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Conserved domains on  [gi|530407765|ref|XP_005255240|]
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serine/threonine-protein kinase SMG1 isoform X3 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase SMG1( domain architecture ID 13879162)

serine/threonine-protein kinase SMG1 (Suppressor of Morphogenetic effect on Genitalia-1) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and belongs to the phosphoinositide 3-kinase-related protein kinase (PIKK) family; PIKKs have intrinsic serine/threonine kinase activity and are distinguished from other PKs by their unique catalytic domain, similar to that of lipid PI3K

CATH:  1.10.510.10
EC:  2.7.11.1
Gene Symbol:  SMG1
Gene Ontology:  GO:0005524|GO:0006468|GO:0004674
SCOP:  3000066

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMG1 pfam15785
Serine/threonine-protein kinase smg-1; SMG1 is a family of eukaryotic proteins. In humans this ...
605-1216 0e+00

Serine/threonine-protein kinase smg-1; SMG1 is a family of eukaryotic proteins. In humans this family acts as an mRNA-surveillance protein. In C.elegans, SMG1, a phosphatidylinositol kinase-related protein kinase, is a key regulator of growth. Loss of SMG1 leads to hyperactive responses to injury and subsequent growth that continues out of control. It has an antagonistic role to mTOR signalling in these worms and possibly also in higher eukaryotes.


:

Pssm-ID: 434936  Cd Length: 622  Bit Score: 851.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   605 MWALSPTVFALLSKNLMIVHSDLAVHFPAIQYAVLYTLYSHCTRHDHFISSSLSSSSPSLFDGAVISTVTTATKKHFSII 684
Cdd:pfam15785    1 MWALKPSIFELLSTNLRAVDLDLWVRYPAVQYAILNLLYSHCSRHHNFVSSSSLITSTSLFDGSLISEVTSPTANNFSII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   685 LNLLGILLKKDNLNQDTRKLLMTWALEAAvLMKKSETYAP-LFSLPSFHKFCKGLLANTLVEDVNICLQACSS----LHA 759
Cdd:pfam15785   81 LNLLAKLLEKDNLNPDTLLLLLKWILELA-LLRESETYAPlLFSQPEFLNICRSLLANALKEDVNISLEACACiqsvLKY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   760 LSSSLPDDLLQRCVDVCRVQLVHSGTRIRQAFGKLLKSIPLDVVLS-----------------NNNHTEIQEISLALRSH 822
Cdd:pfam15785  160 GPTSSKDELLQLYVDLALQQLVHLAPNVRQTFGQLLASIPLHVVLSggsilslgmdskrvcvwQQRHSEISAVSLAIRSH 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   823 MSKAPSNTFHPQDFSDVISFILYGNSHRTGKDNWLERLFYSCQRLDKRD--QSTIPRNLLKTDAVLWQWAIWEAAQFTVL 900
Cdd:pfam15785  240 MRRAPNGTFHDQVFRDFMEFILYPETHQQGLTNWLEDLFYSCCQLIKQDerQAKLSRCALRCQALLWFWAQWEAAQYCVL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   901 SKLRTPLGRAQDTFQTIEGIIRSLAAHTLNPDQDVSQWT-TADNDEGHGNNQLRLVLLLQYLENLEKLMYNAYEGCANAL 979
Cdd:pfam15785  320 NKLRTPLGKPQDTFTTIEGIIKRLARELSGPAKEVSRWAlTGLSLEGLLNNQLRLRLLLQFLEHLEKLIYNAAEGCAFAL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   980 TSPPKVIRTFFYTNRQTCQDWLTRIRLSIMRVGLLAGQPAVTVRHGFDLLTEMKTTSLSQGNELEVTIMMVVEALCELHC 1059
Cdd:pfam15785  400 RPPPKPVRTFFRTNRPTCQEWLNRIRLAVVIVALHSGQPALAIRHGQQLLTEMKTNSNTQGAEFEQAIVYLAWALVELQE 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  1060 PEAIQGIAVWSSSIVGKNLLWINSVAQQAEGRFEKASVEYQEHLCAMTGVdCCISSFDKSVLtlanagrnsASPKHSLNg 1139
Cdd:pfam15785  480 SDAIRGLYVWSKEKVGKKFLWLKAAADQAAGKFEKAAEEYQNILCEMTGQ-CELEPHTRKLT---------EIPKKSLG- 548
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407765  1140 esrktVLSKPTDSSPEVINYLGNKACECYISIADWAAVQEWQNAIHDLKKSTSSTSLNLKADF--NYIKSLSSFESGKF 1216
Cdd:pfam15785  549 -----ILLKPSDCSPEVLNFVVAQLCECYQSLGDWSQLVEWKQNELNLPEDSEDNPFNQRSDVesNYIRLLSKFEEGDF 622
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2095-2428 0e+00

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: 614.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2174
Cdd:cd05170     1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGATPLFGLYKRWQQREAALQAQKAQDSYQTPQnpgIVPRPSELYYSKIGPALKTVGLSLDVSRRDWPLHVM 2254
Cdd:cd05170    81 RSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDSGSTPP---PVPRPSELFYNKLKPALKAAGIRKSTSRREWPLEVL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2255 KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2334
Cdd:cd05170   158 RQVLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2335 KGnikvdftfmrakcflvkgqkyndlsfqgKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLT 2414
Cdd:cd05170   238 KG----------------------------KRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLT 289
                         330
                  ....*....|....
gi 530407765 2415 LLEAFVYDPLVDWT 2428
Cdd:cd05170   290 LLEAFVYDPLVDWT 303
DUF5303 pfam17229
Region of unknown function (DUF5303); This disordered region of unknown function shows ...
6-114 2.33e-50

Region of unknown function (DUF5303); This disordered region of unknown function shows similarity to the N-terminal region of SMG1.


:

Pssm-ID: 435799  Cd Length: 106  Bit Score: 174.25  E-value: 2.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765     6 TDSASADPDNLKYSSSRDRGGSSSYGLQPSNSAVvSRQRHDDTRVHADIqNDEKGGYSVNGGSGENTYGRKSLGQELRVN 85
Cdd:pfam17229    1 GDSVSASQDNLKYSASRERGSSASYDLQPSNSPV-SPPRHDDARAAADA-NEEEGGYEVNGGVGENTFGWKSLGQELRVN 78
                           90       100
                   ....*....|....*....|....*....
gi 530407765    86 NVTSpEFTSVQHGSRALATKDMRKSQERS 114
Cdd:pfam17229   79 DVTS-DLTSFQHGNRALATKDMRKSQDRG 106
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
3633-3662 4.30e-10

FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution structure of the FATC domain suggests it plays a role in redox-dependent structural and cellular stability.


:

Pssm-ID: 426683 [Multi-domain]  Cd Length: 32  Bit Score: 57.01  E-value: 4.30e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 530407765  3633 MSVAEQVDYVIKEATNLDNLAQLYEGWTAW 3662
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPW 31
 
Name Accession Description Interval E-value
SMG1 pfam15785
Serine/threonine-protein kinase smg-1; SMG1 is a family of eukaryotic proteins. In humans this ...
605-1216 0e+00

Serine/threonine-protein kinase smg-1; SMG1 is a family of eukaryotic proteins. In humans this family acts as an mRNA-surveillance protein. In C.elegans, SMG1, a phosphatidylinositol kinase-related protein kinase, is a key regulator of growth. Loss of SMG1 leads to hyperactive responses to injury and subsequent growth that continues out of control. It has an antagonistic role to mTOR signalling in these worms and possibly also in higher eukaryotes.


Pssm-ID: 434936  Cd Length: 622  Bit Score: 851.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   605 MWALSPTVFALLSKNLMIVHSDLAVHFPAIQYAVLYTLYSHCTRHDHFISSSLSSSSPSLFDGAVISTVTTATKKHFSII 684
Cdd:pfam15785    1 MWALKPSIFELLSTNLRAVDLDLWVRYPAVQYAILNLLYSHCSRHHNFVSSSSLITSTSLFDGSLISEVTSPTANNFSII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   685 LNLLGILLKKDNLNQDTRKLLMTWALEAAvLMKKSETYAP-LFSLPSFHKFCKGLLANTLVEDVNICLQACSS----LHA 759
Cdd:pfam15785   81 LNLLAKLLEKDNLNPDTLLLLLKWILELA-LLRESETYAPlLFSQPEFLNICRSLLANALKEDVNISLEACACiqsvLKY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   760 LSSSLPDDLLQRCVDVCRVQLVHSGTRIRQAFGKLLKSIPLDVVLS-----------------NNNHTEIQEISLALRSH 822
Cdd:pfam15785  160 GPTSSKDELLQLYVDLALQQLVHLAPNVRQTFGQLLASIPLHVVLSggsilslgmdskrvcvwQQRHSEISAVSLAIRSH 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   823 MSKAPSNTFHPQDFSDVISFILYGNSHRTGKDNWLERLFYSCQRLDKRD--QSTIPRNLLKTDAVLWQWAIWEAAQFTVL 900
Cdd:pfam15785  240 MRRAPNGTFHDQVFRDFMEFILYPETHQQGLTNWLEDLFYSCCQLIKQDerQAKLSRCALRCQALLWFWAQWEAAQYCVL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   901 SKLRTPLGRAQDTFQTIEGIIRSLAAHTLNPDQDVSQWT-TADNDEGHGNNQLRLVLLLQYLENLEKLMYNAYEGCANAL 979
Cdd:pfam15785  320 NKLRTPLGKPQDTFTTIEGIIKRLARELSGPAKEVSRWAlTGLSLEGLLNNQLRLRLLLQFLEHLEKLIYNAAEGCAFAL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   980 TSPPKVIRTFFYTNRQTCQDWLTRIRLSIMRVGLLAGQPAVTVRHGFDLLTEMKTTSLSQGNELEVTIMMVVEALCELHC 1059
Cdd:pfam15785  400 RPPPKPVRTFFRTNRPTCQEWLNRIRLAVVIVALHSGQPALAIRHGQQLLTEMKTNSNTQGAEFEQAIVYLAWALVELQE 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  1060 PEAIQGIAVWSSSIVGKNLLWINSVAQQAEGRFEKASVEYQEHLCAMTGVdCCISSFDKSVLtlanagrnsASPKHSLNg 1139
Cdd:pfam15785  480 SDAIRGLYVWSKEKVGKKFLWLKAAADQAAGKFEKAAEEYQNILCEMTGQ-CELEPHTRKLT---------EIPKKSLG- 548
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407765  1140 esrktVLSKPTDSSPEVINYLGNKACECYISIADWAAVQEWQNAIHDLKKSTSSTSLNLKADF--NYIKSLSSFESGKF 1216
Cdd:pfam15785  549 -----ILLKPSDCSPEVLNFVVAQLCECYQSLGDWSQLVEWKQNELNLPEDSEDNPFNQRSDVesNYIRLLSKFEEGDF 622
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2095-2428 0e+00

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: 614.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2174
Cdd:cd05170     1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGATPLFGLYKRWQQREAALQAQKAQDSYQTPQnpgIVPRPSELYYSKIGPALKTVGLSLDVSRRDWPLHVM 2254
Cdd:cd05170    81 RSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDSGSTPP---PVPRPSELFYNKLKPALKAAGIRKSTSRREWPLEVL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2255 KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2334
Cdd:cd05170   158 RQVLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2335 KGnikvdftfmrakcflvkgqkyndlsfqgKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLT 2414
Cdd:cd05170   238 KG----------------------------KRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLT 289
                         330
                  ....*....|....
gi 530407765 2415 LLEAFVYDPLVDWT 2428
Cdd:cd05170   290 LLEAFVYDPLVDWT 303
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
2123-2428 4.71e-59

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 204.87  E-value: 4.71e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  2123 SYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRqetPRFHARHYSVTPLGTRSGLIQWVDGATPLfglykrwqqreAAL 2202
Cdd:pfam00454    1 GYGGIYKVGDDLRQDELILQVFKLMDEELSKDNL---DLRRLKPYSVIPLGPKCGIIEWVPNSETL-----------AYI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  2203 QaqkaqdsyqtpqnpgivprpSELYYSKIGPALKtvglsldVSRRDWPLHVMKAVLEELMEA--TPPNLLAKELWSSCTT 2280
Cdd:pfam00454   67 L--------------------DEYGENGVPPTAM-------VKILHSALNYPKLKLEFESRIslPPKVGLLQWFVKKSPD 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  2281 PDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFEKgnikvdftfmrakcflvkgqkyndl 2360
Cdd:pfam00454  120 AEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTTGKLFHIDFGLCLPD------------------------- 174
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407765  2361 sfQGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2428
Cdd:pfam00454  175 --AGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADGLPDWS 240
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2014-2427 1.25e-52

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 206.56  E-value: 1.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2014 FQDNYGDAIENALEKLKTPLNPakpgsSWIPFKEIMLSLQQRAQKRASYILRLEEISPwLAAMTNTEIALPGEV-SARDT 2092
Cdd:COG5032  1691 LIKKSPRKIRKKFKIDISLLNL-----SRKLYISVLRSIRKRLKRLLELRLKKVSPKL-LLFHAFLEIKLPGQYlLDKPF 1764
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2093 VTIHSVGGTITILPTKT-KPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTP 2171
Cdd:COG5032  1765 VLIERFEPEVSVVKSHLqRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVIP 1844
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2172 LGTRSGLIQWVDGATPLFGLYK--RWQQREAALQAQKAQDSYQtpqnpgivprpselyyskigpaLKTVGLSLDVsrrdw 2249
Cdd:COG5032  1845 LSPGSGIIEWVPNSDTLHSILReyHKRKNISIDQEKKLAARLD----------------------NLKLLLKDEF----- 1897
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2250 plhvmkavlEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDy 2329
Cdd:COG5032  1898 ---------FTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHID- 1967
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2330 nvcfekgnikvdFTFMrakcflvkgqkyndLSFQGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGR 2409
Cdd:COG5032  1968 ------------FGFI--------------LFNAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNA 2021
                         410
                  ....*....|....*...
gi 530407765 2410 ETLLTLLEAFVYDPLVDW 2427
Cdd:COG5032  2022 DSLMNVLELFVRDPLIEW 2039
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2127-2428 5.18e-51

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: 181.73  E-value: 5.18e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   2127 LFKGLEDLHLDERIMQFLSIVNTMFAtiNRQETPR--FHARHYSVTPLGTRSGLIQWVDGATPLFGL---YKRWQQREAA 2201
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQ--KDKETRRrdLHLRPYKVIPTGPKSGLIEVVPNSTTLHEIlkeYRKQKGKVLD 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   2202 LQAQKAqdsyqtpqnpgivprpselyyskigpalktvglsldvSRRDWPLHVMKAVLEelmeaTPPNLLAKELWSSCTTP 2281
Cdd:smart00146   80 LRSQTA-------------------------------------TRLKKLELFLEATGK-----FPDPVLYDWFTKKFPDP 117
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   2282 DE-WWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFEKGNIKVDFtfmrakcflvkgqkyndl 2360
Cdd:smart00146  118 SEdYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLD-KTGHLFHIDFGFILGNGPKLFGF------------------ 178
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407765   2361 sfqgkslrvPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2428
Cdd:smart00146  179 ---------PERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPDWR 237
DUF5303 pfam17229
Region of unknown function (DUF5303); This disordered region of unknown function shows ...
6-114 2.33e-50

Region of unknown function (DUF5303); This disordered region of unknown function shows similarity to the N-terminal region of SMG1.


Pssm-ID: 435799  Cd Length: 106  Bit Score: 174.25  E-value: 2.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765     6 TDSASADPDNLKYSSSRDRGGSSSYGLQPSNSAVvSRQRHDDTRVHADIqNDEKGGYSVNGGSGENTYGRKSLGQELRVN 85
Cdd:pfam17229    1 GDSVSASQDNLKYSASRERGSSASYDLQPSNSPV-SPPRHDDARAAADA-NEEEGGYEVNGGVGENTFGWKSLGQELRVN 78
                           90       100
                   ....*....|....*....|....*....
gi 530407765    86 NVTSpEFTSVQHGSRALATKDMRKSQERS 114
Cdd:pfam17229   79 DVTS-DLTSFQHGNRALATKDMRKSQDRG 106
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
3633-3662 4.30e-10

FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution structure of the FATC domain suggests it plays a role in redox-dependent structural and cellular stability.


Pssm-ID: 426683 [Multi-domain]  Cd Length: 32  Bit Score: 57.01  E-value: 4.30e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 530407765  3633 MSVAEQVDYVIKEATNLDNLAQLYEGWTAW 3662
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPW 31
 
Name Accession Description Interval E-value
SMG1 pfam15785
Serine/threonine-protein kinase smg-1; SMG1 is a family of eukaryotic proteins. In humans this ...
605-1216 0e+00

Serine/threonine-protein kinase smg-1; SMG1 is a family of eukaryotic proteins. In humans this family acts as an mRNA-surveillance protein. In C.elegans, SMG1, a phosphatidylinositol kinase-related protein kinase, is a key regulator of growth. Loss of SMG1 leads to hyperactive responses to injury and subsequent growth that continues out of control. It has an antagonistic role to mTOR signalling in these worms and possibly also in higher eukaryotes.


Pssm-ID: 434936  Cd Length: 622  Bit Score: 851.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   605 MWALSPTVFALLSKNLMIVHSDLAVHFPAIQYAVLYTLYSHCTRHDHFISSSLSSSSPSLFDGAVISTVTTATKKHFSII 684
Cdd:pfam15785    1 MWALKPSIFELLSTNLRAVDLDLWVRYPAVQYAILNLLYSHCSRHHNFVSSSSLITSTSLFDGSLISEVTSPTANNFSII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   685 LNLLGILLKKDNLNQDTRKLLMTWALEAAvLMKKSETYAP-LFSLPSFHKFCKGLLANTLVEDVNICLQACSS----LHA 759
Cdd:pfam15785   81 LNLLAKLLEKDNLNPDTLLLLLKWILELA-LLRESETYAPlLFSQPEFLNICRSLLANALKEDVNISLEACACiqsvLKY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   760 LSSSLPDDLLQRCVDVCRVQLVHSGTRIRQAFGKLLKSIPLDVVLS-----------------NNNHTEIQEISLALRSH 822
Cdd:pfam15785  160 GPTSSKDELLQLYVDLALQQLVHLAPNVRQTFGQLLASIPLHVVLSggsilslgmdskrvcvwQQRHSEISAVSLAIRSH 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   823 MSKAPSNTFHPQDFSDVISFILYGNSHRTGKDNWLERLFYSCQRLDKRD--QSTIPRNLLKTDAVLWQWAIWEAAQFTVL 900
Cdd:pfam15785  240 MRRAPNGTFHDQVFRDFMEFILYPETHQQGLTNWLEDLFYSCCQLIKQDerQAKLSRCALRCQALLWFWAQWEAAQYCVL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   901 SKLRTPLGRAQDTFQTIEGIIRSLAAHTLNPDQDVSQWT-TADNDEGHGNNQLRLVLLLQYLENLEKLMYNAYEGCANAL 979
Cdd:pfam15785  320 NKLRTPLGKPQDTFTTIEGIIKRLARELSGPAKEVSRWAlTGLSLEGLLNNQLRLRLLLQFLEHLEKLIYNAAEGCAFAL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   980 TSPPKVIRTFFYTNRQTCQDWLTRIRLSIMRVGLLAGQPAVTVRHGFDLLTEMKTTSLSQGNELEVTIMMVVEALCELHC 1059
Cdd:pfam15785  400 RPPPKPVRTFFRTNRPTCQEWLNRIRLAVVIVALHSGQPALAIRHGQQLLTEMKTNSNTQGAEFEQAIVYLAWALVELQE 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  1060 PEAIQGIAVWSSSIVGKNLLWINSVAQQAEGRFEKASVEYQEHLCAMTGVdCCISSFDKSVLtlanagrnsASPKHSLNg 1139
Cdd:pfam15785  480 SDAIRGLYVWSKEKVGKKFLWLKAAADQAAGKFEKAAEEYQNILCEMTGQ-CELEPHTRKLT---------EIPKKSLG- 548
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407765  1140 esrktVLSKPTDSSPEVINYLGNKACECYISIADWAAVQEWQNAIHDLKKSTSSTSLNLKADF--NYIKSLSSFESGKF 1216
Cdd:pfam15785  549 -----ILLKPSDCSPEVLNFVVAQLCECYQSLGDWSQLVEWKQNELNLPEDSEDNPFNQRSDVesNYIRLLSKFEEGDF 622
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2095-2428 0e+00

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: 614.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2174
Cdd:cd05170     1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGATPLFGLYKRWQQREAALQAQKAQDSYQTPQnpgIVPRPSELYYSKIGPALKTVGLSLDVSRRDWPLHVM 2254
Cdd:cd05170    81 RSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDSGSTPP---PVPRPSELFYNKLKPALKAAGIRKSTSRREWPLEVL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2255 KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2334
Cdd:cd05170   158 RQVLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2335 KGnikvdftfmrakcflvkgqkyndlsfqgKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLT 2414
Cdd:cd05170   238 KG----------------------------KRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLT 289
                         330
                  ....*....|....
gi 530407765 2415 LLEAFVYDPLVDWT 2428
Cdd:cd05170   290 LLEAFVYDPLVDWT 303
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
2095-2422 2.01e-96

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: 311.13  E-value: 2.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2174
Cdd:cd05164     1 IASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGDDDLRKDERVMQLFQLLNTLLEKDKETRKRNLTIRTYSVVPLSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGATPLFGLYKRWqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwplhvm 2254
Cdd:cd05164    81 QSGLIEWVDNTTTLKPVLKKW----------------------------------------------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2255 kavleelmeatppnllakeLWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2334
Cdd:cd05164   102 -------------------FNETFPDPTQWYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKTGEVVHIDFGMIFN 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2335 KGnikvdftfmrakcflvkgqkyndlsfqgKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLT 2414
Cdd:cd05164   163 KG----------------------------KTLPVPEIVPFRLTRNIINGMGPTGVEGLFRKSCEQVLRVFRKHKDKLIT 214

                  ....*...
gi 530407765 2415 LLEAFVYD 2422
Cdd:cd05164   215 FLDTFLYD 222
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
2095-2427 1.72e-88

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: 290.92  E-value: 1.72e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2174
Cdd:cd05169     1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDERVMQLFGLVNTLLKNDSETSRRNLSIQRYSVIPLSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGATPLFGLYKRW-QQREAALQAQKAQDSYQTPQnpgivprpselYYSkigpalktvglsldvsrrdwpLHV 2253
Cdd:cd05169    81 NSGLIGWVPGCDTLHSLIRDYrEKRKIPLNIEHRLMLQMAPD-----------YDN---------------------LTL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2254 M--KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNV 2331
Cdd:cd05169   129 IqkVEVFEYALENTPGDDLRRVLWLKSPSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDFGD 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2332 CFEKgnikvdfTFMRAKCflvkgqkyndlsfqgkslrvPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRET 2411
Cdd:cd05169   209 CFEV-------AMHREKF--------------------PEKVPFRLTRMLVNAMEVSGVEGTFRSTCEDVMRVLRENKDS 261
                         330
                  ....*....|....*.
gi 530407765 2412 LLTLLEAFVYDPLVDW 2427
Cdd:cd05169   262 LMAVLEAFVHDPLISW 277
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
2095-2428 6.60e-79

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: 261.29  E-value: 6.60e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2174
Cdd:cd00892     1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGatplfglykrwqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwpLHVM 2254
Cdd:cd00892    81 ECGIIEWVPN------------------------------------------------------------------TVTL 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2255 KAVLEELMeatPPnLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2334
Cdd:cd00892    95 RSILSTLY---PP-VLHEWFLKNFPDPTAWYEARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFD 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2335 KGnikvdftfmrakcflvkgqkyndlsfqgKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLT 2414
Cdd:cd00892   171 KG----------------------------LTLEVPERVPFRLTQNMVDAMGVTGVEGTFRRTCEVTLRVLRENRETLMS 222
                         330
                  ....*....|....
gi 530407765 2415 LLEAFVYDPLVDWT 2428
Cdd:cd00892   223 VLETFVHDPLVEWS 236
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
2095-2428 3.60e-74

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: 249.76  E-value: 3.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFAtiNRQET--PRFHARHYSVTPL 2172
Cdd:cd05171     1 ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLK--RDKETrkRKLRIRTYKVVPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2173 GTRSGLIQWVDGATPLfGLYKRwqqreAALQAQKAQDSYqtpqnpgivpRPSELYYSKIGPALKTVGLSLDVSRRdwplh 2252
Cdd:cd05171    79 SPRSGVLEFVENTIPL-GEYLV-----GASSKSGAHARY----------RPKDWTASTCRKKMREKAKASAEERL----- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2253 vmkAVLEELMEATPPnLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVC 2332
Cdd:cd05171   138 ---KVFDEICKNFKP-VFRHFFLEKFPDPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2333 FEkgnikvdftfmrakcflvkgqkyndlsfQGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETL 2412
Cdd:cd05171   214 FE----------------------------QGKLLPIPETVPFRLTRDIVDGMGITGVEGVFRRCCEETLRVLRENKEAL 265
                         330
                  ....*....|....*.
gi 530407765 2413 LTLLEAFVYDPLVDWT 2428
Cdd:cd05171   266 LTILEVLLYDPLYSWT 281
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
2123-2428 4.71e-59

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


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 204.87  E-value: 4.71e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  2123 SYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRqetPRFHARHYSVTPLGTRSGLIQWVDGATPLfglykrwqqreAAL 2202
Cdd:pfam00454    1 GYGGIYKVGDDLRQDELILQVFKLMDEELSKDNL---DLRRLKPYSVIPLGPKCGIIEWVPNSETL-----------AYI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  2203 QaqkaqdsyqtpqnpgivprpSELYYSKIGPALKtvglsldVSRRDWPLHVMKAVLEELMEA--TPPNLLAKELWSSCTT 2280
Cdd:pfam00454   67 L--------------------DEYGENGVPPTAM-------VKILHSALNYPKLKLEFESRIslPPKVGLLQWFVKKSPD 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765  2281 PDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFEKgnikvdftfmrakcflvkgqkyndl 2360
Cdd:pfam00454  120 AEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTTGKLFHIDFGLCLPD------------------------- 174
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407765  2361 sfQGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2428
Cdd:pfam00454  175 --AGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADGLPDWS 240
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2014-2427 1.25e-52

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 206.56  E-value: 1.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2014 FQDNYGDAIENALEKLKTPLNPakpgsSWIPFKEIMLSLQQRAQKRASYILRLEEISPwLAAMTNTEIALPGEV-SARDT 2092
Cdd:COG5032  1691 LIKKSPRKIRKKFKIDISLLNL-----SRKLYISVLRSIRKRLKRLLELRLKKVSPKL-LLFHAFLEIKLPGQYlLDKPF 1764
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2093 VTIHSVGGTITILPTKT-KPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTP 2171
Cdd:COG5032  1765 VLIERFEPEVSVVKSHLqRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVIP 1844
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2172 LGTRSGLIQWVDGATPLFGLYK--RWQQREAALQAQKAQDSYQtpqnpgivprpselyyskigpaLKTVGLSLDVsrrdw 2249
Cdd:COG5032  1845 LSPGSGIIEWVPNSDTLHSILReyHKRKNISIDQEKKLAARLD----------------------NLKLLLKDEF----- 1897
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2250 plhvmkavlEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDy 2329
Cdd:COG5032  1898 ---------FTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHID- 1967
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2330 nvcfekgnikvdFTFMrakcflvkgqkyndLSFQGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGR 2409
Cdd:COG5032  1968 ------------FGFI--------------LFNAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNA 2021
                         410
                  ....*....|....*...
gi 530407765 2410 ETLLTLLEAFVYDPLVDW 2427
Cdd:COG5032  2022 DSLMNVLELFVRDPLIEW 2039
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2127-2428 5.18e-51

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: 181.73  E-value: 5.18e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   2127 LFKGLEDLHLDERIMQFLSIVNTMFAtiNRQETPR--FHARHYSVTPLGTRSGLIQWVDGATPLFGL---YKRWQQREAA 2201
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQ--KDKETRRrdLHLRPYKVIPTGPKSGLIEVVPNSTTLHEIlkeYRKQKGKVLD 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   2202 LQAQKAqdsyqtpqnpgivprpselyyskigpalktvglsldvSRRDWPLHVMKAVLEelmeaTPPNLLAKELWSSCTTP 2281
Cdd:smart00146   80 LRSQTA-------------------------------------TRLKKLELFLEATGK-----FPDPVLYDWFTKKFPDP 117
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765   2282 DE-WWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFEKGNIKVDFtfmrakcflvkgqkyndl 2360
Cdd:smart00146  118 SEdYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLD-KTGHLFHIDFGFILGNGPKLFGF------------------ 178
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530407765   2361 sfqgkslrvPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2428
Cdd:smart00146  179 ---------PERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPDWR 237
DUF5303 pfam17229
Region of unknown function (DUF5303); This disordered region of unknown function shows ...
6-114 2.33e-50

Region of unknown function (DUF5303); This disordered region of unknown function shows similarity to the N-terminal region of SMG1.


Pssm-ID: 435799  Cd Length: 106  Bit Score: 174.25  E-value: 2.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765     6 TDSASADPDNLKYSSSRDRGGSSSYGLQPSNSAVvSRQRHDDTRVHADIqNDEKGGYSVNGGSGENTYGRKSLGQELRVN 85
Cdd:pfam17229    1 GDSVSASQDNLKYSASRERGSSASYDLQPSNSPV-SPPRHDDARAAADA-NEEEGGYEVNGGVGENTFGWKSLGQELRVN 78
                           90       100
                   ....*....|....*....|....*....
gi 530407765    86 NVTSpEFTSVQHGSRALATKDMRKSQERS 114
Cdd:pfam17229   79 DVTS-DLTSFQHGNRALATKDMRKSQDRG 106
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
2095-2427 6.04e-50

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: 178.15  E-value: 6.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2174
Cdd:cd05172     1 IVGFDPRVLVLSSKRRPKRITIRGSDEKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDPACRQRRLRIRTYQVIPMTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGATPLfglykrwqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwplhvm 2254
Cdd:cd05172    81 RLGLIEWVDNTTPL------------------------------------------------------------------ 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2255 KAVLEElmeatppNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2334
Cdd:cd05172    95 KEILEN-------DLLRRALLSLASSPEAFLALRSNFARSLAAMSICGYILGIGDRHLSNFLVDLSTGRLIGIDFGHAFG 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2335 KGNIKvdftfmrakcflvkgqkyndlsfqgksLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLT 2414
Cdd:cd05172   168 SATQF---------------------------LPIPELVPFRLTRQLLNLLQPLDARGLLRSDMVHVLRALRAGRDLLLA 220
                         330
                  ....*....|...
gi 530407765 2415 LLEAFVYDPLVDW 2427
Cdd:cd05172   221 TMDVFVKEPLLDW 233
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
2095-2422 4.49e-34

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: 132.07  E-value: 4.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2095 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFatinRQETPRFHARHYSVTPLGT 2174
Cdd:cd00142     1 NALDVGILKVIHSKQRPKKITLIGADGKTYSFLLKRRDDLRKDERSFQFMRLIQSIL----EKESVNLVLPPYKVIPLSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2175 RSGLIQWVDGATPLFGLykrwqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwplhvm 2254
Cdd:cd00142    77 NSGLIEIVKDAQTIEDL--------------------------------------------------------------- 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2255 kavleelmeatppnllAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFE 2334
Cdd:cd00142    94 ----------------LKSLWRKSPSSQSWLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIMIE-PSGNIFHIDFGFIFS 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2335 KgnikvdftfmrakcflvkgqkyndlsfqGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLT 2414
Cdd:cd00142   157 G----------------------------RKLAEGVETVPFRLTPMLENAMGTAGVNGPFQISMVKIMEILREHADLIVP 208

                  ....*...
gi 530407765 2415 LLEAFVYD 2422
Cdd:cd00142   209 ILEHSLRD 216
PIKK_TRRAP cd05163
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs ...
2112-2394 8.11e-12

Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs to the the phosphoinositide 3-kinase-related protein kinase (PIKK) subfamily. It contains a FATC (FRAP, ATM and TRRAP, C-terminal) domain and has a large molecular weight. Unlike most PIKK proteins, however, it contains an inactive PI3K-like pseudokinase domain, which lacks the conserved residues necessary for ATP binding and catalytic activity. TRRAP also contains many motifs that may be critical for protein-protein interactions. TRRAP is a common component of many histone acetyltransferase (HAT) complexes, and is responsible for the recruitment of these complexes to chromatin during transcription, replication, and DNA repair. TRRAP also exists in non-HAT complexes such as the p400 and MRN complexes, which are implicated in ATP-dependent remodeling and DNA repair, respectively. The TRRAP pseudokinase 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: 270707  Cd Length: 252  Bit Score: 68.32  E-value: 8.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2112 KKLLFLGSDGKSYPYL--FKGLEDLHLDERIMQFLSIVNTMFATinRQETPRFHARHY--SVTPLGTRSGLIQwvdgatp 2187
Cdd:cd05163    19 RRLTIRGHDGSKYPFLvqTPSARHSRREERVMQLFRLLNRVLER--KKETRRRNLQFHvpIVVPLSPQVRLVE------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2188 lfglykrwqqreaalqaqkAQDSYQTPQNPgivprpselyYSKigpalktvglsldvsrrdwpLHVMKAVLEELMeatPP 2267
Cdd:cd05163    90 -------------------DDPSYISLQDI----------YEK--------------------LEILNEIQSKMV---PE 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2268 NLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYnvcfekgnikvdftfmra 2347
Cdd:cd05163   118 TILSNYFLRTMPSPSDLWLFRKQFTLQLALSSFMTYVLSLGNRTPHRILISRSTGNVFMTDF------------------ 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 530407765 2348 kcflvkgqkYNDLSFQGKSLRVPEKVPFRMTQNIETALGVTGVEGVF 2394
Cdd:cd05163   180 ---------LPSINSQGPLLDNNEPVPFRLTPNIQHFIGPIGVEGLL 217
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2102-2329 8.04e-11

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: 66.79  E-value: 8.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2102 ITILPTKTK-------PKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFatinRQE------TPrfharhYS 2168
Cdd:cd00896    64 TGIIPEKSTvfksalmPLKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLL----KKEnldlklTP------YK 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2169 VTPLGTRSGLIQWVDGATPLFGLYKRWQQREAALQAQkaqdsyqtpqnpgivpRPSElyyskigpalktvglsldvsrrD 2248
Cdd:cd00896   134 VLATSPNDGLVEFVPNSKALADILKKYGSILNFLRKH----------------NPDE----------------------S 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2249 WPLHVMKAVLeelmeatppnllakelwsscttpdewwrvtQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHID 2328
Cdd:cd00896   176 GPYGIKPEVM------------------------------DNFVKSCAGYCVITYILGVGDRHLDNLLLT-KDGHLFHID 224

                  .
gi 530407765 2329 Y 2329
Cdd:cd00896   225 F 225
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
3633-3662 4.30e-10

FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution structure of the FATC domain suggests it plays a role in redox-dependent structural and cellular stability.


Pssm-ID: 426683 [Multi-domain]  Cd Length: 32  Bit Score: 57.01  E-value: 4.30e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 530407765  3633 MSVAEQVDYVIKEATNLDNLAQLYEGWTAW 3662
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPW 31
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
2278-2476 3.40e-07

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: 55.35  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2278 CTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIdMTTGEVVHIDYNVCFekGNIKVDFTFMRakcflvkgqky 2357
Cdd:cd05173   183 YNSGDDLERAIEEFTLSCAGYCVATYVLGIGDRHSDNIMV-RKNGQLFHIDFGHIL--GNFKSKFGIKR----------- 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2358 ndlsfqgkslrvpEKVPFRMTQNI-----ETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWTAGGE 2432
Cdd:cd05173   249 -------------ERVPFILTYDFihviqQGKTGNTEKFGRFRQYCEDAYLILRKNGNLFITLFALMLTAGLPELTSVKD 315
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 530407765 2433 AGFAGAVYGGGGQQAES-KQSKREMEREITRSLFSsrvaeiKVNW 2476
Cdd:cd05173   316 IQYLKDSLALGKSEEEAlKQFRQKFDEALRESWTT------KVNW 354
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2106-2341 4.22e-07

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: 54.99  E-value: 4.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2106 PTKTKPKKLLFLGSD--GKSYPYLFKGLEDLHLDERIMQFLSIVNTMFatinRQETPRFHARHYSVTPLGTRSGLIQWVD 2183
Cdd:cd05166    71 NSNALPLKLVFRNADprAEPISVIFKVGDDLRQDMLTLQLIRIMDKIW----LQEGLDLKMITFRCVPTGNKRGMVELVP 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2184 GATPLfglykRWQQREAALqaqkaqdsyqtpqnpgivprpselyyskigpalktVGlsldvSRRDWPLhvmkavleelme 2263
Cdd:cd05166   147 EAETL-----REIQTEHGL-----------------------------------TG-----SFKDRPL------------ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2264 atppnllAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDynvcFEK-------- 2335
Cdd:cd05166   170 -------ADWLQKHNPSELEYEKAVENFIRSCAGYCVATYVLGICDRHNDNIMLK-TSGHLFHID----FGKflgdaqmf 237

                  ....*.
gi 530407765 2336 GNIKVD 2341
Cdd:cd05166   238 GNFKRD 243
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2278-2416 4.22e-06

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: 51.80  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2278 CTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDynvcFEK--GNIKVDFTFMRakcflvkgq 2355
Cdd:cd00891   175 NPTEEEYEEAVENFIRSCAGYCVATYVLGIGDRHNDNIMVT-KSGHLFHID----FGHflGNFKKKFGIKR--------- 240
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530407765 2356 kyndlsfqgkslrvpEKVPFRMTQNIETALGvtGVEGV----FRLSCEQVLHIMRRGRETLLTLL 2416
Cdd:cd00891   241 ---------------ERAPFVFTPEMAYVMG--GEDSEnfqkFEDLCCKAYNILRKHGNLLINLF 288
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
2275-2407 1.02e-04

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: 47.74  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2275 WSSCTTP-DEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIdMTTGEVVHIDYNVCFekGNIKVDFTFMRakcflvk 2353
Cdd:cd05174   182 WLKSKNPgDALDQAIEEFTLSCAGYCVATYVLGIGDRHSDNIMI-RESGQLFHIDFGHFL--GNFKTKFGINR------- 251
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530407765 2354 gqkyndlsfqgkslrvpEKVPFRMTQNIETAL--GVTGVEGV---FRLSCEQVLHIMRR 2407
Cdd:cd05174   252 -----------------ERVPFILTYDFVHVIqqGKTNNSEKferFRGYCERAYTILRR 293
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
2289-2419 9.80e-04

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: 44.17  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2289 QSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIdynvcfekgnikvDFTFMrakcflvkgqkyndLSFQGKSLR 2368
Cdd:cd00893   122 DNFLQSLVAYSLVCYFLQIKDRHNGNILLD-KEGHIIHI-------------DFGFF--------------LSSHPGFYG 173
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530407765 2369 VpEKVPFRMTQNIETALGVTGVE--GVFRLSCEQVLHIMRRGRETLLTLLEAF 2419
Cdd:cd00893   174 F-EGAPFKLSSEYIEVLGGVDSElfKEFRKLFLKGFMALRKHSDKILSLVEMM 225
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
2291-2421 2.73e-03

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: 42.97  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2291 YARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFEK---GNIKVdftfmrakcflvkgqkyndlsfqgksl 2367
Cdd:cd05167   144 FIKSMAGYSLVSYLLQIKDRHNGNIMID-DDGHIIHIDFGFIFEIspgGNLGF--------------------------- 195
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530407765 2368 rvpEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIM---RRGRETLLTLLEAFVY 2421
Cdd:cd05167   196 ---ESAPFKLTKEMVDLMGGSMESEPFKWFVELCVRGYlavRPYAEAIVSLVELMLD 249
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
2268-2389 4.45e-03

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: 42.54  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2268 NLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIdMTTGEVVHIDYNVCFekGNIKvdftfmra 2347
Cdd:cd00894   177 EVLNHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMI-TETGNLFHIDFGHIL--GNYK-------- 245
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530407765 2348 kcflvkgqkyndlSFQGKSlrvPEKVPFRMTQNIETALGVTG 2389
Cdd:cd00894   246 -------------SFLGIN---KERVPFVLTPDFLFVMGTSG 271
PI3Kc_C2_beta cd00895
Catalytic domain of Class II Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
2270-2354 4.67e-03

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: 42.30  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407765 2270 LAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFEK----GNIKVD---F 2342
Cdd:cd00895   170 LADWLQKHNPTEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDNIMLK-TTGHMFHIDFGRFLGHaqmfGNIKRDrapF 248
                          90
                  ....*....|..
gi 530407765 2343 TFMRAKCFLVKG 2354
Cdd:cd00895   249 VFTSDMAYVING 260
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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