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Conserved domains on  [gi|14389295|ref|NP_112345|]
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phosphatidylinositol 4-kinase beta [Rattus norvegicus]

Protein Classification

phosphatidylinositol 4-kinase beta( domain architecture ID 16908555)

phosphatidylinositol 4-kinase beta (PI4KB) 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
EC:  2.7.1.67
Gene Symbol:  PI4KB
Gene Ontology:  GO:0004430|GO:0016310|GO:0005524
PubMed:  16793271|16244704
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 ...
529-816 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: 552.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 529 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 608
Cdd:cd05168   1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 609 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 686
Cdd:cd05168  81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 687 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCF--H 764
Cdd:cd05168 161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSKLPCFfgG 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 14389295 765 GSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 816
Cdd:cd05168 241 GEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
PI4KB_NTD cd22246
N-terminal domain of phosphatidylinositol 4-kinase beta; Phosphatidylinositol 4-kinase beta ...
2-66 1.17e-31

N-terminal domain of phosphatidylinositol 4-kinase beta; Phosphatidylinositol 4-kinase beta (PI4K-beta, PI4Kbeta or PI4KB), also called PtdIns 4-kinase beta, NPIK, PI4K92, or PI4KIII, catalyzes the phosphorylation of phosphatidylinositol (PI) to form phosphatidylinositol 4-phosphate (PI4P), in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). It may regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. PI4K-beta is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools. It is recruited to membranes via its interaction with Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3). The ACBD3:PI4K-beta complex formation is essential for proper function of the Golgi. PI4K-beta also plays an essential role in Aichi virus RNA replication. It is recruited by ACBD3 at viral replication sites. This model corresponds to the N-terminal domain of PI4K-beta, which is responsible for interacting with ACBD3 by forming a complex with the Q domain.


:

Pssm-ID: 412074  Cd Length: 65  Bit Score: 117.60  E-value: 1.17e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14389295   2 GDMVVEPATLKPTSEPTPSPSGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGV 66
Cdd:cd22246   1 GDTDVEPAPVLLTSEPTSGPPGNGGGGPLSVITEGVGELSVIDPEVAKKACQEVLEKVKLLHGVS 65
 
Name Accession Description Interval E-value
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
529-816 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: 552.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 529 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 608
Cdd:cd05168   1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 609 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 686
Cdd:cd05168  81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 687 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCF--H 764
Cdd:cd05168 161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSKLPCFfgG 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 14389295 765 GSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 816
Cdd:cd05168 241 GEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
561-766 6.60e-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: 224.87  E-value: 6.60e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295    561 VIVKCGDDLRQELLAFQVLKQLQSIWEQE----RVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS---------- 626
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYrkqkgkvldl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295    627 ----------------------QLSLLDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGH 684
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPDPS-EDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGH 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295    685 IIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCF 763
Cdd:smart00146 160 LFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELM-LYDGLPDW 236

                   ...
gi 14389295    764 HGS 766
Cdd:smart00146 237 RSG 239
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
543-815 6.29e-57

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 212.72  E-value: 6.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  543 RIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIW----EQERVPLWIKPYKILVISADSGMIEPVVNAVS 618
Cdd:COG5032 1781 LQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDT 1860
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  619 IHQVKK------------QSQL-------------------------SLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYC 661
Cdd:COG5032 1861 LHSILReyhkrknisidqEKKLaarldnlklllkdefftkatlksppVLYDWFSESFPNP--EDWLTARTNFARSLAVYS 1938
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  662 LVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGGLNGDMFnyYKMLMLQGLIA 739
Cdd:COG5032 1939 VIGYILGLGDRHPGNILIDrSSGHVIHIDFGFILFNAPGRFPFpEKVPFRLTRNIVEAMGVSGVEGS--FRELCETAFRA 2016
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  740 ARKHMDKVVQIVEIMQ-----QGSQLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLT 812
Cdd:COG5032 2017 LRKNADSLMNVLELFVrdpliEWRRLPCFREIQnnEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLAT 2096

                 ...
gi 14389295  813 NGI 815
Cdd:COG5032 2097 MYI 2099
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
560-754 3.20e-39

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: 145.55  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295   560 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLW-IKPYKILVISADSGMIEPVVNAVSIHQ----------------- 621
Cdd:pfam00454   3 GGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPNSETLAYildeygengvpptamvk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295   622 ------------VKKQSQLS------LLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 682
Cdd:pfam00454  83 ilhsalnypklkLEFESRISlppkvgLLQWFVKKSPDA--EEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTt 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14389295   683 GHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 754
Cdd:pfam00454 161 GKLFHIDFGLCLPDAGKDLPFpEKVPFRLTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLM 231
PI4KB_NTD cd22246
N-terminal domain of phosphatidylinositol 4-kinase beta; Phosphatidylinositol 4-kinase beta ...
2-66 1.17e-31

N-terminal domain of phosphatidylinositol 4-kinase beta; Phosphatidylinositol 4-kinase beta (PI4K-beta, PI4Kbeta or PI4KB), also called PtdIns 4-kinase beta, NPIK, PI4K92, or PI4KIII, catalyzes the phosphorylation of phosphatidylinositol (PI) to form phosphatidylinositol 4-phosphate (PI4P), in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). It may regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. PI4K-beta is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools. It is recruited to membranes via its interaction with Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3). The ACBD3:PI4K-beta complex formation is essential for proper function of the Golgi. PI4K-beta also plays an essential role in Aichi virus RNA replication. It is recruited by ACBD3 at viral replication sites. This model corresponds to the N-terminal domain of PI4K-beta, which is responsible for interacting with ACBD3 by forming a complex with the Q domain.


Pssm-ID: 412074  Cd Length: 65  Bit Score: 117.60  E-value: 1.17e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14389295   2 GDMVVEPATLKPTSEPTPSPSGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGV 66
Cdd:cd22246   1 GDTDVEPAPVLLTSEPTSGPPGNGGGGPLSVITEGVGELSVIDPEVAKKACQEVLEKVKLLHGVS 65
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
598-695 2.60e-07

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 54.71  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295   598 YKILVISADSGMIEPVvnavsihqvkKQSQLSLLDYFlqEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNI 677
Cdd:PTZ00303 1090 YSVLPLSCDSGLIEKA----------EGRELSNLDNM--DIASYVLYRGTRSCINFLASAKLFLLLNYIFSIGDRHKGNV 1157
                          90
                  ....*....|....*...
gi 14389295   678 LLDAEGHIIHIDFGFILS 695
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 ...
529-816 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: 552.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 529 SAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 608
Cdd:cd05168   1 SAAAFGESWEEKKERIRKSSPYGHLPGWDLRSVIVKSGDDLRQELLAMQLIKQFQRIFEEAGLPLWLRPYEILVTSSDSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 609 MIEPVVNAVSIHQVKKQSQ--LSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHII 686
Cdd:cd05168  81 LIETIPDTVSIDSLKKRFPnfTSLLDYFERTFGDPNSERFKEAQRNFVESLAAYSLVCYLLQIKDRHNGNILLDSEGHII 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 687 HIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCF--H 764
Cdd:cd05168 161 HIDFGFMLSNSPGGLGFETAPFKLTQEYVEVMGGLESDMFRYFKTLMIQGFLALRKHADRIVLLVEIMQQGSKLPCFfgG 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 14389295 765 GSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 816
Cdd:cd05168 241 GEFTIEQLRERFKLNLTEEECAQFVDSLIDKSLNNWRTRQYDNFQYLTNGIL 292
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
533-816 2.21e-151

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: 444.40  E-value: 2.21e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 533 LKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEP 612
Cdd:cd00893   2 FGEDWTDKTERIREKSPYGNLKGWKLVSLIVKTGDDLKQEQLALQLISQFDQIFKEEGLPLWLRPYEILSLGPDSGIIEM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 613 VVNAVSIHQVKKQSQ-----LSLLDYFLQEHGSyttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIH 687
Cdd:cd00893  82 IKNAVSIDSLKKKLDsfnkfVSLSDFFDDNFGD---EAIQKARDNFLQSLVAYSLVCYFLQIKDRHNGNILLDKEGHIIH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 688 IDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFhGSS 767
Cdd:cd00893 159 IDFGFFLSSHPGFYGFEGAPFKLSSEYIEVLGGVDSELFKEFRKLFLKGFMALRKHSDKILSLVEMMYSGHGITCF-GKK 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 14389295 768 TIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM 816
Cdd:cd00893 238 TIQQLKQRFNPELTEGELEVYVLSLINKSLDNWRTRWYDKYQYFSQGIF 286
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
559-816 2.79e-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: 315.69  E-value: 2.79e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 559 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEH 638
Cdd:cd05167  50 QAAIFKVGDDCRQDMLALQLISLFKNIFEEVGLDLYLFPYRVVATGPGCGVIEVIPNSKSRDQIGRETDNGLYEYFLSKY 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 639 GSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSP-RNLGFETSAFKLTTEFVDV 717
Cdd:cd05167 130 GDESTPAFQKARRNFIKSMAGYSLVSYLLQIKDRHNGNIMIDDDGHIIHIDFGFIFEISPgGNLGFESAPFKLTKEMVDL 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 718 MGG-LNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGsSTIRNLKERFHMSMTEEQLQLLVEQMVDGS 796
Cdd:cd05167 210 MGGsMESEPFKWFVELCVRGYLAVRPYAEAIVSLVELM-LDSGLPCFRG-QTIKNLRERFALEMSEREAANFMIKLIADS 287
                       250       260
                ....*....|....*....|
gi 14389295 797 MRSITTKLYDGFQYLTNGIM 816
Cdd:cd05167 288 YLKIRTKGYDMFQYYQNGIP 307
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
532-757 4.87e-78

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: 251.10  E-value: 4.87e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 532 ALKEPWQEKVRRIReGSPYGHLPNWR---LLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSG 608
Cdd:cd00142   1 NALDVGILKVIHSK-QRPKKITLIGAdgkTYSFLLKRRDDLRKDERSFQFMRLIQSILEKESVNLVLPPYKVIPLSENSG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 609 MIEPVVNAVSIHqvkkqsqlSLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHI 688
Cdd:cd00142  80 LIEIVKDAQTIE--------DLLKSLWRKSPSS--QSWLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIMIEPSGNIFHI 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14389295 689 DFGFILSSSPRNLGFETSAFKLTTEFVDVMGGlnGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQG 757
Cdd:cd00142 150 DFGFIFSGRKLAEGVETVPFRLTPMLENAMGT--AGVNGPFQISMVKIMEILREHADLIVPILEHSLRD 216
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
561-766 6.60e-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: 224.87  E-value: 6.60e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295    561 VIVKCGDDLRQELLAFQVLKQLQSIWEQE----RVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS---------- 626
Cdd:smart00146   1 VIFKGGDDLRQDERVLQLLRLMNKLLQKDketrRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYrkqkgkvldl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295    627 ----------------------QLSLLDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGH 684
Cdd:smart00146  81 rsqtatrlkklelfleatgkfpDPVLYDWFTKKFPDPS-EDYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLDKTGH 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295    685 IIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCF 763
Cdd:smart00146 160 LFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMG--DSGYFGLFRSLCERALRALRKNSNLIMSLLELM-LYDGLPDW 236

                   ...
gi 14389295    764 HGS 766
Cdd:smart00146 237 RSG 239
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
543-815 6.29e-57

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 212.72  E-value: 6.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  543 RIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIW----EQERVPLWIKPYKILVISADSGMIEPVVNAVS 618
Cdd:COG5032 1781 LQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILkkdkETRRRDLWIRPYKVIPLSPGSGIIEWVPNSDT 1860
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  619 IHQVKK------------QSQL-------------------------SLLDYFLQEHGSYttEAFLSAQRNFVQSCAGYC 661
Cdd:COG5032 1861 LHSILReyhkrknisidqEKKLaarldnlklllkdefftkatlksppVLYDWFSESFPNP--EDWLTARTNFARSLAVYS 1938
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  662 LVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGGLNGDMFnyYKMLMLQGLIA 739
Cdd:COG5032 1939 VIGYILGLGDRHPGNILIDrSSGHVIHIDFGFILFNAPGRFPFpEKVPFRLTRNIVEAMGVSGVEGS--FRELCETAFRA 2016
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295  740 ARKHMDKVVQIVEIMQ-----QGSQLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLT 812
Cdd:COG5032 2017 LRKNADSLMNVLELFVrdpliEWRRLPCFREIQnnEIVNVLERFRLKLSEKDAEKFVDLLINKSVESLITQATDPFQLAT 2096

                 ...
gi 14389295  813 NGI 815
Cdd:COG5032 2097 MYI 2099
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
560-806 7.72e-46

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: 167.71  E-value: 7.72e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 560 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQsQLSLLDYFLQEHG 639
Cdd:cd00896  94 KVIFKHGDDLRQDQLVLQIITLMDRLLKKENLDLKLTPYKVLATSPNDGLVEFVPNSKALADILKK-YGSILNFLRKHNP 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 640 SYTTEAFLSAQ--RNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLgfeTSAFKLTTEFVDV 717
Cdd:cd00896 173 DESGPYGIKPEvmDNFVKSCAGYCVITYILGVGDRHLDNLLLTKDGHLFHIDFGYILGRDPKPF---PPPMKLCKEMVEA 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 718 MGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSS--TIRNLKERFHMSMTEEQLQLLVEQMVDG 795
Cdd:cd00896 250 MGGANSEGYKEFKKYCCTAYNILRKHANLILNLFSLM-VDANIPDIALEPdkAVLKVQEKFRLDLSDEEAEQYFQNLIDE 328
                       250
                ....*....|.
gi 14389295 796 SMRSITTKLYD 806
Cdd:cd00896 329 SVNALFPAVVE 339
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
561-784 1.49e-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: 166.59  E-value: 1.49e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 561 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAV---SIHQVKKQ-----SQLSLLD 632
Cdd:cd00891  90 VIFKAGDDLRQDQLTLQLLRIMDKLWKKEGLDLRMTPYKCIATGDEVGMIEVVPNSEttaAIQKKYGGfgaafKDTPISN 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 633 YFLQEHGsyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 710
Cdd:cd00891 170 WLKKHNP--TEEEYEEAVENFIRSCAGYCVATYVLGIGDRHNDNIMVTKSGHLFHIDFGHFLGNFKKKFGIkrERAPFVF 247
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14389295 711 TTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSSTIRNLKERFHMSMTEEQ 784
Cdd:cd00891 248 TPEMAYVMGGEDSENFQKFEDLCCKAYNILRKHGNLLINLFSLM-LSAGIPELQSIEDIEYLRDALQLDLSDEE 320
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
560-754 3.20e-39

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: 145.55  E-value: 3.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295   560 SVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLW-IKPYKILVISADSGMIEPVVNAVSIHQ----------------- 621
Cdd:pfam00454   3 GGIYKVGDDLRQDELILQVFKLMDEELSKDNLDLRrLKPYSVIPLGPKCGIIEWVPNSETLAYildeygengvpptamvk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295   622 ------------VKKQSQLS------LLDYFLQEHGSYttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 682
Cdd:pfam00454  83 ilhsalnypklkLEFESRISlppkvgLLQWFVKKSPDA--EEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTt 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14389295   683 GHIIHIDFGFILSSSPRNLGF-ETSAFKLTTEFVDVMGglNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 754
Cdd:pfam00454 161 GKLFHIDFGLCLPDAGKDLPFpEKVPFRLTREMVYAMG--PSGDEGLFRELCETAYEALRRNLNLLTNLLKLM 231
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
561-743 2.87e-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: 134.68  E-value: 2.87e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 561 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL--------SLLD 632
Cdd:cd05165  98 IIFKNGDDLRQDMLTLQIIRIMDNIWKEEGLDLRMLPYGCLSTGDNVGLIEVVRNAKTIANIQKKKGKvatlafnkDSLH 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 633 YFLQEHgSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 710
Cdd:cd05165 178 KWLKEK-NKTGEKYDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVKENGQLFHIDFGHFLGNFKKKFGIkrERVPFVL 256
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14389295 711 TTEFVDVM----GGLNGDMFNYYKMLMLQGLIAARKH 743
Cdd:cd05165 257 THDFVYVIargqDNTKSEEFQEFQELCEKAYLILRRH 293
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
559-804 1.99e-32

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: 129.33  E-value: 1.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 559 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL------SLLD 632
Cdd:cd05166  91 ISVIFKVGDDLRQDMLTLQLIRIMDKIWLQEGLDLKMITFRCVPTGNKRGMVELVPEAETLREIQTEHGLtgsfkdRPLA 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 633 YFLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 710
Cdd:cd05166 171 DWLQKHNP-SELEYEKAVENFIRSCAGYCVATYVLGICDRHNDNIMLKTSGHLFHIDFGKFLGDAQMFGNFkrDRVPFVL 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 711 TTEFVDVMGGlnGDM----FNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFhGSSTIRNLKERFHMSMTEEQLQ 786
Cdd:cd05166 250 TSDMAYVING--GDKpssrFQLFVDLCCQAFNIIRKNSNLLLNLLSLMLS-SGIPGV-TQDDLRYVQDALLPELTDAEAT 325
                       250
                ....*....|....*...
gi 14389295 787 LLVEQMVDGSMRSITTKL 804
Cdd:cd05166 326 AHFTRMIEESLSSKFTQL 343
PI4KB_NTD cd22246
N-terminal domain of phosphatidylinositol 4-kinase beta; Phosphatidylinositol 4-kinase beta ...
2-66 1.17e-31

N-terminal domain of phosphatidylinositol 4-kinase beta; Phosphatidylinositol 4-kinase beta (PI4K-beta, PI4Kbeta or PI4KB), also called PtdIns 4-kinase beta, NPIK, PI4K92, or PI4KIII, catalyzes the phosphorylation of phosphatidylinositol (PI) to form phosphatidylinositol 4-phosphate (PI4P), in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). It may regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. PI4K-beta is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools. It is recruited to membranes via its interaction with Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3). The ACBD3:PI4K-beta complex formation is essential for proper function of the Golgi. PI4K-beta also plays an essential role in Aichi virus RNA replication. It is recruited by ACBD3 at viral replication sites. This model corresponds to the N-terminal domain of PI4K-beta, which is responsible for interacting with ACBD3 by forming a complex with the Q domain.


Pssm-ID: 412074  Cd Length: 65  Bit Score: 117.60  E-value: 1.17e-31
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14389295   2 GDMVVEPATLKPTSEPTPSPSGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGV 66
Cdd:cd22246   1 GDTDVEPAPVLLTSEPTSGPPGNGGGGPLSVITEGVGELSVIDPEVAKKACQEVLEKVKLLHGVS 65
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
559-784 1.28e-31

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: 127.29  E-value: 1.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 559 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKkQSQL--------SL 630
Cdd:cd00894 100 IGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQ-QSTVgntgafkdEV 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 631 LDYFLQEHGSYTtEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAF 708
Cdd:cd00894 179 LNHWLKEKCPIE-EKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGInkERVPF 257
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14389295 709 KLTTEFVDVMGGLNGDM---FNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFHGSSTIRNLKERFHMSMTEEQ 784
Cdd:cd00894 258 VLTPDFLFVMGTSGKKTslhFQKFQDVCVKAYLALRHHTNLLIILFSMMLM-TGMPQLTSKEDIEYIRDALTVGKSEED 335
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
559-754 2.83e-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: 120.00  E-value: 2.83e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 559 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL-------SLL 631
Cdd:cd05177  92 ISIIFKTGDDLRQDMLVLQIVRVMDNIWLQEGLDMQMIIYRCLSTGKTQGLVQMVPDAVTLAKIHRESGLigplkenTIE 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 632 DYFLQEHgsYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFK 709
Cdd:cd05177 172 KWFHMHN--KLKEDYDKAVRNFFHSCAGWCVVTFILGVCDRHNDNIMLTHSGHMFHIDFGKFLGHAQTFGSIkrDRAPFI 249
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 14389295 710 LTTE--FVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIM 754
Cdd:cd05177 250 FTSEmeYFITEGGKKPQRFQRFVELCCRAYNIVRKHSQLLLNLLEMM 296
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
558-804 2.83e-28

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


Pssm-ID: 270717 [Multi-domain]  Cd Length: 362  Bit Score: 117.37  E-value: 2.83e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 558 LLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQS----------Q 627
Cdd:cd05173  94 SLGIIFKNGDDLRQDMLTLQILRLMDTLWKEAGLDLRIVPYGCLATGDRSGLIEVVSSAETIADIQLNSsnvaaaaafnK 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 628 LSLLDYfLQEHGSytTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ET 705
Cdd:cd05173 174 DALLNW-LKEYNS--GDDLERAIEEFTLSCAGYCVATYVLGIGDRHSDNIMVRKNGQLFHIDFGHILGNFKSKFGIkrER 250
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 706 SAFKLTTEFVDVM---GGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSqLPCFHGSSTIRNLKERFHMSMTE 782
Cdd:cd05173 251 VPFILTYDFIHVIqqgKTGNTEKFGRFRQYCEDAYLILRKNGNLFITLFALMLTAG-LPELTSVKDIQYLKDSLALGKSE 329
                       250       260
                ....*....|....*....|...
gi 14389295 783 EQLQLLVEQMVDGSMR-SITTKL 804
Cdd:cd05173 330 EEALKQFRQKFDEALReSWTTKV 352
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
561-804 3.39e-28

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


Pssm-ID: 270719 [Multi-domain]  Cd Length: 370  Bit Score: 117.08  E-value: 3.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 561 VIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLS--------LLD 632
Cdd:cd05175 105 IIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKgalqfnshTLH 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 633 YFLQEHGSytTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKL 710
Cdd:cd05175 185 QWLKDKNK--GEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYkrERVPFVL 262
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 711 TTEFVDVMGG-----LNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSSTIRNLKERFHMSMTE-EQ 784
Cdd:cd05175 263 TQDFLIVISKgaqecTKTREFERFQEMCYKAYLAIRQHANLFINLFSMM-LGSGMPELQSFDDIAYIRKTLALDKTEqEA 341
                       250       260
                ....*....|....*....|
gi 14389295 785 LQLLVEQMVDGSMRSITTKL 804
Cdd:cd05175 342 LEYFMKQMNDAHHGGWTTKM 361
PI3Kc_C2_alpha cd05176
Catalytic domain of Class II Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
559-804 6.21e-28

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


Pssm-ID: 270720 [Multi-domain]  Cd Length: 353  Bit Score: 116.23  E-value: 6.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 559 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQL--SLLDYFLQ 636
Cdd:cd05176  91 INVMFKVGEDLRQDMLALQMIKIMDKIWLQEGLDLRMVIFKCLSTGKDRGMVELVPSSDTLRKIQVEYGVtgSFKDKPLA 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 637 E---HGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETSAFKLT 711
Cdd:cd05176 171 EwlrKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFkrDRAPFVLT 250
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 712 TEFVDVMGGlnGDM----FNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFHGSSTIRNLKERFHMSMTEEQLQL 787
Cdd:cd05176 251 SDMAYVING--GEKptirFQLFVDLCCQAYNLIRKHTNLFLNLLSLMLS-SGLPELTGIQDLKYVFDALQPQTTDAEATI 327
                       250
                ....*....|....*..
gi 14389295 788 LVEQMVDGSMRSITTKL 804
Cdd:cd05176 328 FFTRLIESSLGSVATKF 344
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
559-784 2.64e-27

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


Pssm-ID: 270718 [Multi-domain]  Cd Length: 366  Bit Score: 114.38  E-value: 2.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 559 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQ----------SQL 628
Cdd:cd05174  98 VGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLSTGDKTGLIEVVLHSDTIANIQLNksnmaataafNKD 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 629 SLLDYFLQEHGSyttEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGF--ETS 706
Cdd:cd05174 178 ALLNWLKSKNPG---DALDQAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGInrERV 254
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 707 AFKLTTEFVDVM---GGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMqQGSQLPCFHGSSTIRNLKERFHMSMTEE 783
Cdd:cd05174 255 PFILTYDFVHVIqqgKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALM-KAAGLPELSCSKDIQYLKDSLALGKTEE 333

                .
gi 14389295 784 Q 784
Cdd:cd05174 334 E 334
PI3Kc_C2_beta cd00895
Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
559-804 2.23e-25

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


Pssm-ID: 119421 [Multi-domain]  Cd Length: 354  Bit Score: 108.55  E-value: 2.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 559 LSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLS-------LL 631
Cdd:cd00895  92 IRVIFKCGDDLRQDMLTLQMIRIMNKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRKIQVEHGVTgsfkdrpLA 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 632 DYfLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPR--NLGFETSAFK 709
Cdd:cd00895 172 DW-LQKHNP-TEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLKTTGHMFHIDFGRFLGHAQMfgNIKRDRAPFV 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 710 LTTEFVDVMGGlnGDM----FNYYKMLMLQGLIAARKHMDKVVQIVEIMQQgSQLPCFHGSSTIRNLKERFHMSMTEEQL 785
Cdd:cd00895 250 FTSDMAYVING--GDKpssrFHDFVDLCCQAYNLIRKHTHLFLNLLGLMLS-CGIPELSDLEDLKYVYDALRPQDTEADA 326
                       250
                ....*....|....*....
gi 14389295 786 QLLVEQMVDGSMRSITTKL 804
Cdd:cd00895 327 TTYFTRLIESSLGSVATKL 345
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
562-754 1.32e-21

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


Pssm-ID: 270708 [Multi-domain]  Cd Length: 222  Bit Score: 94.26  E-value: 1.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 562 IVKCGDDLRQE---LLAFQVL-KQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVkkqsqlsLLDYFLqe 637
Cdd:cd05164  33 LVKGDDDLRKDervMQLFQLLnTLLEKDKETRKRNLTIRTYSVVPLSSQSGLIEWVDNTTTLKPV-------LKKWFN-- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 638 HGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVD 716
Cdd:cd05164 104 ETFPDPTQWYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKtGEVVHIDFGMIFNKGKTLPVPEIVPFRLTRNIIN 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14389295 717 VMG--GLNGdmfNYYKMlMLQGLIAARKHMDKVVQIVEIM 754
Cdd:cd05164 184 GMGptGVEG---LFRKS-CEQVLRVFRKHKDKLITFLDTF 219
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
562-743 5.15e-21

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


Pssm-ID: 270716 [Multi-domain]  Cd Length: 235  Bit Score: 92.64  E-value: 5.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 562 IVKCGDDLR-----QELLAF--QVLKQLQSIWEQErvpLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSqlsLLDYF 634
Cdd:cd05172  33 LVKGGEDLRqdqriQQLFDVmnNILASDPACRQRR---LRIRTYQVIPMTSRLGLIEWVDNTTPLKEILEND---LLRRA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 635 LQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLD-AEGHIIHIDFGFILSSSPRNLGF-ETSAFKLTT 712
Cdd:cd05172 107 LLSLAS-SPEAFLALRSNFARSLAAMSICGYILGIGDRHLSNFLVDlSTGRLIGIDFGHAFGSATQFLPIpELVPFRLTR 185
                       170       180       190
                ....*....|....*....|....*....|.
gi 14389295 713 EFVDVMGGLNGDmfNYYKMLMLQGLIAARKH 743
Cdd:cd05172 186 QLLNLLQPLDAR--GLLRSDMVHVLRALRAG 214
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
562-723 1.40e-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: 81.05  E-value: 1.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 562 IVKCGDDLRQELLAFQVLKQLQSIWEQERVP----LWIKPYKILVISADSGMIEPVVNAVSIHQV--------------- 622
Cdd:cd05171  33 LVKGGDDLRQDAVMEQVFELVNQLLKRDKETrkrkLRIRTYKVVPLSPRSGVLEFVENTIPLGEYlvgassksgaharyr 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 623 ----------KKQSQLSLLD--------------------YFLQEHGSyTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDR 672
Cdd:cd05171 113 pkdwtastcrKKMREKAKASaeerlkvfdeicknfkpvfrHFFLEKFP-DPSDWFERRLAYTRSVATSSIVGYILGLGDR 191
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14389295 673 HNGNILLDAE-GHIIHIDFGFI-----LSSSPrnlgfETSAFKLTTEFVDVMG--GLNG 723
Cdd:cd05171 192 HLNNILIDQKtGELVHIDLGIAfeqgkLLPIP-----ETVPFRLTRDIVDGMGitGVEG 245
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
557-719 3.55e-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: 64.06  E-value: 3.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 557 RLLSVIVKCGDDLRQEL----LAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSI-HQVKKQSQLSLL 631
Cdd:cd00892  28 KKYPFLCKPKDDLRKDArmmeFNTLINRLLSKDPESRRRNLHIRTYAVIPLNEECGIIEWVPNTVTLrSILSTLYPPVLH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 632 DYFLQEHGSYTteAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDF------GFILsSSPrnlgfE 704
Cdd:cd00892 108 EWFLKNFPDPT--AWYEARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTtGDVVHVDFdclfdkGLTL-EVP-----E 179
                       170
                ....*....|....*
gi 14389295 705 TSAFKLTTEFVDVMG 719
Cdd:cd00892 180 RVPFRLTQNMVDAMG 194
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
568-753 2.53e-07

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


Pssm-ID: 270713 [Multi-domain]  Cd Length: 279  Bit Score: 52.87  E-value: 2.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 568 DLRQELLAFQVLKQLQSIWEQERVP----LWIKPYKILVISADSGMIEPVVNAVSIHQVKKQ------------------ 625
Cdd:cd05169  39 DLRLDERVMQLFGLVNTLLKNDSETsrrnLSIQRYSVIPLSPNSGLIGWVPGCDTLHSLIRDyrekrkiplniehrlmlq 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 626 -----SQLSLLD-YFLQEHG----------------SYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE- 682
Cdd:cd05169 119 mapdyDNLTLIQkVEVFEYAlentpgddlrrvlwlkSPSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLt 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 683 GHIIHIDFGFIlsssprnlgFETSA----------FKLTTEFVDVMG--GLNGdmfNYYK-----MLMLqgliaaRKHMD 745
Cdd:cd05169 199 GKVIHIDFGDC---------FEVAMhrekfpekvpFRLTRMLVNAMEvsGVEG---TFRStcedvMRVL------RENKD 260

                ....*...
gi 14389295 746 KVVQIVEI 753
Cdd:cd05169 261 SLMAVLEA 268
PTZ00303 PTZ00303
phosphatidylinositol kinase; Provisional
598-695 2.60e-07

phosphatidylinositol kinase; Provisional


Pssm-ID: 140324 [Multi-domain]  Cd Length: 1374  Bit Score: 54.71  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295   598 YKILVISADSGMIEPVvnavsihqvkKQSQLSLLDYFlqEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNI 677
Cdd:PTZ00303 1090 YSVLPLSCDSGLIEKA----------EGRELSNLDNM--DIASYVLYRGTRSCINFLASAKLFLLLNYIFSIGDRHKGNV 1157
                          90
                  ....*....|....*...
gi 14389295   678 LLDAEGHIIHIDFGFILS 695
Cdd:PTZ00303 1158 LIGTNGALLHIDFRFIFS 1175
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
639-723 3.74e-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: 3.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14389295 639 GSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAE-GHIIHIDFgfilsssprNLGF---------ETSAF 708
Cdd:cd05170 180 SSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLStGEVVHIDY---------NVCFekgkrlrvpEKVPF 250
                        90
                ....*....|....*..
gi 14389295 709 KLTTEFVDVMG--GLNG 723
Cdd:cd05170 251 RLTQNIEHALGptGVEG 267
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
641-691 5.22e-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: 38.19  E-value: 5.22e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14389295 641 YTTEAFLSAQRN--FVQSCAGYCLVCYLLQV--KDRHNGNILLDAEGHIIHIDFG 691
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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