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Conserved domains on  [gi|2217268219|ref|XP_047278546|]
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phosphatidylinositol 4-kinase beta isoform X3 [Homo sapiens]

Protein Classification

phosphatidylinositol 4-kinase( domain architecture ID 10142440)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 197-505 0e+00

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


:

Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 537.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 197 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd05168     1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 277 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 354
Cdd:cd05168    81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 355 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGcrrcsgssp 434
Cdd:cd05168   161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQG--------- 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217268219 435 sgpmmtvaqvicSQLPCF--HGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 505
Cdd:cd05168   232 ------------SKLPCFfgGGEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
 
Name Accession Description Interval E-value
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 197-505 0e+00

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


Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 537.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 197 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd05168     1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 277 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 354
Cdd:cd05168    81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 355 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGcrrcsgssp 434
Cdd:cd05168   161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQG--------- 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217268219 435 sgpmmtvaqvicSQLPCF--HGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 505
Cdd:cd05168   232 ------------SKLPCFfgGGEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 229-423 7.54e-68

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: 217.94  E-value: 7.54e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  229 VIVKCGDDLRQELLAFQVLKQLQSIWEQE----RVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS---------- 294
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYrkqkgkvldl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  295 ----------------------QLSLLDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGH 352
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPDPS-EDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGH 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217268219  353 IIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQ 423
Cdd:smart00146 160 LFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELML 229
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
211-504 4.40e-57

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 205.79  E-value: 4.40e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  211 RIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIW----EQERVPLWIKPYKILVISADSGMIEPVVNAVS 286
Cdd:COG5032   1781 LQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDT 1860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  287 IHQVKK------------QSQL-------------------------SLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYC 329
Cdd:COG5032   1861 LHSILReyhkrknisidqEKKLaarldnlklllkdefftkatlksppVLYDWFSESFPNP--EDWLTARTNFARSLAVYS 1938

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  330 LVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGGLDGDMFnyYKMLMLQGLIA 407
Cdd:COG5032   1939 VIGYILGLGDRHPGNILIDrSSGHVIHIDFGFILFNAPGRFPFpEKVPFRLTRNIVEAMGVSGVEGS--FRELCETAFRA 2016

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  408 ARKHMDKVVQIVEIMQqgcrRCSGSSPSGpmmtvaqvicsqLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDGS 485
Cdd:COG5032   2017 LRKNADSLMNVLELFV----RDPLIEWRR------------LPCFREIQnnEIVNVLERFRLKLSEKDAEKFVDLLINKS 2080

                          330
                   ....*....|....*....
gi 2217268219  486 MRSITTKLYDGFQYLTNGI 504
Cdd:COG5032   2081 VESLITQATDPFQLATMYI 2099
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 228-422 4.19e-40

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 144.78  E-value: 4.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 228 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLW-IKPYKILVISADSGMIEPVVNAVSIHQ----------------- 289
Cdd:pfam00454   3 GGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPNSETLAYildeygengvpptamvk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 290 ------------VKKQSQLS------LLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 350
Cdd:pfam00454  83 ilhsalnypklkLEFESRISlppkvgLLQWFVKKSPDA--EEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTt 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217268219 351 GHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:pfam00454 161 GKLFHIDFGLCLPDAGKDLPFpEKVPFRLTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLM 231
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 266-363 8.39e-08

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 55.09  E-value: 8.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  266 YKILVISADSGMIEPVvnavsihqvkKQSQLSLLDYFlqEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNI 345
Cdd:PTZ00303  1090 YSVLPLSCDSGLIEKA----------EGRELSNLDNM--DIASYVLYRGTRSCINFLASAKLFLLLNYIFSIGDRHKGNV 1157

                           90
                   ....*....|....*...
gi 2217268219  346 LLDAEGHIIHIDFGFILS 363
Cdd:PTZ00303  1158 LIGTNGALLHIDFRFIFS 1175
 
Name Accession Description Interval E-value
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 197-505 0e+00

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


Pssm-ID: 270712 [Multi-domain]  Cd Length: 292  Bit Score: 537.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 197 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd05168     1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 277 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 354
Cdd:cd05168    81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 355 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGcrrcsgssp 434
Cdd:cd05168   161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQG--------- 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217268219 435 sgpmmtvaqvicSQLPCF--HGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 505
Cdd:cd05168   232 ------------SKLPCFfgGGEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
 201-505 5.13e-150

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: 430.14  E-value: 5.13e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 201 LKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEP 280
Cdd:cd00893     2 FGEDWTDKTERIREKSPYGNLKGWKLVSLIVKTGDDLKQEQLALQLISQFDQIFKEEGLPLWLRPYEILSLGPDSGIIEM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 281 VVNAVSIHQVKKQSQ-----LSLLDYFLQEHGSyttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIH 355
Cdd:cd00893    82 IKNAVSIDSLKKKLDsfnkfVSLSDFFDDNFGD---EAIQKARDNFLQSLVAYSLVCYFLQIKDRHNGNILLDKEGHIIH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 356 IDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqqgcrrCSGSSPS 435
Cdd:cd00893   159 IDFGFFLSSHPGFYGFEGAPFKLSSEYIEVLGGVDSELFKEFRKLFLKGFMALRKHSDKILSLVEMM------YSGHGIT 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 436 gpmmtvaqvicsqlpcFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 505
Cdd:cd00893   233 ----------------CFGKKTIQQLKQRFNPELTEGELEVYVLSLINKSLDNWRTRWYDKYQYFSQGIF 286
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
 227-505 5.48e-101

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: 305.67  E-value: 5.48e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEH 306
Cdd:cd05167    50 QAAIFKVGDDCRQDMLALQLISLFKNIFEEVGLDLYLFPYRVVATGPGCGVIEVIPNSKSRDQIGRETDNGLYEYFLSKY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 307 GSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSP-RNLGFETSAFKLTTEFVDV 385
Cdd:cd05167   130 GDESTPAFQKARRNFIKSMAGYSLVSYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFEISPgGNLGFESAPFKLTKEMVDL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 386 MGG-LDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgcrrcsgsspsgpmmtvaqvicSQLPCFHGsSTIRNLKER 464
Cdd:cd05167   210 MGGsMESEPFKWFVELCVRGYLAVRPYAEAIVSLVELMLD----------------------SGLPCFRG-QTIKNLRER 266

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217268219 465 FHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 505
Cdd:cd05167   267 FALEMSEREAANFMIKLIADSYLKIRTKGYDMFQYYQNGIP 307
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
 200-425 1.45e-80

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


Pssm-ID: 270621 [Multi-domain]  Cd Length: 216  Bit Score: 249.94  E-value: 1.45e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 200 ALKEPWQEKVRRIReGSPYGHLPNWR---LLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 276
Cdd:cd00142     1 NALDVGILKVIHSK-QRPKKITLIGAdgkTYSFLLKRRDDLRKDERSFQFMRLIQSILEKESVNLVLPPYKVIPLSENSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 277 MIEPVVNAVSIHqvkkqsqlSLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHI 356
Cdd:cd00142    80 LIEIVKDAQTIE--------DLLKSLWRKSPSS--QSWLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIMIEPSGNIFHI 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217268219 357 DFGFILSSSPRNLGFETSAFKLTTEFVDVMGGldGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQG 425
Cdd:cd00142   150 DFGFIFSGRKLAEGVETVPFRLTPMLENAMGT--AGVNGPFQISMVKIMEILREHADLIVPILEHSLRD 216
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 229-423 7.54e-68

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: 217.94  E-value: 7.54e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  229 VIVKCGDDLRQELLAFQVLKQLQSIWEQE----RVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS---------- 294
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYrkqkgkvldl 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  295 ----------------------QLSLLDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGH 352
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPDPS-EDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGH 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217268219  353 IIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQ 423
Cdd:smart00146 160 LFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELML 229
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
211-504 4.40e-57

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 205.79  E-value: 4.40e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  211 RIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIW----EQERVPLWIKPYKILVISADSGMIEPVVNAVS 286
Cdd:COG5032   1781 LQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDT 1860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  287 IHQVKK------------QSQL-------------------------SLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYC 329
Cdd:COG5032   1861 LHSILReyhkrknisidqEKKLaarldnlklllkdefftkatlksppVLYDWFSESFPNP--EDWLTARTNFARSLAVYS 1938

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  330 LVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGGLDGDMFnyYKMLMLQGLIA 407
Cdd:COG5032   1939 VIGYILGLGDRHPGNILIDrSSGHVIHIDFGFILFNAPGRFPFpEKVPFRLTRNIVEAMGVSGVEGS--FRELCETAFRA 2016

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  408 ARKHMDKVVQIVEIMQqgcrRCSGSSPSGpmmtvaqvicsqLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDGS 485
Cdd:COG5032   2017 LRKNADSLMNVLELFV----RDPLIEWRR------------LPCFREIQnnEIVNVLERFRLKLSEKDAEKFVDLLINKS 2080

                          330
                   ....*....|....*....
gi 2217268219  486 MRSITTKLYDGFQYLTNGI 504
Cdd:COG5032   2081 VESLITQATDPFQLATMYI 2099
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 229-473 4.67e-45

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: 160.81  E-value: 4.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 229 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAV---SIHQVKKQ-----SQLSLLD 300
Cdd:cd00891    90 VIFKAGDDLRQDQLTLQLLRIMDKLWKKEGLDLRMTPYKCIATGDEVGMIEVVPNSEttaAIQKKYGGfgaafKDTPISN 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 301 YFLQEHGsyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd00891   170 WLKKHNP--TEEEYEEAVENFIRSCAGYCVATYVLGIGDRHNDNIMVTKSGHLFHIDFGHFLGNFKKKFGIkrERAPFVF 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 379 TTEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqqgcrrcsgsspsgpmmtvaqvICSQLPCFHGSSTI 458
Cdd:cd00891   248 TPEMAYVMGGEDSENFQKFEDLCCKAYNILRKHGNLLINLFSLM----------------------LSAGIPELQSIEDI 305

                         250
                  ....*....|....*
gi 2217268219 459 RNLKERFHMSMTEEQ 473
Cdd:cd00891   306 EYLRDALQLDLSDEE 320
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 228-495 1.18e-43

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: 157.69  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 228 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQsQLSLLDYFLQEHG 307
Cdd:cd00896    94 KVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPNDGLVEFVPNSKALADILKK-YGSILNFLRKHNP 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 308 SYTTEAFLSAQ--RNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLgfeTSAFKLTTEFVDV 385
Cdd:cd00896   173 DESGPYGIKPEvmDNFVKSCAGYCVITYILGVGDRHLDNLLLTKDGHLFHIDFGYILGRDPKPF---PPPMKLCKEMVEA 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 386 MGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgcrrcsgsspsgpmmtvaqvicSQLPCFHGSS--TIRNLKE 463
Cdd:cd00896   250 MGGANSEGYKEFKKYCCTAYNILRKHANLILNLFSLMVD----------------------ANIPDIALEPdkAVLKVQE 307

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2217268219 464 RFHMSMTEEQLQLLVEQMVDGSMRSITTKLYD 495
Cdd:cd00896   308 KFRLDLSDEEAEQYFQNLIDESVNALFPAVVE 339
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 228-422 4.19e-40

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 144.78  E-value: 4.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 228 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLW-IKPYKILVISADSGMIEPVVNAVSIHQ----------------- 289
Cdd:pfam00454   3 GGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPNSETLAYildeygengvpptamvk 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 290 ------------VKKQSQLS------LLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 350
Cdd:pfam00454  83 ilhsalnypklkLEFESRISlppkvgLLQWFVKKSPDA--EEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTt 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217268219 351 GHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:pfam00454 161 GKLFHIDFGLCLPDAGKDLPFpEKVPFRLTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLM 231
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 229-411 1.28e-34

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


Pssm-ID: 270709 [Multi-domain]  Cd Length: 363  Bit Score: 133.14  E-value: 1.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 229 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL--------SLLD 300
Cdd:cd05165    98 IIFKNGDDLRQDMLTLQIIRIMDNIWKEEGLDLRMLPYGCLSTGDNVGLIEVVRNAKTIANIQKKKGKvatlafnkDSLH 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 301 YFLQEHgSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd05165   178 KWLKEK-NKTGEKYDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVKENGQLFHIDFGHFLGNFKKKFGIkrERVPFVL 256

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217268219 379 TTEFVDVM----GGLDGDMFNYYKMLMLQGLIAARKH 411
Cdd:cd05165   257 THDFVYVIargqDNTKSEEFQEFQELCEKAYLILRRH 293
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 227-422 8.68e-32

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


Pssm-ID: 270627 [Multi-domain]  Cd Length: 367  Bit Score: 125.75  E-value: 8.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKkQSQL--------SL 298
Cdd:cd00894   100 IGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQ-QSTVgntgafkdEV 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 299 LDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAF 376
Cdd:cd00894   179 LNHWLKEKCPIE-EKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGInkERVPF 257

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217268219 377 KLTTEFVDVMGGLDGDM---FNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:cd00894   258 VLTPDFLFVMGTSGKKTslhFQKFQDVCVKAYLALRHHTNLLIILFSMM 306
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 227-422 1.56e-31

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: 124.32  E-value: 1.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL------SLLD 300
Cdd:cd05166    91 ISVIFKVGDDLRQDMLTLQLIRIMDKIWLQEGLDLKMITFRCVPTGNKRGMVELVPEAETLREIQTEHGLtgsfkdRPLA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 301 YFLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd05166   171 DWLQKHNP-SELEYEKAVENFIRSCAGYCVATYVLGICDRHNDNIMLKTSGHLFHIDFGKFLGDAQMFGNFkrDRVPFVL 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217268219 379 TTEFVDVMGGLD--GDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:cd05166   250 TSDMAYVINGGDkpSSRFQLFVDLCCQAFNIIRKNSNLLLNLLSLM 295
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 227-422 4.87e-29

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


Pssm-ID: 270721 [Multi-domain]  Cd Length: 354  Bit Score: 117.69  E-value: 4.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL-------SLL 299
Cdd:cd05177    92 ISIIFKTGDDLRQDMLVLQIVRVMDNIWLQEGLDMQMIIYRCLSTGKTQGLVQMVPDAVTLAKIHRESGLigplkenTIE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 300 DYFLQEHgsYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFK 377
Cdd:cd05177   172 KWFHMHN--KLKEDYDKAVRNFFHSCAGWCVVTFILGVCDRHNDNIMLTHSGHMFHIDFGKFLGHAQTFGSIkrDRAPFI 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217268219 378 LTTE--FVDVMGGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:cd05177   250 FTSEmeYFITEGGKKPQRFQRFVELCCRAYNIVRKHSQLLLNLLEMM 296
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 226-493 2.42e-26

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: 110.05  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 226 LLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS----------Q 295
Cdd:cd05173    94 SLGIIFKNGDDLRQDMLTLQILRLMDTLWKEAGLDLRIVPYGCLATGDRSGLIEVVSSAETIADIQLNSsnvaaaaafnK 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 296 LSLLDYfLQEHGSytTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ET 373
Cdd:cd05173   174 DALLNW-LKEYNS--GDDLERAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVRKNGQLFHIDFGHILGNFKSKFGIkrER 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 374 SAFKLTTEFVDVM-GGLDGDM--FNYYKMLMLQGLIAARKHMDKVVQIVEIMqqgcrrcsgsspsgpmmtvaqvICSQLP 450
Cdd:cd05173   251 VPFILTYDFIHVIqQGKTGNTekFGRFRQYCEDAYLILRKNGNLFITLFALM----------------------LTAGLP 308

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2217268219 451 CFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMR-SITTKL 493
Cdd:cd05173   309 ELTSVKDIQYLKDSLALGKSEEEALKQFRQKFDEALReSWTTKV 352
PI3Kc_C2_alpha cd05176
Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 227-493 3.60e-26

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: 109.30  E-value: 3.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL--SLLDYFLQ 304
Cdd:cd05176    91 INVMFKVGEDLRQDMLALQMIKIMDKIWLQEGLDLRMVIFKCLSTGKDRGMVELVPSSDTLRKIQVEYGVtgSFKDKPLA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 305 E---HGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKLT 379
Cdd:cd05176   171 EwlrKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFkrDRAPFVLT 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 380 TEFVDVMGGLDGDM--FNYYKMLMLQGLIAARKHMDKVVQIVEIMqqgcrrcsgsspsgpmmtvaqvICSQLPCFHGSST 457
Cdd:cd05176   251 SDMAYVINGGEKPTirFQLFVDLCCQAYNLIRKHTNLFLNLLSLM----------------------LSSGLPELTGIQD 308

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2217268219 458 IRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKL 493
Cdd:cd05176   309 LKYVFDALQPQTTDAEATIFFTRLIESSLGSVATKF 344
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 229-493 8.72e-25

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: 105.53  E-value: 8.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 229 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLS--------LLD 300
Cdd:cd05175   105 IIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKgalqfnshTLH 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 301 YFLQEHGSytTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 378
Cdd:cd05175   185 QWLKDKNK--GEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYkrERVPFVL 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 379 TTEFVDVMGG-----LDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqqgcrrcsgsspsgpmmtvaqvICSQLPCFH 453
Cdd:cd05175   263 TQDFLIVISKgaqecTKTREFERFQEMCYKAYLAIRQHANLFINLFSMM----------------------LGSGMPELQ 320

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217268219 454 GSSTIRNLKERFHMSMTE-EQLQLLVEQMVDGSMRSITTKL 493
Cdd:cd05175   321 SFDDIAYIRKTLALDKTEqEALEYFMKQMNDAHHGGWTTKM 361
PI3Kc_C2_beta cd00895
Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 227-422 1.30e-24

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: 104.70  E-value: 1.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLS-------LL 299
Cdd:cd00895    92 IRVIFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHGVTgsfkdrpLA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 300 DYfLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPR--NLGFETSAFK 377
Cdd:cd00895   172 DW-LQKHNP-TEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMfgNIKRDRAPFV 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217268219 378 LTTEFVDVMGGLD--GDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 422
Cdd:cd00895   250 FTSDMAYVINGGDkpSSRFHDFVDLCCQAYNLIRKHTHLFLNLLGLM 296
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
 227-473 2.39e-24

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: 104.36  E-value: 2.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 227 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQ----------SQL 296
Cdd:cd05174    98 VGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLSTGDKTGLIEVVLHSDTIANIQLNksnmaataafNKD 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 297 SLLDYFLQEHGSyttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETS 374
Cdd:cd05174   178 ALLNWLKSKNPG---DALDQAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGInrERV 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 375 AFKLTTEFVDVM---GGLDGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqqgcrRCSGsspsgpmmtvaqvicsqLPC 451
Cdd:cd05174   255 PFILTYDFVHVIqqgKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALM-----KAAG-----------------LPE 312

                         250       260
                  ....*....|....*....|..
gi 2217268219 452 FHGSSTIRNLKERFHMSMTEEQ 473
Cdd:cd05174   313 LSCSKDIQYLKDSLALGKTEEE 334
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
 230-411 6.66e-22

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: 94.56  E-value: 6.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 230 IVKCGDDLR-----QELLAF--QVLKQLQSIWEQErvpLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSqlsLLDYF 302
Cdd:cd05172    33 LVKGGEDLRqdqriQQLFDVmnNILASDPACRQRR---LRIRTYQVIPMTSRLGLIEWVDNTTPLKEILEND---LLRRA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 303 LQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTT 380
Cdd:cd05172   107 LLSLAS-SPEAFLALRSNFARSLAAMSICGYILGIGDRHLSNFLVDlSTGRLIGIDFGHAFGSATQFLPIpELVPFRLTR 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217268219 381 EFVDVMGGLDGDmfNYYKMLMLQGLIAARKH 411
Cdd:cd05172   186 QLLNLLQPLDAR--GLLRSDMVHVLRALRAG 214
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
 230-422 6.75e-22

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: 93.88  E-value: 6.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 230 IVKCGDDLRQE---LLAFQVL-KQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVkkqsqlsLLDYFLqe 305
Cdd:cd05164    33 LVKGDDDLRKDervMQLFQLLnTLLEKDKETRKRNLTIRTYSVVPLSSQSGLIEWVDNTTTLKPV-------LKKWFN-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 306 HGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVD 384
Cdd:cd05164   104 ETFPDPTQWYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKtGEVVHIDFGMIFNKGKTLPVPEIVPFRLTRNIIN 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2217268219 385 VMG--GLDGdmfNYYKMlMLQGLIAARKHMDKVVQIVEIM 422
Cdd:cd05164   184 GMGptGVEG---LFRKS-CEQVLRVFRKHKDKLITFLDTF 219
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 230-391 1.15e-16

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


Pssm-ID: 270715 [Multi-domain]  Cd Length: 282  Bit Score: 80.28  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 230 IVKCGDDLRQELLAFQVLKQLQSIWEQERVP----LWIKPYKILVISADSGMIEPVVNAVSIHQV--------------- 290
Cdd:cd05171    33 LVKGGDDLRQDAVMEQVFELVNQLLKRDKETrkrkLRIRTYKVVPLSPRSGVLEFVENTIPLGEYlvgassksgaharyr 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 291 ----------KKQSQLSLLD--------------------YFLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDR 340
Cdd:cd05171   113 pkdwtastcrKKMREKAKASaeerlkvfdeicknfkpvfrHFFLEKFP-DPSDWFERRLAYTRSVATSSIVGYILGLGDR 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217268219 341 HNGNILLDAE-GHIIHIDFGFI-----LSSSPrnlgfETSAFKLTTEFVDVMG--GLDG 391
Cdd:cd05171   192 HLNNILIDQKtGELVHIDLGIAfeqgkLLPIP-----ETVPFRLTRDIVDGMGitGVEG 245
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 225-391 1.12e-11

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


Pssm-ID: 270625 [Multi-domain]  Cd Length: 237  Bit Score: 64.83  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 225 RLLSVIVKCGDDLRQEL----LAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSI-HQVKKQSQLSLL 299
Cdd:cd00892    28 KKYPFLCKPKDDLRKDArmmeFNTLINRLLSKDPESRRRNLHIRTYAVIPLNEECGIIEWVPNTVTLrSILSTLYPPVLH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 300 DYFLQEHGSYTteAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDF------GFILsSSPrnlgfE 372
Cdd:cd00892   108 EWFLKNFPDPT--AWYEARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTtGDVVHVDFdclfdkGLTL-EVP-----E 179

                         170       180
                  ....*....|....*....|.
gi 2217268219 373 TSAFKLTTEFVDVMG--GLDG 391
Cdd:cd00892   180 RVPFRLTQNMVDAMGvtGVEG 200
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 236-421 4.88e-08

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: 54.41  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 236 DLRQELLAFQVLKQLQSIWEQERVP----LWIKPYKILVISADSGMIEPVVNAVSIHQVKKQ------------------ 293
Cdd:cd05169    39 DLRLDERVMQLFGLVNTLLKNDSETsrrnLSIQRYSVIPLSPNSGLIGWVPGCDTLHSLIRDyrekrkiplniehrlmlq 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 294 -----SQLSLLD-YFLQEHG----------------SYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 350
Cdd:cd05169   119 mapdyDNLTLIQkVEVFEYAlentpgddlrrvlwlkSPSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLt 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 351 GHIIHIDFGFIlsssprnlgFETSA----------FKLTTEFVDVMG--GLDGdmfNYYK-----MLMLqgliaaRKHMD 413
Cdd:cd05169   199 GKVIHIDFGDC---------FEVAMhrekfpekvpFRLTRMLVNAMEvsGVEG---TFRStcedvMRVL------RENKD 260


                  ....*...
gi 2217268219 414 KVVQIVEI 421
Cdd:cd05169   261 SLMAVLEA 268
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
 266-363 8.39e-08

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 55.09  E-value: 8.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219  266 YKILVISADSGMIEPVvnavsihqvkKQSQLSLLDYFlqEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNI 345
Cdd:PTZ00303  1090 YSVLPLSCDSGLIEKA----------EGRELSNLDNM--DIASYVLYRGTRSCINFLASAKLFLLLNYIFSIGDRHKGNV 1157

                           90
                   ....*....|....*...
gi 2217268219  346 LLDAEGHIIHIDFGFILS 363
Cdd:PTZ00303  1158 LIGTNGALLHIDFRFIFS 1175
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
 307-391 1.89e-06

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


Pssm-ID: 270714  Cd Length: 304  Bit Score: 49.56  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268219 307 GSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDFgfilsssprNLGF---------ETSAF 376
Cdd:cd05170   180 SSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLStGEVVHIDY---------NVCFekgkrlrvpEKVPF 250

                          90
                  ....*....|....*..
gi 2217268219 377 KLTTEFVDVMG--GLDG 391
Cdd:cd05170   251 RLTQNIEHALGptGVEG 267
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 309-359 3.48e-03

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 37.81  E-value: 3.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217268219 309 YTTEAFLSAQRN--FVQSCAGYCLVCYLLQV--KDRHNGNILLDAEGHIIHIDFG 359
Cdd:cd13968    82 YTQEEELDEKDVesIMYQLAECMRLLHSFHLihRDLNNDNILLSEDGNVKLIDFG 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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