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Conserved domains on  [gi|767970205|ref|XP_011541146|]
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serine-protein kinase ATM isoform X4 [Homo sapiens]

Protein Classification

FAT and PIKKc_ATM domain-containing protein( domain architecture ID 12033446)

protein containing domains FAT, PIKKc_ATM, and FATC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 2335-2614 0e+00

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: 584.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2335 IQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQ 2414
Cdd:cd05171     1 ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLKRDKETRKRKLRIRTYKVVPLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2415 RSGVLEWCTGTVPIGEFLVNN--EDGAHKRYRPNDFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFL 2492
Cdd:cd05171    81 RSGVLEFVENTIPLGEYLVGAssKSGAHARYRPKDWTASTCRKKMREKAKASAEERLKVFDEICKNFKPVFRHFFLEKFP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2493 DPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGI 2572
Cdd:cd05171   161 DPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIAFEQGKLLPIPETVPFRLTRDIVDGMGI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767970205 2573 TGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTM 2614
Cdd:cd05171   241 TGVEGVFRRCCEETLRVLRENKEALLTILEVLLYDPLYSWTV 282
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 1749-2141 7.91e-57

FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.


:

Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 201.81  E-value: 7.91e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1749 ELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEVEEMCKRSLESVYSLYPTLSRL 1828
Cdd:pfam02259    2 PLAAEAAWRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVRL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1829 QAIGELESIGELFSRSV-THRQLSEVYIKWQKHSQLLKDsDFSFQEPIMALRTVILEILMEKEMDnsqrecikDILTKHL 1907
Cdd:pfam02259   82 QQLAELEEIIQYKQKLGqSSEELKSLLQTWRNRLPGCQD-DVEIWQDILTVRSLVLSPIEDVYLG--------GYHAEMW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1908 VELSILARTFKNTQLPERAIFQIKQYNSVSCGVsEWQLEEAQVFWAKKEQSLALSILKQMIKKldasCAANNPSLKLTYT 1987
Cdd:pfam02259  153 LKFANLARKSGRFSLAEKALLKLLGEDPEEWLP-EVVYAYAKYLWPTGEQQEALLKLREFLSC----YLQKNGELLSGLE 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1988 EClrvcgnwLAETCLENPAVIMQTYLEKAVEVAGNYDGESSdELRNGKMKAFLSLARFSDTQYQrIENYMKSSEFENKQA 2067
Cdd:pfam02259  228 VI-------NPTNLEEFTELLARCYLLKGKWQAALGQNWAE-EKSEEILQAYLLATQFDPSWYK-AWHTWALFNFEVLRK 298

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767970205  2068 LLKRAKEEVgllrehkiqtnrytvkvqreleldelalralKEDRKRFLCKAVENYINCLLSGEEHDM-WVFRLCS 2141
Cdd:pfam02259  299 EEQGKEEEG-------------------------------PEDLSRYVVPAVEGYLRSLSLSSENSLqDTLRLLT 342
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
 2678-2707 2.74e-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: 57.01  E-value: 2.74e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 767970205  2678 LSVGGQVNLLIQQAIDPKNLSRLFPGWKAW 2707
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPW 31
 
Name Accession Description Interval E-value
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 2335-2614 0e+00

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: 584.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2335 IQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQ 2414
Cdd:cd05171     1 ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLKRDKETRKRKLRIRTYKVVPLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2415 RSGVLEWCTGTVPIGEFLVNN--EDGAHKRYRPNDFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFL 2492
Cdd:cd05171    81 RSGVLEFVENTIPLGEYLVGAssKSGAHARYRPKDWTASTCRKKMREKAKASAEERLKVFDEICKNFKPVFRHFFLEKFP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2493 DPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGI 2572
Cdd:cd05171   161 DPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIAFEQGKLLPIPETVPFRLTRDIVDGMGI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767970205 2573 TGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTM 2614
Cdd:cd05171   241 TGVEGVFRRCCEETLRVLRENKEALLTILEVLLYDPLYSWTV 282
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 2367-2616 4.05e-81

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: 267.63  E-value: 4.05e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205   2367 LVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKRYRPn 2446
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKVLDL- 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205   2447 dfsafqcqkkmMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFLDPA-IWFEKRLAYTRSVATSSIVGYILGLGDRHV 2525
Cdd:smart00146   81 -----------RSQTATRLKKLELFLEATGKFPDPVLYDWFTKKFPDPSeDYFEARKNFTRSCAGYSVITYILGLGDRHN 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205   2526 QNILINEqSAELVHIDLGVAFEQGKILPTP-ETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVL 2604
Cdd:smart00146  150 DNIMLDK-TGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELM 228

                           250
                    ....*....|..
gi 767970205   2605 LYDPLFDWTMNP 2616
Cdd:smart00146  229 LYDGLPDWRSGK 240
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2331-2707 1.20e-73

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 275.12  E-value: 1.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2331 NLVTIQSFKAEFRLA-GGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKV 2409
Cdd:COG5032  1763 PFVLIERFEPEVSVVkSHLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKV 1842

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2410 VPLSQRSGVLEWCTGTVPIGEFLvnneDGAHKRYRpndFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCME 2489
Cdd:COG5032  1843 IPLSPGSGIIEWVPNSDTLHSIL----REYHKRKN---ISIDQEKKLAARLDNLKLLLKDEFFTKATLKSPPVLYDWFSE 1915

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2490 KFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLG-VAFEQGKILPTPETVPFRLTRDIVD 2568
Cdd:COG5032  1916 SFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFGfILFNAPGRFPFPEKVPFRLTRNIVE 1995

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2569 GMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPlkalylqqrpedetelhptlnaddqeckrnls 2648
Cdd:COG5032  1996 AMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRRLP-------------------------------- 2043

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970205 2649 DIDQSFNKVAERVLMRLQEKLKG--VEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGWKAW 2707
Cdd:COG5032  2044 CFREIQNNEIVNVLERFRLKLSEkdAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPF 2104
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 2367-2614 5.59e-58

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: 201.40  E-value: 5.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  2367 LVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRkltICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDgahKRYRPN 2446
Cdd:pfam00454    5 IYKVGDDLRQDELILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGE---NGVPPT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  2447 DFSAFQCQKKMMEVQKKSFEEKYEVFMDVcqnfqPVFRYFcMEKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQ 2526
Cdd:pfam00454   79 AMVKILHSALNYPKLKLEFESRISLPPKV-----GLLQWF-VKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  2527 NILINEQSAELVHIDLGVAF-EQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLL 2605
Cdd:pfam00454  153 NILVDKTTGKLFHIDFGLCLpDAGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMV 232


                   ....*....
gi 767970205  2606 YDPLFDWTM 2614
Cdd:pfam00454  233 ADGLPDWSI 241
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 1749-2141 7.91e-57

FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 201.81  E-value: 7.91e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1749 ELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEVEEMCKRSLESVYSLYPTLSRL 1828
Cdd:pfam02259    2 PLAAEAAWRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVRL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1829 QAIGELESIGELFSRSV-THRQLSEVYIKWQKHSQLLKDsDFSFQEPIMALRTVILEILMEKEMDnsqrecikDILTKHL 1907
Cdd:pfam02259   82 QQLAELEEIIQYKQKLGqSSEELKSLLQTWRNRLPGCQD-DVEIWQDILTVRSLVLSPIEDVYLG--------GYHAEMW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1908 VELSILARTFKNTQLPERAIFQIKQYNSVSCGVsEWQLEEAQVFWAKKEQSLALSILKQMIKKldasCAANNPSLKLTYT 1987
Cdd:pfam02259  153 LKFANLARKSGRFSLAEKALLKLLGEDPEEWLP-EVVYAYAKYLWPTGEQQEALLKLREFLSC----YLQKNGELLSGLE 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1988 EClrvcgnwLAETCLENPAVIMQTYLEKAVEVAGNYDGESSdELRNGKMKAFLSLARFSDTQYQrIENYMKSSEFENKQA 2067
Cdd:pfam02259  228 VI-------NPTNLEEFTELLARCYLLKGKWQAALGQNWAE-EKSEEILQAYLLATQFDPSWYK-AWHTWALFNFEVLRK 298

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767970205  2068 LLKRAKEEVgllrehkiqtnrytvkvqreleldelalralKEDRKRFLCKAVENYINCLLSGEEHDM-WVFRLCS 2141
Cdd:pfam02259  299 EEQGKEEEG-------------------------------PEDLSRYVVPAVEGYLRSLSLSSENSLqDTLRLLT 342
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
 2678-2707 2.74e-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: 57.01  E-value: 2.74e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 767970205  2678 LSVGGQVNLLIQQAIDPKNLSRLFPGWKAW 2707
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPW 31
 
Name Accession Description Interval E-value
PIKKc_ATM cd05171
Catalytic domain of Ataxia Telangiectasia Mutated; ATM is critical in the response to DNA ...
 2335-2614 0e+00

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: 584.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2335 IQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQ 2414
Cdd:cd05171     1 ISRFEDTFTLAGGINLPKIITCIGSDGKKYKQLVKGGDDLRQDAVMEQVFELVNQLLKRDKETRKRKLRIRTYKVVPLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2415 RSGVLEWCTGTVPIGEFLVNN--EDGAHKRYRPNDFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFL 2492
Cdd:cd05171    81 RSGVLEFVENTIPLGEYLVGAssKSGAHARYRPKDWTASTCRKKMREKAKASAEERLKVFDEICKNFKPVFRHFFLEKFP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2493 DPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGI 2572
Cdd:cd05171   161 DPSDWFERRLAYTRSVATSSIVGYILGLGDRHLNNILIDQKTGELVHIDLGIAFEQGKLLPIPETVPFRLTRDIVDGMGI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767970205 2573 TGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTM 2614
Cdd:cd05171   241 TGVEGVFRRCCEETLRVLRENKEALLTILEVLLYDPLYSWTV 282
PIKKc cd05164
Catalytic domain of Phosphoinositide 3-kinase-related protein kinases; PIKK subfamily members ...
 2335-2607 1.61e-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: 1.61e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2335 IQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQ 2414
Cdd:cd05164     1 IASFDPRVRILASLQKPKKITILGSDGKEYPFLVKGDDDLRKDERVMQLFQLLNTLLEKDKETRKRNLTIRTYSVVPLSS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2415 RSGVLEWCTGTVPIGeflvnnedgahkryrpndfsafqcqkkmmevqkksfeekyevfmdvcqnfqPVFRYFCMEKFLDP 2494
Cdd:cd05164    81 QSGLIEWVDNTTTLK---------------------------------------------------PVLKKWFNETFPDP 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2495 AIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITG 2574
Cdd:cd05164   110 TQWYEARSNYTKSTAVMSMVGYIIGLGDRHLENILIDTKTGEVVHIDFGMIFNKGKTLPVPEIVPFRLTRNIINGMGPTG 189

                         250       260       270
                  ....*....|....*....|....*....|...
gi 767970205 2575 VEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYD 2607
Cdd:cd05164   190 VEGLFRKSCEQVLRVFRKHKDKLITFLDTFLYD 222
PIKKc_ATR cd00892
Catalytic domain of Ataxia telangiectasia and Rad3-related proteins; ATR is also referred to ...
 2351-2613 2.65e-85

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: 279.39  E-value: 2.65e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2351 PKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGE 2430
Cdd:cd00892    17 PKKITLVGSDGKKYPFLCKPKDDLRKDARMMEFNTLINRLLSKDPESRRRNLHIRTYAVIPLNEECGIIEWVPNTVTLRS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2431 FLVnnedgahkRYRPndfsafqcqkkmmevqkksfeekyevfmdvcqnfqPVFRYFCMEKFLDPAIWFEKRLAYTRSVAT 2510
Cdd:cd00892    97 ILS--------TLYP-----------------------------------PVLHEWFLKNFPDPTAWYEARNNYTRSTAV 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2511 SSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVM 2590
Cdd:cd00892   134 MSMVGYILGLGDRHGENILFDSTTGDVVHVDFDCLFDKGLTLEVPERVPFRLTQNMVDAMGVTGVEGTFRRTCEVTLRVL 213

                         250       260
                  ....*....|....*....|...
gi 767970205 2591 RNSQETLLTIVEVLLYDPLFDWT 2613
Cdd:cd00892   214 RENRETLMSVLETFVHDPLVEWS 236
PI3Kc smart00146
Phosphoinositide 3-kinase, catalytic domain; Phosphoinositide 3-kinase isoforms participate in ...
 2367-2616 4.05e-81

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: 267.63  E-value: 4.05e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205   2367 LVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKRYRPn 2446
Cdd:smart00146    2 IFKGGDDLRQDERVLQLLRLMNKLLQKDKETRRRDLHLRPYKVIPTGPKSGLIEVVPNSTTLHEILKEYRKQKGKVLDL- 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205   2447 dfsafqcqkkmMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFLDPA-IWFEKRLAYTRSVATSSIVGYILGLGDRHV 2525
Cdd:smart00146   81 -----------RSQTATRLKKLELFLEATGKFPDPVLYDWFTKKFPDPSeDYFEARKNFTRSCAGYSVITYILGLGDRHN 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205   2526 QNILINEqSAELVHIDLGVAFEQGKILPTP-ETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVL 2604
Cdd:smart00146  150 DNIMLDK-TGHLFHIDFGFILGNGPKLFGFpERVPFRLTPEMVDVMGDSGYFGLFRSLCERALRALRKNSNLIMSLLELM 228

                           250
                    ....*....|..
gi 767970205   2605 LYDPLFDWTMNP 2616
Cdd:smart00146  229 LYDGLPDWRSGK 240
TEL1 COG5032
Phosphatidylinositol kinase or protein kinase, PI-3 family [Signal transduction mechanisms];
2331-2707 1.20e-73

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


Pssm-ID: 227365 [Multi-domain]  Cd Length: 2105  Bit Score: 275.12  E-value: 1.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2331 NLVTIQSFKAEFRLA-GGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKV 2409
Cdd:COG5032  1763 PFVLIERFEPEVSVVkSHLQRPRRLTIRGSDGKLYSFIVKGGDDLRQDELALQLIRLMNKILKKDKETRRRDLWIRPYKV 1842

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2410 VPLSQRSGVLEWCTGTVPIGEFLvnneDGAHKRYRpndFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCME 2489
Cdd:COG5032  1843 IPLSPGSGIIEWVPNSDTLHSIL----REYHKRKN---ISIDQEKKLAARLDNLKLLLKDEFFTKATLKSPPVLYDWFSE 1915

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2490 KFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLG-VAFEQGKILPTPETVPFRLTRDIVD 2568
Cdd:COG5032  1916 SFPNPEDWLTARTNFARSLAVYSVIGYILGLGDRHPGNILIDRSSGHVIHIDFGfILFNAPGRFPFPEKVPFRLTRNIVE 1995

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2569 GMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPlkalylqqrpedetelhptlnaddqeckrnls 2648
Cdd:COG5032  1996 AMGVSGVEGSFRELCETAFRALRKNADSLMNVLELFVRDPLIEWRRLP-------------------------------- 2043

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970205 2649 DIDQSFNKVAERVLMRLQEKLKG--VEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGWKAW 2707
Cdd:COG5032  2044 CFREIQNNEIVNVLERFRLKLSEkdAEKFVDLLINKSVESLITQATDPFQLATMYIGWMPF 2104
PIKKc_TOR cd05169
Catalytic domain of Target of Rapamycin; TOR contains a rapamycin binding domain, a catalytic ...
 2335-2612 1.24e-73

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: 247.78  E-value: 1.24e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2335 IQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDA-VMQqVFQMCNTLLQRNTETRKRKLTICTYKVVPLS 2413
Cdd:cd05169     1 ISSFDPTLEVITSKQRPRKLTIVGSDGKEYKFLLKGHEDLRLDErVMQ-LFGLVNTLLKNDSETSRRNLSIQRYSVIPLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2414 QRSGVLEWctgtvpigeflVNNEDGAH---KRYRPNDFSAFQCQKKMMEVQKKSFE-----EKYEVFMDVCQNFQP--VF 2483
Cdd:cd05169    80 PNSGLIGW-----------VPGCDTLHsliRDYREKRKIPLNIEHRLMLQMAPDYDnltliQKVEVFEYALENTPGddLR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2484 RYFCMeKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPT-PETVPFRL 2562
Cdd:cd05169   149 RVLWL-KSPSSEAWLERRTNFTRSLAVMSMVGYILGLGDRHPSNIMLDRLTGKVIHIDFGDCFEVAMHREKfPEKVPFRL 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767970205 2563 TRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDW 2612
Cdd:cd05169   228 TRMLVNAMEVSGVEGTFRSTCEDVMRVLRENKDSLMAVLEAFVHDPLISW 277
PIKKc_SMG1 cd05170
Catalytic domain of Suppressor of Morphogenetic effect on Genitalia-1; SMG-1 plays a critical ...
 2351-2613 5.85e-69

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: 235.23  E-value: 5.85e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2351 PKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIge 2430
Cdd:cd05170    17 PKKLVFLGSDGKRYPYLFKGLEDLHLDERIMQFLSIVNAMLASDNEHRRRRYRARHYSVTPLGPRSGLIQWVDGATPL-- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2431 FLV--------------NNEDGA-------------HKRYRP----NDFSAFQCQKKM-MEVQKKSFEE-KYEVFMDVCQ 2477
Cdd:cd05170    95 FSLykrwqqrraaaqaqKNQDSGstpppvprpselfYNKLKPalkaAGIRKSTSRREWpLEVLRQVLEElVAETPRDLLA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2478 NfqpvfRYFCMEkfLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPET 2557
Cdd:cd05170   175 R-----ELWCSS--PSSAEWWRVTQRFARSLAVMSMIGYIIGLGDRHLDNILVDLSTGEVVHIDYNVCFEKGKRLRVPEK 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767970205 2558 VPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWT 2613
Cdd:cd05170   248 VPFRLTQNIEHALGPTGVEGTFRLSCEQVLKILRKGRETLLTLLEAFVYDPLVDWT 303
PIKKc_DNA-PK cd05172
Catalytic domain of DNA-dependent protein kinase; DNA-PK is comprised of a regulatory subunit, ...
 2351-2612 2.97e-61

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: 210.51  E-value: 2.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2351 PKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGE 2430
Cdd:cd05172    17 PKRITIRGSDEKEYKFLVKGGEDLRQDQRIQQLFDVMNNILASDPACRQRRLRIRTYQVIPMTSRLGLIEWVDNTTPLKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2431 FLVNNedgahkryrpndfsafqcqkkmmevqkksfeekyevfmdvcqnfqpVFRYFCMEKFLDPAIWFEKRLAYTRSVAT 2510
Cdd:cd05172    97 ILEND----------------------------------------------LLRRALLSLASSPEAFLALRSNFARSLAA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2511 SSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQG-KILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEV 2589
Cdd:cd05172   131 MSICGYILGIGDRHLSNFLVDLSTGRLIGIDFGHAFGSAtQFLPIPELVPFRLTRQLLNLLQPLDARGLLRSDMVHVLRA 210

                         250       260
                  ....*....|....*....|...
gi 767970205 2590 MRNSQETLLTIVEVLLYDPLFDW 2612
Cdd:cd05172   211 LRAGRDLLLATMDVFVKEPLLDW 233
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 2367-2614 5.59e-58

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: 201.40  E-value: 5.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  2367 LVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRkltICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDgahKRYRPN 2446
Cdd:pfam00454    5 IYKVGDDLRQDELILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGE---NGVPPT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  2447 DFSAFQCQKKMMEVQKKSFEEKYEVFMDVcqnfqPVFRYFcMEKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQ 2526
Cdd:pfam00454   79 AMVKILHSALNYPKLKLEFESRISLPPKV-----GLLQWF-VKKSPDAEEWGEARKNFVRSCAGYSVLDYILGNGDRHLD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  2527 NILINEQSAELVHIDLGVAF-EQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLL 2605
Cdd:pfam00454  153 NILVDKTTGKLFHIDFGLCLpDAGKDLPFPEKVPFRLTREMVYAMGPSGDEGLFRELCETAYEALRRNLNLLTNLLKLMV 232


                   ....*....
gi 767970205  2606 YDPLFDWTM 2614
Cdd:pfam00454  233 ADGLPDWSI 241
FAT pfam02259
FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.
 1749-2141 7.91e-57

FAT domain; The FAT domain is named after FRAP, ATM and TRRAP.


Pssm-ID: 396714 [Multi-domain]  Cd Length: 342  Bit Score: 201.81  E-value: 7.91e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1749 ELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEVEEMCKRSLESVYSLYPTLSRL 1828
Cdd:pfam02259    2 PLAAEAAWRLGQWDLMREYLSLMKKDSPDKAFFEAILALHRNQFDEAERYIEKARQLLDTELSALSGESYNRAYPLLVRL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1829 QAIGELESIGELFSRSV-THRQLSEVYIKWQKHSQLLKDsDFSFQEPIMALRTVILEILMEKEMDnsqrecikDILTKHL 1907
Cdd:pfam02259   82 QQLAELEEIIQYKQKLGqSSEELKSLLQTWRNRLPGCQD-DVEIWQDILTVRSLVLSPIEDVYLG--------GYHAEMW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1908 VELSILARTFKNTQLPERAIFQIKQYNSVSCGVsEWQLEEAQVFWAKKEQSLALSILKQMIKKldasCAANNPSLKLTYT 1987
Cdd:pfam02259  153 LKFANLARKSGRFSLAEKALLKLLGEDPEEWLP-EVVYAYAKYLWPTGEQQEALLKLREFLSC----YLQKNGELLSGLE 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205  1988 EClrvcgnwLAETCLENPAVIMQTYLEKAVEVAGNYDGESSdELRNGKMKAFLSLARFSDTQYQrIENYMKSSEFENKQA 2067
Cdd:pfam02259  228 VI-------NPTNLEEFTELLARCYLLKGKWQAALGQNWAE-EKSEEILQAYLLATQFDPSWYK-AWHTWALFNFEVLRK 298

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767970205  2068 LLKRAKEEVgllrehkiqtnrytvkvqreleldelalralKEDRKRFLCKAVENYINCLLSGEEHDM-WVFRLCS 2141
Cdd:pfam02259  299 EEQGKEEEG-------------------------------PEDLSRYVVPAVEGYLRSLSLSSENSLqDTLRLLT 342
PI3Kc_like cd00142
Catalytic domain of Phosphoinositide 3-kinase and similar proteins; Members of the family ...
 2351-2607 1.67e-35

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


Pssm-ID: 270621 [Multi-domain]  Cd Length: 216  Bit Score: 135.54  E-value: 1.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2351 PKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLqrntETRKRKLTICTYKVVPLSQRSGVLEWctgtVPIGE 2430
Cdd:cd00142    17 PKKITLIGADGKTYSFLLKRRDDLRKDERSFQFMRLIQSIL----EKESVNLVLPPYKVIPLSENSGLIEI----VKDAQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2431 FLvnnedgahkryrpndfsafqcqkkmmEVQKKSFEEK---YEVFMDVCQNFqpvfryfcmekfldpaiwfekrlayTRS 2507
Cdd:cd00142    89 TI--------------------------EDLLKSLWRKspsSQSWLNRRENF-------------------------SCS 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2508 VATSSIVGYILGLGDRHVQNILINEqSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTM 2587
Cdd:cd00142   118 LAGYSVLGYIFGIGDRHPSNIMIEP-SGNIFHIDFGFIFSGRKLAEGVETVPFRLTPMLENAMGTAGVNGPFQISMVKIM 196

                         250       260
                  ....*....|....*....|
gi 767970205 2588 EVMRNSQETLLTIVEVLLYD 2607
Cdd:cd00142   197 EILREHADLIVPILEHSLRD 216
PI3Kc_III cd00896
Catalytic domain of Class III Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2351-2584 2.73e-22

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: 101.07  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2351 PKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNtetrKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGE 2430
Cdd:cd00896    80 PLKLTFKTLDGGEYKVIFKHGDDLRQDQLVLQIITLMDRLLKKE----NLDLKLTPYKVLATSPNDGLVEFVPNSKALAD 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2431 FLvnnedgahKRYrpNDFSAFqcqkkmMEVQKKSFEEKYEVFMDVCQNfqpvfryfcmekfldpaiwfekrlaYTRSVAT 2510
Cdd:cd00896   156 IL--------KKY--GSILNF------LRKHNPDESGPYGIKPEVMDN-------------------------FVKSCAG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2511 SSIVGYILGLGDRHVQNILINEqSAELVHIDLGvaFeqgkIL---PTPETVPFRLTRDIVDGMGITGVEG--VFRR-CCE 2584
Cdd:cd00896   195 YCVITYILGVGDRHLDNLLLTK-DGHLFHIDFG--Y----ILgrdPKPFPPPMKLCKEMVEAMGGANSEGykEFKKyCCT 267
PIKK_TRRAP cd05163
Pseudokinase domain of TRansformation/tRanscription domain-Associated Protein; TRRAP belongs ...
 2358-2579 1.51e-15

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: 79.10  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2358 GSDGKERRQLVK---GRDDLRQDAVMQQvFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLvn 2434
Cdd:cd05163    25 GHDGSKYPFLVQtpsARHSRREERVMQL-FRLLNRVLERKKETRRRNLQFHVPIVVPLSPQVRLVEDDPSYISLQDIY-- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2435 nedgahkryrpndfsafqcqkkmmevqkksfeEKYEVFMDVCQNFQP---VFRYFcMEKFLDP-AIW-FEKRLayTRSVA 2509
Cdd:cd05163   102 --------------------------------EKLEILNEIQSKMVPetiLSNYF-LRTMPSPsDLWlFRKQF--TLQLA 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970205 2510 TSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKIL-PTPETVPFRLTRDIVDGMGITGVEGVF 2579
Cdd:cd05163   147 LSSFMTYVLSLGNRTPHRILISRSTGNVFMTDFLPSINSQGPLlDNNEPVPFRLTPNIQHFIGPIGVEGLL 217
PI4Kc_III_beta cd05168
Catalytic domain of Type III Phosphoinositide 4-kinase beta; PI4Ks catalyze the transfer of ...
 2368-2655 2.03e-15

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: 79.45  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2368 VKGRDDLRQDAVMQQVFQmcntLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIgeflvnneDGAHKRYrPND 2447
Cdd:cd05168    35 VKSGDDLRQELLAMQLIK----QFQRIFEEAGLPLWLRPYEILVTSSDSGLIETIPDTVSI--------DSLKKRF-PNF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2448 FSAFQCqkkmmevqkksFEEKY-----EVFMDVCQNFqpvfryfcmekfldpaiwfekrlayTRSVATSSIVGYILGLGD 2522
Cdd:cd05168   102 TSLLDY-----------FERTFgdpnsERFKEAQRNF-------------------------VESLAAYSLVCYLLQIKD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2523 RHVQNILINEQsAELVHIDLG---------VAFeqgkilptpETVPFRLTRDIVDGMGitGVEG----VFRRCCEKTMEV 2589
Cdd:cd05168   146 RHNGNILLDSE-GHIIHIDFGfmlsnspggLGF---------ETAPFKLTQEYVEVMG--GLESdmfrYFKTLMIQGFLA 213

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970205 2590 MRNSQETLLTIVEVLLYD----PLFDWTMNPLKAlyLQQRpedeteLHPTLNadDQECKRN-LSDIDQSFN 2655
Cdd:cd05168   214 LRKHADRIVLLVEIMQQGsklpCFFGGGEFTIEQ--LRER------FKLNLT--EEECAQFvDSLIDKSLN 274
PI4Kc_III cd00893
Catalytic domain of Type III Phosphoinositide 4-kinase; PI4Ks catalyze the transfer of the ...
 2368-2655 2.54e-14

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: 76.15  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2368 VKGRDDLRQDA-------VMQQVFQMCNTllqrntetrkrKLTICTYKVVPLSQRSGVLEWCtgtvpigeflvnnedgah 2440
Cdd:cd00893    32 VKTGDDLKQEQlalqlisQFDQIFKEEGL-----------PLWLRPYEILSLGPDSGIIEMI------------------ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2441 kryrPNDFSAFQCQKKMMEVQKKS-----FEEKYEVfmdvcQNFQPVFRYFCmekfldpaiwfekrlaytRSVATSSIVG 2515
Cdd:cd00893    83 ----KNAVSIDSLKKKLDSFNKFVslsdfFDDNFGD-----EAIQKARDNFL------------------QSLVAYSLVC 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2516 YILGLGDRHVQNILINEQsAELVHIDLGVAFEQgkilpTP-----ETVPFRLTRDIVDGMGITGVE--GVFRRCCEKTME 2588
Cdd:cd00893   136 YFLQIKDRHNGNILLDKE-GHIIHIDFGFFLSS-----HPgfygfEGAPFKLSSEYIEVLGGVDSElfKEFRKLFLKGFM 209

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767970205 2589 VMRNSQETLLTIVEvLLYDPLFDWTMNPLKALYLQQRpedeteLHPTLNadDQECKRNLSD-IDQSFN 2655
Cdd:cd00893   210 ALRKHSDKILSLVE-MMYSGHGITCFGKKTIQQLKQR------FNPELT--EGELEVYVLSlINKSLD 268
PI4Kc_III_alpha cd05167
Catalytic domain of Type III Phosphoinositide 4-kinase alpha; PI4Ks catalyze the transfer of ...
 2338-2606 9.93e-12

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: 68.77  E-value: 9.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2338 FKAEFRLA-GGVNLPKIIDCVGSDGKERRQ--LVKGRDDLRQD-------AVMQQVFQMCNTllqrntetrkrKLTICTY 2407
Cdd:cd05167    21 FLVTFKVKdCGVDELEHEGTESEATKEVWQaaIFKVGDDCRQDmlalqliSLFKNIFEEVGL-----------DLYLFPY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2408 KVVPLSQRSGVLEwctgtvpigefLVNNEDGAHKRYRPNDFSAFQcqkkmmevqkkSFEEKYEVFMDVcqNFQpvfryfc 2487
Cdd:cd05167    90 RVVATGPGCGVIE-----------VIPNSKSRDQIGRETDNGLYE-----------YFLSKYGDESTP--AFQ------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2488 mekfldpaiwfEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQsAELVHIDLGVAFEQ--GKILPTpETVPFRLTRD 2565
Cdd:cd05167   139 -----------KARRNFIKSMAGYSLVSYLLQIKDRHNGNIMIDDD-GHIIHIDFGFIFEIspGGNLGF-ESAPFKLTKE 205

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 767970205 2566 IVDGMGITGVEGVFRRCCEKTMEVM---RNSQETLLTIVEVLLY 2606
Cdd:cd05167   206 MVDLMGGSMESEPFKWFVELCVRGYlavRPYAEAIVSLVELMLD 249
PI3Kc_IA_delta cd05174
Catalytic domain of Class IA Phosphoinositide 3-kinase delta; PI3Ks catalyze the transfer of ...
 2338-2591 1.28e-10

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: 65.84  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2338 FKAEFRLAGGVNLpkiidcvgsdgkerrqLVKGRDDLRQDAVMQQVFQMCNTLLQrnteTRKRKLTICTYKVVPLSQRSG 2417
Cdd:cd05174    88 YSSEEAGAGNVGI----------------IFKNGDDLRQDMLTLQMIQLMDVLWK----QEGLDLRMTPYGCLSTGDKTG 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2418 VLEWCTGTVPIGEFLVNNEDGAHKryrpndfSAFQCQKKMMEVQKKSFEEKyevfmdvcqnfqpvfryfcmekfLDPAIw 2497
Cdd:cd05174   148 LIEVVLHSDTIANIQLNKSNMAAT-------AAFNKDALLNWLKSKNPGDA-----------------------LDQAI- 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2498 fEKrlaYTRSVATSSIVGYILGLGDRHVQNILINEqSAELVHIDLG--VAFEQGKILPTPETVPFRLTRDIVDGM--GIT 2573
Cdd:cd05174   197 -EE---FTLSCAGYCVATYVLGIGDRHSDNIMIRE-SGQLFHIDFGhfLGNFKTKFGINRERVPFILTYDFVHVIqqGKT 271

                         250       260
                  ....*....|....*....|.
gi 767970205 2574 GVEGVFRR---CCEKTMEVMR 2591
Cdd:cd05174   272 NNSEKFERfrgYCERAYTILR 292
FATC pfam02260
FATC domain; The FATC domain is named after FRAP, ATM, TRRAP C-terminal. The solution ...
 2678-2707 2.74e-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: 57.01  E-value: 2.74e-10
                           10        20        30
                   ....*....|....*....|....*....|
gi 767970205  2678 LSVGGQVNLLIQQAIDPKNLSRLFPGWKAW 2707
Cdd:pfam02260    2 LSVEGQVDELIQEATDPENLAQMYIGWCPW 31
PI3Kc_IA_beta cd05173
Catalytic domain of Class IA Phosphoinositide 3-kinase beta; PI3Ks catalyze the transfer of ...
 2367-2605 3.95e-09

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: 61.13  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2367 LVKGRDDLRQDAVMQQVFQMCNTLLQRntetRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKryrpn 2446
Cdd:cd05173    98 IFKNGDDLRQDMLTLQILRLMDTLWKE----AGLDLRIVPYGCLATGDRSGLIEVVSSAETIADIQLNSSNVAAA----- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2447 dfSAFQcqkkmmevqkksfeekyevfMDVCQNFqpvFRYFCMEKFLDPAIWfekrlAYTRSVATSSIVGYILGLGDRHVQ 2526
Cdd:cd05173   169 --AAFN--------------------KDALLNW---LKEYNSGDDLERAIE-----EFTLSCAGYCVATYVLGIGDRHSD 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2527 NILInEQSAELVHIDLG--VAFEQGKILPTPETVPFRLTRDIVDGM--GITGVE---GVFRRCCEKTMEVMRNSQETLLT 2599
Cdd:cd05173   219 NIMV-RKNGQLFHIDFGhiLGNFKSKFGIKRERVPFILTYDFIHVIqqGKTGNTekfGRFRQYCEDAYLILRKNGNLFIT 297


                  ....*.
gi 767970205 2600 IVEVLL 2605
Cdd:cd05173   298 LFALML 303
PI3Kc_II cd05166
Catalytic domain of Class II Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2372-2628 6.57e-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: 54.22  E-value: 6.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2372 DDLRQDA-VMQQVFQMCNTLLQRNTEtrkrkLTICTYKVVPLSQRSGVLEwctgtvpigefLVNNedgahkryrpndfsa 2450
Cdd:cd05166    99 DDLRQDMlTLQLIRIMDKIWLQEGLD-----LKMITFRCVPTGNKRGMVE-----------LVPE--------------- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2451 fqcQKKMMEVQKK-----SFEEKyeVFMDVCQNFQPvfryfcmekflDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHV 2525
Cdd:cd05166   148 ---AETLREIQTEhgltgSFKDR--PLADWLQKHNP-----------SELEYEKAVENFIRSCAGYCVATYVLGICDRHN 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2526 QNILInEQSAELVHIDLgvafeqGKILPTPET--------VPFRLTRD----IVDGMGITGVEGVFRRCCEKTMEVMRNS 2593
Cdd:cd05166   212 DNIML-KTSGHLFHIDF------GKFLGDAQMfgnfkrdrVPFVLTSDmayvINGGDKPSSRFQLFVDLCCQAFNIIRKN 284

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767970205 2594 QETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPED 2628
Cdd:cd05166   285 SNLLLNLLSLMLSSGIPGVTQDDLRYVQDALLPEL 319
PI3Kc_I cd05165
Catalytic domain of Class I Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2504-2591 2.50e-06

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


Pssm-ID: 270709 [Multi-domain]  Cd Length: 363  Bit Score: 52.25  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2504 YTRSVATSSIVGYILGLGDRHVQNILINEqSAELVHIDLgvafeqGKILP--------TPETVPFRLTRD----IVDGMG 2571
Cdd:cd05165   197 FTLSCAGYCVATYVLGIGDRHSDNIMVKE-NGQLFHIDF------GHFLGnfkkkfgiKRERVPFVLTHDfvyvIARGQD 269

                          90       100
                  ....*....|....*....|..
gi 767970205 2572 ITGVEGV--FRRCCEKTMEVMR 2591
Cdd:cd05165   270 NTKSEEFqeFQELCEKAYLILR 291
PI3Kc cd00891
Catalytic domain of Phosphoinositide 3-kinase; PI3Ks catalyze the transfer of the ...
 2372-2600 3.28e-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: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2372 DDLRQDAVMQQVFQMCNTLLQRntETRKRKLTIctYKVVPLSQRSGVLEWCTGTVPIGEFlvnnedgaHKRYRPNdFSAF 2451
Cdd:cd00891    96 DDLRQDQLTLQLLRIMDKLWKK--EGLDLRMTP--YKCIATGDEVGMIEVVPNSETTAAI--------QKKYGGF-GAAF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2452 qcqkkmmevqkksfeeKYEVFMDvcqnfqpvfryFCMEKFLDPAIWFEKRLAYTRS-----VATssivgYILGLGDRHVQ 2526
Cdd:cd00891   163 ----------------KDTPISN-----------WLKKHNPTEEEYEEAVENFIRScagycVAT-----YVLGIGDRHND 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2527 NILINeQSAELVHIDlgvaFeqGKIL---PTP-----ETVPFRLTRDIVDGMGitGVEGV----FRRCCEKTMEVMRNSQ 2594
Cdd:cd00891   211 NIMVT-KSGHLFHID----F--GHFLgnfKKKfgikrERAPFVFTPEMAYVMG--GEDSEnfqkFEDLCCKAYNILRKHG 281


                  ....*.
gi 767970205 2595 ETLLTI 2600
Cdd:cd00891   282 NLLINL 287
PI3Kc_IB_gamma cd00894
Catalytic domain of Class IB Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 2504-2633 1.34e-05

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: 50.25  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2504 YTRSVATSSIVGYILGLGDRHVQNILINEQsAELVHIDLGVAFEQGKIL--PTPETVPFRLTRDIVDGMGITGVEGV--- 2578
Cdd:cd00894   200 FVYSCAGYCVATFVLGIGDRHNDNIMITET-GNLFHIDFGHILGNYKSFlgINKERVPFVLTPDFLFVMGTSGKKTSlhf 278

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767970205 2579 --FRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNP----LKALYLQQRPEDETELH 2633
Cdd:cd00894   279 qkFQDVCVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEdieyIRDALTVGKSEEDAKKH 339
PI3Kc_IA_alpha cd05175
Catalytic domain of Class IA Phosphoinositide 3-kinase alpha; PI3Ks catalyze the transfer of ...
 2504-2567 3.92e-04

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


Pssm-ID: 270719 [Multi-domain]  Cd Length: 370  Bit Score: 45.43  E-value: 3.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767970205 2504 YTRSVATSSIVGYILGLGDRHVQNILINEqSAELVHIDLG--VAFEQGKILPTPETVPFRLTRDIV 2567
Cdd:cd05175   203 FTRSCAGYCVATFILGIGDRHNSNIMVKD-DGQLFHIDFGhfLDHKKKKFGYKRERVPFVLTQDFL 267
PI3Kc_C2_gamma cd05177
Catalytic domain of Class II Phosphoinositide 3-kinase gamma; PI3Ks catalyze the transfer of ...
 2356-2635 4.28e-03

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


Pssm-ID: 270721 [Multi-domain]  Cd Length: 354  Bit Score: 42.19  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2356 CVGSDGKERRQLVKGRDDLRQDAVMQQVFQ-MCNTLLQRNTEtrkrkLTICTYKVVPLSQRSGVLEWCTGTVPIGEflVN 2434
Cdd:cd05177    84 NANPLAKNISIIFKTGDDLRQDMLVLQIVRvMDNIWLQEGLD-----MQMIIYRCLSTGKTQGLVQMVPDAVTLAK--IH 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2435 NEDGAHKRYRPNDFSA-FQCQKKMmevqKKSFEEKYEVFMDVCqnfqpvfryfcmekfldpAIWfekrlaytrsvatsSI 2513
Cdd:cd05177   157 RESGLIGPLKENTIEKwFHMHNKL----KEDYDKAVRNFFHSC------------------AGW--------------CV 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767970205 2514 VGYILGLGDRHVQNILINeQSAELVHIDLgvafeqGKILPTPET--------VPFRLTRDIV-----DGMGITGVEGVFR 2580
Cdd:cd05177   201 VTFILGVCDRHNDNIMLT-HSGHMFHIDF------GKFLGHAQTfgsikrdrAPFIFTSEMEyfiteGGKKPQRFQRFVE 273

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767970205 2581 RCCEkTMEVMRNSQETLLTIVEVLLYDPLFDWT-MNPLKALYLQQRPEDeTELHPT 2635
Cdd:cd05177   274 LCCR-AYNIVRKHSQLLLNLLEMMLHAGLPELKdIQDLKYVYNNLRPQD-TDLEAT 327
 
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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