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Conserved domains on  [gi|62243658|ref|NP_055907|]
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serine/threonine-protein kinase SMG1 [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 ...
631-1242 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: 464869  Cd Length: 602  Bit Score: 839.50  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    631 MWALSPTVFALLSKNLMIVHSDLAVHFPAIQYAVLYTLYSHCTRHDHFISSSLSSSSPSLFDGAVISTVTTATKKHFSII 710
Cdd:pfam15785    1 MWALSPSIFELLSTNLRAVDLDLWVRYPAVQYALLNLLYSHCQRHHNFVSSSSLSSSPSLRDGSVQSEVTSPTANNFSTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    711 LNLLGILLKKDNLNQDTRKLLMTWALEaavlMKKSETYAP-LFSLPSFHKFCKGLLANTLVEDVNICLQAC----SSLHA 785
Cdd:pfam15785   81 LNLLAKLLKKDNLNPDNRRLLLKWILE----LRESRTYAPlLFSSPEFLNICRSLLANALKEDVNILLEACaciqAVLSY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    786 LSSSLPDDLLQRCVDVCRVQLVHSGTRIRQAFGKLLKSIPLDVVLS-----------------NNNHTEIQEIslalrsh 848
Cdd:pfam15785  157 NPTFSKDELLQLYVDLCLQQLVHSAPNVRQPFGQLLASLPLHVTLSggsilslgmksrrvcvwQQRHSQISAV------- 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    849 msKAPSNTFHPQDFSDVISFILYGNSHRTGKDNWLERLFYSCQRLDKRD--QSTIPRNLLKTDAVLWQWAIWEAAQFTVL 926
Cdd:pfam15785  230 --RRPSNTFHDQVFRDFMEFILYPETHQQGLTNWLEDLFYSCCQLAKQDerQEMLSRCLLRCQALLWFWAQWEAAQYCVL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    927 SKLRTPLGRAQDTFQTIEGIIRSLAAHTLNPDQDVSQWT-TADNDEGHGNNQLRLVLLLQYLENLEKLMYNAYEGCANAL 1005
Cdd:pfam15785  308 NRLRTPLGKPQDTFQGIEGIIKMHARHLSGPAKEVSRSAlTGLSLEGLLNNQLRLVLLLQFLENLEKLIYNAYEGCAFAL 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   1006 TSPPKVIRTFFYTNRQTCQDWLTRIRLSIMRVGLLAGQPAVTVRHGFDLLTEMKTTSLSQGNELEVTIMMVVEALCELHC 1085
Cdd:pfam15785  388 PAPPKPVRTFFRTNRPTCQEWLSRIRSSVVIIALHSGQPALAIRHGQQLLTEMKKNSLTQGPEFEQAIVYLAWALCELKE 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   1086 PEAIQGIAVWSSSIVGKNLLWINSVAQQAEGRFEKASVEYQEHLCAMTGVDCCISSFDksvltlanagrnsaspkhslng 1165
Cdd:pfam15785  468 SDAIRGLYVWSKEKVGKSFLWLNSLADQAEGKFEKAAAEYQNLLCEMTGQDCELEPHT---------------------- 525
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62243658   1166 esRKTVLSKPTDSSPEVINYLGNKACECYISIADWAAVQEWQNAIHDLKKSTSSTSLNLKADF--NYIKSLSSFESGKF 1242
Cdd:pfam15785  526 --RQKLSINNSPKPPEVLNFVVAQAMECYQSLGDWSSLMEWQQNVLNLPEDSELNPFNQKSDVesNYIRLLSKFEEGDF 602
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2121-2426 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: 628.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2200
Cdd:cd05170    1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGATPLFGLYKRWQQREAALQAQKAQDSYQTPQnpgIVPRPSELYYSKIGPALKTVGLSLDVSRRDWPLHVM 2280
Cdd:cd05170   81 RSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDSGSTPP---PVPRPSELFYNKLKPALKAAGIRKSTSRREWPLEVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2281 KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2360
Cdd:cd05170  158 RQVLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFE 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62243658 2361 KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:cd05170  238 KGKRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLTLLEAFVYDPLVDWT 303
SMG1_N pfam17229
Serine/threonine-protein kinase SMG1 N-terminal; This entry represents the N-terminal ...
32-140 2.38e-50

Serine/threonine-protein kinase SMG1 N-terminal; This entry represents the N-terminal disordered region of SMG1, which is a member of the phosphoinositide 3 kinase-like kinase (PIKK) family. SMG1 associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay. It also plays an important role in genotoxic stress responses to DNA damage.


:

Pssm-ID: 435799  Cd Length: 106  Bit Score: 174.25  E-value: 2.38e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658     32 TDSASADPDNLKYSSSRDRGGSSSYGLQPSNSAVvSRQRHDDTRVHADIqNDEKGGYSVNGGSGENTYGRKSLGQELRVN 111
Cdd:pfam17229    1 GDSVSASQDNLKYSASRERGSSASYDLQPSNSPV-SPPRHDDARAAADA-NEEEGGYEVNGGVGENTFGWKSLGQELRVN 78
                           90       100
                   ....*....|....*....|....*....
gi 62243658    112 NVTSpEFTSVQHGSRALATKDMRKSQERS 140
Cdd:pfam17229   79 DVTS-DLTSFQHGNRALATKDMRKSQDRG 106
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
3631-3660 3.48e-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: 460514 [Multi-domain]  Cd Length: 32  Bit Score: 57.39  E-value: 3.48e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 62243658   3631 MSVAEQVDYVIKEATNLDNLAQLYEGWTAW 3660
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 ...
631-1242 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: 464869  Cd Length: 602  Bit Score: 839.50  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    631 MWALSPTVFALLSKNLMIVHSDLAVHFPAIQYAVLYTLYSHCTRHDHFISSSLSSSSPSLFDGAVISTVTTATKKHFSII 710
Cdd:pfam15785    1 MWALSPSIFELLSTNLRAVDLDLWVRYPAVQYALLNLLYSHCQRHHNFVSSSSLSSSPSLRDGSVQSEVTSPTANNFSTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    711 LNLLGILLKKDNLNQDTRKLLMTWALEaavlMKKSETYAP-LFSLPSFHKFCKGLLANTLVEDVNICLQAC----SSLHA 785
Cdd:pfam15785   81 LNLLAKLLKKDNLNPDNRRLLLKWILE----LRESRTYAPlLFSSPEFLNICRSLLANALKEDVNILLEACaciqAVLSY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    786 LSSSLPDDLLQRCVDVCRVQLVHSGTRIRQAFGKLLKSIPLDVVLS-----------------NNNHTEIQEIslalrsh 848
Cdd:pfam15785  157 NPTFSKDELLQLYVDLCLQQLVHSAPNVRQPFGQLLASLPLHVTLSggsilslgmksrrvcvwQQRHSQISAV------- 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    849 msKAPSNTFHPQDFSDVISFILYGNSHRTGKDNWLERLFYSCQRLDKRD--QSTIPRNLLKTDAVLWQWAIWEAAQFTVL 926
Cdd:pfam15785  230 --RRPSNTFHDQVFRDFMEFILYPETHQQGLTNWLEDLFYSCCQLAKQDerQEMLSRCLLRCQALLWFWAQWEAAQYCVL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    927 SKLRTPLGRAQDTFQTIEGIIRSLAAHTLNPDQDVSQWT-TADNDEGHGNNQLRLVLLLQYLENLEKLMYNAYEGCANAL 1005
Cdd:pfam15785  308 NRLRTPLGKPQDTFQGIEGIIKMHARHLSGPAKEVSRSAlTGLSLEGLLNNQLRLVLLLQFLENLEKLIYNAYEGCAFAL 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   1006 TSPPKVIRTFFYTNRQTCQDWLTRIRLSIMRVGLLAGQPAVTVRHGFDLLTEMKTTSLSQGNELEVTIMMVVEALCELHC 1085
Cdd:pfam15785  388 PAPPKPVRTFFRTNRPTCQEWLSRIRSSVVIIALHSGQPALAIRHGQQLLTEMKKNSLTQGPEFEQAIVYLAWALCELKE 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   1086 PEAIQGIAVWSSSIVGKNLLWINSVAQQAEGRFEKASVEYQEHLCAMTGVDCCISSFDksvltlanagrnsaspkhslng 1165
Cdd:pfam15785  468 SDAIRGLYVWSKEKVGKSFLWLNSLADQAEGKFEKAAAEYQNLLCEMTGQDCELEPHT---------------------- 525
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62243658   1166 esRKTVLSKPTDSSPEVINYLGNKACECYISIADWAAVQEWQNAIHDLKKSTSSTSLNLKADF--NYIKSLSSFESGKF 1242
Cdd:pfam15785  526 --RQKLSINNSPKPPEVLNFVVAQAMECYQSLGDWSSLMEWQQNVLNLPEDSELNPFNQKSDVesNYIRLLSKFEEGDF 602
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2121-2426 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: 628.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2200
Cdd:cd05170    1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGATPLFGLYKRWQQREAALQAQKAQDSYQTPQnpgIVPRPSELYYSKIGPALKTVGLSLDVSRRDWPLHVM 2280
Cdd:cd05170   81 RSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDSGSTPP---PVPRPSELFYNKLKPALKAAGIRKSTSRREWPLEVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2281 KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2360
Cdd:cd05170  158 RQVLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFE 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62243658 2361 KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:cd05170  238 KGKRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLTLLEAFVYDPLVDWT 303
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
2149-2426 3.03e-63

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: 216.81  E-value: 3.03e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   2149 SYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRqetPRFHARHYSVTPLGTRSGLIQWVDGATPLfglykrwqqreAAL 2228
Cdd:pfam00454    1 GYGGIYKVGDDLRQDELILQVFKLMDEELSKDNL---DLRRLKPYSVIPLGPKCGIIEWVPNSETL-----------AYI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   2229 QaqkaqdsyqtpqnpgivprpSELYYSKIGPALKtvglsldVSRRDWPLHVMKAVLEELMEA--TPPNLLAKELWSSCTT 2306
Cdd:pfam00454   67 L--------------------DEYGENGVPPTAM-------VKILHSALNYPKLKLEFESRIslPPKVGLLQWFVKKSPD 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   2307 PDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCF-EKGKSLRVPEKVPFRMTQNIETALGV 2385
Cdd:pfam00454  120 AEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTTGKLFHIDFGLCLpDAGKDLPFPEKVPFRLTREMVYAMGP 199
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 62243658   2386 TGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:pfam00454  200 SGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADGLPDWS 240
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2040-2425 5.73e-56

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 217.73  E-value: 5.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2040 FQDNYGDAIENALEKLKTPLNPakpgsSWIPFKEIMLSLQQRAQKRASYILRLEEISPwLAAMTNTEIALPGEV-SARDT 2118
Cdd:COG5032 1691 LIKKSPRKIRKKFKIDISLLNL-----SRKLYISVLRSIRKRLKRLLELRLKKVSPKL-LLFHAFLEIKLPGQYlLDKPF 1764
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2119 VTIHSVGGTITILPTKT-KPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTP 2197
Cdd:COG5032 1765 VLIERFEPEVSVVKSHLqRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVIP 1844
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2198 LGTRSGLIQWVDGATPLFGLYK--RWQQREAALQAQKAQDSYQtpqnpgivprpselyyskigpaLKTVGLSLDVsrrdw 2275
Cdd:COG5032 1845 LSPGSGIIEWVPNSDTLHSILReyHKRKNISIDQEKKLAARLD----------------------NLKLLLKDEF----- 1897
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2276 plhvmkavlEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDY 2355
Cdd:COG5032 1898 ---------FTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDF 1968
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62243658 2356 NVCFE-KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDW 2425
Cdd:COG5032 1969 GFILFnAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEW 2039
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2153-2426 4.80e-55

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: 193.28  E-value: 4.80e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    2153 LFKGLEDLHLDERIMQFLSIVNTMFAtiNRQETPR--FHARHYSVTPLGTRSGLIQWVDGATPLFGL---YKRWQQREAA 2227
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQ--KDKETRRrdLHLRPYKVIPTGPKSGLIEVVPNSTTLHEIlkeYRKQKGKVLD 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    2228 LQAQKAqdsyqtpqnpgivprpselyyskigpalktvglsldvSRRDWPLHVMKAVLEelmeaTPPNLLAKELWSSCTTP 2307
Cdd:smart00146   80 LRSQTA-------------------------------------TRLKKLELFLEATGK-----FPDPVLYDWFTKKFPDP 117
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    2308 DE-WWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFEKGKSLRVP-EKVPFRMTQNIETALGV 2385
Cdd:smart00146  118 SEdYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLD-KTGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGD 196
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 62243658    2386 TGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:smart00146  197 SGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPDWR 237
SMG1_N pfam17229
Serine/threonine-protein kinase SMG1 N-terminal; This entry represents the N-terminal ...
32-140 2.38e-50

Serine/threonine-protein kinase SMG1 N-terminal; This entry represents the N-terminal disordered region of SMG1, which is a member of the phosphoinositide 3 kinase-like kinase (PIKK) family. SMG1 associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay. It also plays an important role in genotoxic stress responses to DNA damage.


Pssm-ID: 435799  Cd Length: 106  Bit Score: 174.25  E-value: 2.38e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658     32 TDSASADPDNLKYSSSRDRGGSSSYGLQPSNSAVvSRQRHDDTRVHADIqNDEKGGYSVNGGSGENTYGRKSLGQELRVN 111
Cdd:pfam17229    1 GDSVSASQDNLKYSASRERGSSASYDLQPSNSPV-SPPRHDDARAAADA-NEEEGGYEVNGGVGENTFGWKSLGQELRVN 78
                           90       100
                   ....*....|....*....|....*....
gi 62243658    112 NVTSpEFTSVQHGSRALATKDMRKSQERS 140
Cdd:pfam17229   79 DVTS-DLTSFQHGNRALATKDMRKSQDRG 106
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
3631-3660 3.48e-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: 460514 [Multi-domain]  Cd Length: 32  Bit Score: 57.39  E-value: 3.48e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 62243658   3631 MSVAEQVDYVIKEATNLDNLAQLYEGWTAW 3660
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 ...
631-1242 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: 464869  Cd Length: 602  Bit Score: 839.50  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    631 MWALSPTVFALLSKNLMIVHSDLAVHFPAIQYAVLYTLYSHCTRHDHFISSSLSSSSPSLFDGAVISTVTTATKKHFSII 710
Cdd:pfam15785    1 MWALSPSIFELLSTNLRAVDLDLWVRYPAVQYALLNLLYSHCQRHHNFVSSSSLSSSPSLRDGSVQSEVTSPTANNFSTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    711 LNLLGILLKKDNLNQDTRKLLMTWALEaavlMKKSETYAP-LFSLPSFHKFCKGLLANTLVEDVNICLQAC----SSLHA 785
Cdd:pfam15785   81 LNLLAKLLKKDNLNPDNRRLLLKWILE----LRESRTYAPlLFSSPEFLNICRSLLANALKEDVNILLEACaciqAVLSY 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    786 LSSSLPDDLLQRCVDVCRVQLVHSGTRIRQAFGKLLKSIPLDVVLS-----------------NNNHTEIQEIslalrsh 848
Cdd:pfam15785  157 NPTFSKDELLQLYVDLCLQQLVHSAPNVRQPFGQLLASLPLHVTLSggsilslgmksrrvcvwQQRHSQISAV------- 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    849 msKAPSNTFHPQDFSDVISFILYGNSHRTGKDNWLERLFYSCQRLDKRD--QSTIPRNLLKTDAVLWQWAIWEAAQFTVL 926
Cdd:pfam15785  230 --RRPSNTFHDQVFRDFMEFILYPETHQQGLTNWLEDLFYSCCQLAKQDerQEMLSRCLLRCQALLWFWAQWEAAQYCVL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    927 SKLRTPLGRAQDTFQTIEGIIRSLAAHTLNPDQDVSQWT-TADNDEGHGNNQLRLVLLLQYLENLEKLMYNAYEGCANAL 1005
Cdd:pfam15785  308 NRLRTPLGKPQDTFQGIEGIIKMHARHLSGPAKEVSRSAlTGLSLEGLLNNQLRLVLLLQFLENLEKLIYNAYEGCAFAL 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   1006 TSPPKVIRTFFYTNRQTCQDWLTRIRLSIMRVGLLAGQPAVTVRHGFDLLTEMKTTSLSQGNELEVTIMMVVEALCELHC 1085
Cdd:pfam15785  388 PAPPKPVRTFFRTNRPTCQEWLSRIRSSVVIIALHSGQPALAIRHGQQLLTEMKKNSLTQGPEFEQAIVYLAWALCELKE 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   1086 PEAIQGIAVWSSSIVGKNLLWINSVAQQAEGRFEKASVEYQEHLCAMTGVDCCISSFDksvltlanagrnsaspkhslng 1165
Cdd:pfam15785  468 SDAIRGLYVWSKEKVGKSFLWLNSLADQAEGKFEKAAAEYQNLLCEMTGQDCELEPHT---------------------- 525
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62243658   1166 esRKTVLSKPTDSSPEVINYLGNKACECYISIADWAAVQEWQNAIHDLKKSTSSTSLNLKADF--NYIKSLSSFESGKF 1242
Cdd:pfam15785  526 --RQKLSINNSPKPPEVLNFVVAQAMECYQSLGDWSSLMEWQQNVLNLPEDSELNPFNQKSDVesNYIRLLSKFEEGDF 602
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
2121-2426 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: 628.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2200
Cdd:cd05170    1 IQSVGSTVTVLPTKTKPKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGATPLFGLYKRWQQREAALQAQKAQDSYQTPQnpgIVPRPSELYYSKIGPALKTVGLSLDVSRRDWPLHVM 2280
Cdd:cd05170   81 RSGLIQWVDGATPLFSLYKRWQQRRAAAQAQKNQDSGSTPP---PVPRPSELFYNKLKPALKAAGIRKSTSRREWPLEVL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2281 KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2360
Cdd:cd05170  158 RQVLEELVAETPRDLLARELWCSSPSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFE 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62243658 2361 KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:cd05170  238 KGKRLRVPEKVPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLTLLEAFVYDPLVDWT 303
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
2121-2420 9.91e-102

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: 326.15  E-value: 9.91e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2200
Cdd:cd05164    1 IASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGDDDLRKDERVMQLFQLLNTLLEKDKETRKRNLTIRTYSVVPLSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGATPLFGLYKRWqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwplhvm 2280
Cdd:cd05164   81 QSGLIEWVDNTTTLKPVLKKW----------------------------------------------------------- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2281 kavleelmeatppnllakeLWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2360
Cdd:cd05164  102 -------------------FNETFPDPTQWYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKTGEVVHIDFGMIFN 162
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2361 KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYD 2420
Cdd:cd05164  163 KGKTLPVPEIVPFRLTRNIINGMGPTGVEGLFRKSCEQVLRVFRKHKDKLITFLDTFLYD 222
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
2121-2425 8.15e-92

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: 300.17  E-value: 8.15e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2200
Cdd:cd05169    1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDERVMQLFGLVNTLLKNDSETSRRNLSIQRYSVIPLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGATPLFGLYKRW-QQREAALQAQKAQDSYQTPQnpgivprpselYYSkigpalktvglsldvsrrdwpLHV 2279
Cdd:cd05169   81 NSGLIGWVPGCDTLHSLIRDYrEKRKIPLNIEHRLMLQMAPD-----------YDN---------------------LTL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2280 M--KAVLEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNV 2357
Cdd:cd05169  129 IqkVEVFEYALENTPGDDLRRVLWLKSPSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDFGD 208
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2358 CFEKGKsLRV--PEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDW 2425
Cdd:cd05169  209 CFEVAM-HREkfPEKVPFRLTRMLVNAMEVSGVEGTFRSTCEDVMRVLRENKDSLMAVLEAFVHDPLISW 277
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
2121-2426 3.50e-84

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: 276.69  E-value: 3.50e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2200
Cdd:cd00892    1 ISGFEDEVEIMPSLQKPKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGatplfglykrwqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwpLHVM 2280
Cdd:cd00892   81 ECGIIEWVPN------------------------------------------------------------------TVTL 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2281 KAVLEELMeatPPnLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2360
Cdd:cd00892   95 RSILSTLY---PP-VLHEWFLKNFPDPTAWYEARNNYTRSTAVMSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFD 170
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62243658 2361 KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:cd00892  171 KGLTLEVPERVPFRLTQNMVDAMGVTGVEGTFRRTCEVTLRVLRENRETLMSVLETFVHDPLVEWS 236
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
2121-2426 2.75e-78

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: 261.70  E-value: 2.75e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFAtiNRQET--PRFHARHYSVTPL 2198
Cdd:cd05171    1 ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLK--RDKETrkRKLRIRTYKVVPL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2199 GTRSGLIQWVDGATPLfGLYKRwqqreAALQAQKAQDSYqtpqnpgivpRPSELYYSKIGPALKTVGLSLDVSRRdwplh 2278
Cdd:cd05171   79 SPRSGVLEFVENTIPL-GEYLV-----GASSKSGAHARY----------RPKDWTASTCRKKMREKAKASAEERL----- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2279 vmkAVLEELMEATPPnLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVC 2358
Cdd:cd05171  138 ---KVFDEICKNFKP-VFRHFFLEKFPDPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIA 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62243658 2359 FEKGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:cd05171  214 FEQGKLLPIPETVPFRLTRDIVDGMGITGVEGVFRRCCEETLRVLRENKEALLTILEVLLYDPLYSWT 281
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
2149-2426 3.03e-63

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: 216.81  E-value: 3.03e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   2149 SYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRqetPRFHARHYSVTPLGTRSGLIQWVDGATPLfglykrwqqreAAL 2228
Cdd:pfam00454    1 GYGGIYKVGDDLRQDELILQVFKLMDEELSKDNL---DLRRLKPYSVIPLGPKCGIIEWVPNSETL-----------AYI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   2229 QaqkaqdsyqtpqnpgivprpSELYYSKIGPALKtvglsldVSRRDWPLHVMKAVLEELMEA--TPPNLLAKELWSSCTT 2306
Cdd:pfam00454   67 L--------------------DEYGENGVPPTAM-------VKILHSALNYPKLKLEFESRIslPPKVGLLQWFVKKSPD 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658   2307 PDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCF-EKGKSLRVPEKVPFRMTQNIETALGV 2385
Cdd:pfam00454  120 AEEWGEARKNFVRSCAGYSVLDYILGNGDRHLDNILVDKTTGKLFHIDFGLCLpDAGKDLPFPEKVPFRLTREMVYAMGP 199
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 62243658   2386 TGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:pfam00454  200 SGDEGLFRELCETAYEALRRNLNLLTNLLKLMVADGLPDWS 240
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2040-2425 5.73e-56

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 217.73  E-value: 5.73e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2040 FQDNYGDAIENALEKLKTPLNPakpgsSWIPFKEIMLSLQQRAQKRASYILRLEEISPwLAAMTNTEIALPGEV-SARDT 2118
Cdd:COG5032 1691 LIKKSPRKIRKKFKIDISLLNL-----SRKLYISVLRSIRKRLKRLLELRLKKVSPKL-LLFHAFLEIKLPGQYlLDKPF 1764
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2119 VTIHSVGGTITILPTKT-KPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTP 2197
Cdd:COG5032 1765 VLIERFEPEVSVVKSHLqRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKVIP 1844
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2198 LGTRSGLIQWVDGATPLFGLYK--RWQQREAALQAQKAQDSYQtpqnpgivprpselyyskigpaLKTVGLSLDVsrrdw 2275
Cdd:COG5032 1845 LSPGSGIIEWVPNSDTLHSILReyHKRKNISIDQEKKLAARLD----------------------NLKLLLKDEF----- 1897
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2276 plhvmkavlEELMEATPPNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDY 2355
Cdd:COG5032 1898 ---------FTKATLKSPPVLYDWFSESFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDF 1968
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62243658 2356 NVCFE-KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDW 2425
Cdd:COG5032 1969 GFILFnAPGRFPFPEKVPFRLTRNIVEAMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEW 2039
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
2153-2426 4.80e-55

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: 193.28  E-value: 4.80e-55
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    2153 LFKGLEDLHLDERIMQFLSIVNTMFAtiNRQETPR--FHARHYSVTPLGTRSGLIQWVDGATPLFGL---YKRWQQREAA 2227
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQ--KDKETRRrdLHLRPYKVIPTGPKSGLIEVVPNSTTLHEIlkeYRKQKGKVLD 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    2228 LQAQKAqdsyqtpqnpgivprpselyyskigpalktvglsldvSRRDWPLHVMKAVLEelmeaTPPNLLAKELWSSCTTP 2307
Cdd:smart00146   80 LRSQTA-------------------------------------TRLKKLELFLEATGK-----FPDPVLYDWFTKKFPDP 117
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658    2308 DE-WWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFEKGKSLRVP-EKVPFRMTQNIETALGV 2385
Cdd:smart00146  118 SEdYFEARKNFTRSCAGYSVITYILGLGDRHNDNIMLD-KTGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGD 196
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 62243658    2386 TGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWT 2426
Cdd:smart00146  197 SGYFGLFRSLCERALRALRKNSNLIMSLLELMLYDGLPDWR 237
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
2121-2425 1.01e-53

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: 189.32  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFATINRQETPRFHARHYSVTPLGT 2200
Cdd:cd05172    1 IVGFDPRVLVLSSKRRPKRITIRGSDEKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDPACRQRRLRIRTYQVIPMTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGATPLfglykrwqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwplhvm 2280
Cdd:cd05172   81 RLGLIEWVDNTTPL------------------------------------------------------------------ 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2281 KAVLEElmeatppNLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFE 2360
Cdd:cd05172   95 KEILEN-------DLLRRALLSLASSPEAFLALRSNFARSLAAMSICGYILGIGDRHLSNFLVDLSTGRLIGIDFGHAFG 167
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62243658 2361 KGKS-LRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDW 2425
Cdd:cd05172  168 SATQfLPIPELVPFRLTRQLLNLLQPLDARGLLRSDMVHVLRALRAGRDLLLATMDVFVKEPLLDW 233
SMG1_N pfam17229
Serine/threonine-protein kinase SMG1 N-terminal; This entry represents the N-terminal ...
32-140 2.38e-50

Serine/threonine-protein kinase SMG1 N-terminal; This entry represents the N-terminal disordered region of SMG1, which is a member of the phosphoinositide 3 kinase-like kinase (PIKK) family. SMG1 associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay. It also plays an important role in genotoxic stress responses to DNA damage.


Pssm-ID: 435799  Cd Length: 106  Bit Score: 174.25  E-value: 2.38e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658     32 TDSASADPDNLKYSSSRDRGGSSSYGLQPSNSAVvSRQRHDDTRVHADIqNDEKGGYSVNGGSGENTYGRKSLGQELRVN 111
Cdd:pfam17229    1 GDSVSASQDNLKYSASRERGSSASYDLQPSNSPV-SPPRHDDARAAADA-NEEEGGYEVNGGVGENTFGWKSLGQELRVN 78
                           90       100
                   ....*....|....*....|....*....
gi 62243658    112 NVTSpEFTSVQHGSRALATKDMRKSQERS 140
Cdd:pfam17229   79 DVTS-DLTSFQHGNRALATKDMRKSQDRG 106
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
2121-2420 2.28e-39

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: 147.09  E-value: 2.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2121 IHSVGGTITILPTKTKPKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFatinRQETPRFHARHYSVTPLGT 2200
Cdd:cd00142    1 NALDVGILKVIHSKQRPKKITLIGADGKTYSFLLKRRDDLRKDERSFQFMRLIQSIL----EKESVNLVLPPYKVIPLSE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2201 RSGLIQWVDGATPLFGLykrwqqreaalqaqkaqdsyqtpqnpgivprpselyyskigpalktvglsldvsrrdwplhvm 2280
Cdd:cd00142   77 NSGLIEIVKDAQTIEDL--------------------------------------------------------------- 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2281 kavleelmeatppnllAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFE 2360
Cdd:cd00142   94 ----------------LKSLWRKSPSSQSWLNRRENFSCSLAGYSVLGYIFGIGDRHPSNIMIE-PSGNIFHIDFGFIFS 156
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2361 KGKSLRVPEKVPFRMTQNIETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYD 2420
Cdd:cd00142  157 GRKLAEGVETVPFRLTPMLENAMGTAGVNGPFQISMVKIMEILREHADLIVPILEHSLRD 216
PIKK_TRRAP cd05163
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs ...
2138-2392 5.87e-14

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: 74.48  E-value: 5.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2138 KKLLFLGSDGKSYPYL--FKGLEDLHLDERIMQFLSIVNTMFATinRQETPRFHARHY--SVTPLGTRSGLIQwvdgatp 2213
Cdd:cd05163   19 RRLTIRGHDGSKYPFLvqTPSARHSRREERVMQLFRLLNRVLER--KKETRRRNLQFHvpIVVPLSPQVRLVE------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2214 lfglykrwqqreaalqaqkAQDSYQTPQNPgivprpselyYSKigpalktvglsldvsrrdwpLHVMKAVLEELMeatPP 2293
Cdd:cd05163   90 -------------------DDPSYISLQDI----------YEK--------------------LEILNEIQSKMV---PE 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2294 NLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDMTTGEVVHIDYNVCFEKGKSL-RVPEKVP 2372
Cdd:cd05163  118 TILSNYFLRTMPSPSDLWLFRKQFTLQLALSSFMTYVLSLGNRTPHRILISRSTGNVFMTDFLPSINSQGPLlDNNEPVP 197
                        250       260
                 ....*....|....*....|
gi 62243658 2373 FRMTQNIETALGVTGVEGVF 2392
Cdd:cd05163  198 FRLTPNIQHFIGPIGVEGLL 217
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2128-2355 7.26e-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: 7.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2128 ITILPTKTK-------PKKLLFLGSDGKSYPYLFKGLEDLHLDERIMQFLSIVNTMFatinRQE------TPrfharhYS 2194
Cdd:cd00896   64 TGIIPEKSTvfksalmPLKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLL----KKEnldlklTP------YK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2195 VTPLGTRSGLIQWVDGATPLFGLYKRWQQREAALQAQkaqdsyqtpqnpgivpRPSElyyskigpalktvglsldvsrrD 2274
Cdd:cd00896  134 VLATSPNDGLVEFVPNSKALADILKKYGSILNFLRKH----------------NPDE----------------------S 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2275 WPLHVMKAVLeelmeatppnllakelwsscttpdewwrvtQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHID 2354
Cdd:cd00896  176 GPYGIKPEVM------------------------------DNFVKSCAGYCVITYILGVGDRHLDNLLLT-KDGHLFHID 224

                 .
gi 62243658 2355 Y 2355
Cdd:cd00896  225 F 225
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
3631-3660 3.48e-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: 460514 [Multi-domain]  Cd Length: 32  Bit Score: 57.39  E-value: 3.48e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 62243658   3631 MSVAEQVDYVIKEATNLDNLAQLYEGWTAW 3660
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPW 31
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2132-2415 4.03e-08

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: 58.46  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2132 PTKTKPKKLLFLGSD--GKSYPYLFKGLEDLHLDERIMQFLSIVNTMFatinRQETPRFHARHYSVTPLGTRSGLIQWVD 2209
Cdd:cd05166   71 NSNALPLKLVFRNADprAEPISVIFKVGDDLRQDMLTLQLIRIMDKIW----LQEGLDLKMITFRCVPTGNKRGMVELVP 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2210 GATPLfglykRWQQREAALqaqkaqdsyqtpqnpgivprpselyyskigpalktVGlsldvSRRDWPLhvmkavleelme 2289
Cdd:cd05166  147 EAETL-----REIQTEHGL-----------------------------------TG-----SFKDRPL------------ 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2290 atppnllAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYnvcfekGKSLRVPE 2369
Cdd:cd05166  170 -------ADWLQKHNPSELEYEKAVENFIRSCAGYCVATYVLGICDRHNDNIMLK-TSGHLFHIDF------GKFLGDAQ 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62243658 2370 K--------VPFRMTQN----IETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLE 2415
Cdd:cd05166  236 MfgnfkrdrVPFVLTSDmayvINGGDKPSSRFQLFVDLCCQAFNIIRKNSNLLLNLLS 293
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
2304-2474 1.30e-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: 56.89  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2304 CTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIdMTTGEVVHIDYNVCFEKGKS-LRVP-EKVPFRMTQNI-- 2379
Cdd:cd05173  183 YNSGDDLERAIEEFTLSCAGYCVATYVLGIGDRHSDNIMV-RKNGQLFHIDFGHILGNFKSkFGIKrERVPFILTYDFih 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2380 ---ETALGVTGVEGVFRLSCEQVLHIMRRGRETLLTLLEAFVYDPLVDWTAGGEAGFAGAVYGGGGQQAES-KQSKREME 2455
Cdd:cd05173  262 viqQGKTGNTEKFGRFRQYCEDAYLILRKNGNLFITLFALMLTAGLPELTSVKDIQYLKDSLALGKSEEEAlKQFRQKFD 341
                        170
                 ....*....|....*....
gi 62243658 2456 REITRSLFSsrvaeiKVNW 2474
Cdd:cd05173  342 EALRESWTT------KVNW 354
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
2304-2414 4.24e-07

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: 54.88  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2304 CTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDY-----NVcfeKGKSLRVPEKVPFRMTQN 2378
Cdd:cd00891  175 NPTEEEYEEAVENFIRSCAGYCVATYVLGIGDRHNDNIMVT-KSGHLFHIDFghflgNF---KKKFGIKRERAPFVFTPE 250
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 62243658 2379 IETALGvtGVEGV----FRLSCEQVLHIMRRGRETLLTLL 2414
Cdd:cd00891  251 MAYVMG--GEDSEnfqkFEDLCCKAYNILRKHGNLLINLF 288
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
2317-2419 1.04e-05

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: 50.67  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2317 YARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDYNVCFE--KGKSLRVpEKVPFRMTQNIETALGVTGVEGVFRL 2394
Cdd:cd05167  144 FIKSMAGYSLVSYLLQIKDRHNGNIMID-DDGHIIHIDFGFIFEisPGGNLGF-ESAPFKLTKEMVDLMGGSMESEPFKW 221
                         90       100
                 ....*....|....*....|....*...
gi 62243658 2395 SCEQVLHIM---RRGRETLLTLLEAFVY 2419
Cdd:cd05167  222 FVELCVRGYlavRPYAEAIVSLVELMLD 249
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
2315-2417 1.24e-05

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: 49.95  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2315 QSYARSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDY---------NVCFekgkslrvpEKVPFRMTQNIETALGV 2385
Cdd:cd00893  122 DNFLQSLVAYSLVCYFLQIKDRHNGNILLD-KEGHIIHIDFgfflsshpgFYGF---------EGAPFKLSSEYIEVLGG 191
                         90       100       110
                 ....*....|....*....|....*....|....
gi 62243658 2386 TGVE--GVFRLSCEQVLHIMRRGRETLLTLLEAF 2417
Cdd:cd00893  192 VDSElfKEFRKLFLKGFMALRKHSDKILSLVEMM 225
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
2301-2405 1.03e-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: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2301 WSSCTTP-DEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIdMTTGEVVHIDYNVCFEKGKSL----RvpEKVPFRM 2375
Cdd:cd05174  182 WLKSKNPgDALDQAIEEFTLSCAGYCVATYVLGIGDRHSDNIMI-RESGQLFHIDFGHFLGNFKTKfginR--ERVPFIL 258
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 62243658 2376 TQNIETAL--GVTGVEGV---FRLSCEQVLHIMRR 2405
Cdd:cd05174  259 TYDFVHVIqqGKTNNSEKferFRGYCERAYTILRR 293
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
2294-2387 1.40e-04

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: 47.17  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2294 NLLAKELWSSCTTPDEWWRVTQSYARSTAVMSMVGYIIGLGDRHLDNVLIdMTTGEVVHIDYNVCFEKGKSLR--VPEKV 2371
Cdd:cd00894  177 EVLNHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMI-TETGNLFHIDFGHILGNYKSFLgiNKERV 255
                         90
                 ....*....|....*.
gi 62243658 2372 PFRMTQNIETALGVTG 2387
Cdd:cd00894  256 PFVLTPDFLFVMGTSG 271
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
2319-2415 1.10e-03

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: 44.01  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62243658 2319 RSTAVMSMVGYIIGLGDRHLDNVLIDmTTGEVVHIDY---------NVCFekgkslrvpEKVPFRMTQNIETALGvtGVE 2389
Cdd:cd05168  129 ESLAAYSLVCYLLQIKDRHNGNILLD-SEGHIIHIDFgfmlsnspgGLGF---------ETAPFKLTQEYVEVMG--GLE 196
                         90       100       110
                 ....*....|....*....|....*....|
gi 62243658 2390 G----VFRLSCEQVLHIMRRGRETLLTLLE 2415
Cdd:cd05168  197 SdmfrYFKTLMIQGFLALRKHADRIVLLVE 226
 
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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