNLQIYCGKAPAlSSKKSAESPSSeskgkhq 110

                        90       100
                ....*....|....*....|....*..
gi 81885714 129 --------LFGKYGMFRQGMHDLKVWP 147
Cdd:cd08399 111 llyyvnllLIDHRFLLRTGEYVLHMWQ 137
 
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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