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Conserved domains on  [gi|767980329|ref|XP_011534968|]
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centrosomal protein of 170 kDa protein B isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
 842-1525 0e+00

CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa (CEP170).


:

Pssm-ID: 464633  Cd Length: 682  Bit Score: 1000.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   842 GRMVIQL-RPGRSPEPDGPAPA--FLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDfHSQDTHLILKETE 918
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASSksFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLILKETE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   919 TALAALEARLLSNSVDAECEGgSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQP--LRAQKEMSPSPPAAQDPG 996
Cdd:pfam15308   80 TALAALEAKLLSESKGDEGEG-SPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSPSAQDKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   997 GTAlvSAREQSSERQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASNHETPEatgagRL 1076
Cdd:pfam15308  159 SQP--SARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYS-----RP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1077 GSRRKPAAPPPSPAAREEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRP 1156
Cdd:pfam15308  232 SSRRKPFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1157 AAEQAKKLSRLDILAMPRKRAGSFTGTSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSR 1236
Cdd:pfam15308  312 PPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKTARTRANSISKQPFSR 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1237 ARSGSARY--TSNTRRRQQGSDYTSTSEEEYGSRHGSPKHTRSHTSTATQTPRAGSSSRARSRAPGPRDTDDDEEEPDPY 1314
Cdd:pfam15308  392 TRSSSAKYssSSNSRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPGHRETEEEEYQPDPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1315 GFIVQTAEIAEIARLSQTLVKDVAILAQEIHDVAGDGDTLGSSEPAHSASLSNMPSTPASTISAREELVQRIPEASLNFQ 1394
Cdd:pfam15308  472 PFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1395 KVPPGSLNSRDFDQNMNDSCEDALANKTRPRNREEVIFDNLMLNPVSQLSQAIRENTEHLAEKMKILFQNTGRAWEDLEA 1474
Cdd:pfam15308  552 KVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNKDRNWEEIEA 631

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767980329  1475 RINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGSLDLLTGN 1525
Cdd:pfam15308  632 KINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
 1-106 1.17e-74

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


:

Pssm-ID: 438777 [Multi-domain]  Cd Length: 106  Bit Score: 242.91  E-value: 1.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    1 MSATSWFLVSSSGARHRLPRELIFVGREECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVT 80
Cdd:cd22725     1 MSVTSWFLVSSSGTRHRLPREMIFVGREDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYIT 80

                          90       100
                  ....*....|....*....|....*.
gi 767980329   81 LKLNDVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22725    81 LKLNDVIRFGYDSNMYVLERSQHKVP 106
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 343-862 4.52e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  343 PVHTRTLKG-HKHEDGTQSDSEDPLAKAASAAgvPLEASGEQVRLQRQIKRDPQELLHNQQAfvieffDEDTPRKKRSQS 421
Cdd:PHA03247 2528 PVHPRMLTWiRGLEELASDDAGDPPPPLPPAA--PPAAPDRSVPPPRPAPRPSEPAVTSRAR------RPDAPPQSARPR 2599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  422 FTHSPSGDPKADKRRGPTPADRDRPSVPAPVQA--------GGRSSGPQRA--------GSLKREKTEERLGSPSPASRT 485
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSpaanepdpHPPPTVPPPErprddpapGRVSRPRRARRLGRAAQASSP 2679

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  486 PARPfgsvgrRSRLAQDFMAQCLRESSPaarPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLS 565
Cdd:PHA03247 2680 PQRP------RRRAARPTVGSLTSLADP---PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  566 DAGTYTIETEAQDTEVEEARKMIDQVFGVLES-PELSRASSATFRPVIRGDRDESDDGGVAQRMALLQEFASRPLGAAPQ 644
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  645 AEHqglPVPGSPggqkwvsrwaSLADSYSDPGLTEDGLGRRGGepegslPVRmRRRLPQLPSERADSPAGPESSRRSGPG 724
Cdd:PHA03247 2831 PTS---AQPTAP----------PPPPGPPPPSLPLGGSVAPGG------DVR-RRPPSRSPAAKPAAPARPPVRRLARPA 2890

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  725 PPeldseQPSRLFGQEELDPDSLsdasgsdggRGPEPGVEPQDSRRRSPQEGPTwsrgrRSPRAPGEPTPasffigdqng 804
Cdd:PHA03247 2891 VS-----RSTESFALPPDQPERP---------PQPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQP---------- 2941

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767980329  805 davlsrkPLAAPGDGEGLGQTAQPSPPARDGVYVSanGRMVIQLRPGRSPEPDGPAPA 862
Cdd:PHA03247 2942 -------PLAPTTDPAGAGEPSGAVPQPWLGALVP--GRVAVPRFRVPQPAPSREAPA 2990
 
Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
 842-1525 0e+00

CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa (CEP170).


Pssm-ID: 464633  Cd Length: 682  Bit Score: 1000.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   842 GRMVIQL-RPGRSPEPDGPAPA--FLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDfHSQDTHLILKETE 918
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASSksFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLILKETE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   919 TALAALEARLLSNSVDAECEGgSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQP--LRAQKEMSPSPPAAQDPG 996
Cdd:pfam15308   80 TALAALEAKLLSESKGDEGEG-SPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSPSAQDKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   997 GTAlvSAREQSSERQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASNHETPEatgagRL 1076
Cdd:pfam15308  159 SQP--SARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYS-----RP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1077 GSRRKPAAPPPSPAAREEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRP 1156
Cdd:pfam15308  232 SSRRKPFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1157 AAEQAKKLSRLDILAMPRKRAGSFTGTSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSR 1236
Cdd:pfam15308  312 PPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKTARTRANSISKQPFSR 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1237 ARSGSARY--TSNTRRRQQGSDYTSTSEEEYGSRHGSPKHTRSHTSTATQTPRAGSSSRARSRAPGPRDTDDDEEEPDPY 1314
Cdd:pfam15308  392 TRSSSAKYssSSNSRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPGHRETEEEEYQPDPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1315 GFIVQTAEIAEIARLSQTLVKDVAILAQEIHDVAGDGDTLGSSEPAHSASLSNMPSTPASTISAREELVQRIPEASLNFQ 1394
Cdd:pfam15308  472 PFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1395 KVPPGSLNSRDFDQNMNDSCEDALANKTRPRNREEVIFDNLMLNPVSQLSQAIRENTEHLAEKMKILFQNTGRAWEDLEA 1474
Cdd:pfam15308  552 KVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNKDRNWEEIEA 631

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767980329  1475 RINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGSLDLLTGN 1525
Cdd:pfam15308  632 KINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
 1-106 1.17e-74

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438777 [Multi-domain]  Cd Length: 106  Bit Score: 242.91  E-value: 1.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    1 MSATSWFLVSSSGARHRLPRELIFVGREECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVT 80
Cdd:cd22725     1 MSVTSWFLVSSSGTRHRLPREMIFVGREDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYIT 80

                          90       100
                  ....*....|....*....|....*.
gi 767980329   81 LKLNDVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22725    81 LKLNDVIRFGYDSNMYVLERSQHKVP 106
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
13-90 1.01e-17

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 79.62  E-value: 1.01e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980329   13 GARHRLPRELIFVGR-EECELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDVIRFG 90
Cdd:COG1716    13 GRRFPLDGGPLTIGRaPDNDIVLDDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRV--TEPAPLRDGDVIRLG 87
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 23-89 3.78e-14

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 68.37  E-value: 3.78e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767980329    23 IFVGRE-ECELMLQSRSVDKQHAVINYDQDRdEHWVKDLGSLNGTFVNDMRIPdQKYVTLKLNDVIRF 89
Cdd:pfam00498    1 VTIGRSpDCDIVLDDPSVSRRHAEIRYDGGG-RFYLEDLGSTNGTFVNGQRLG-PEPVRLKDGDVIRL 66
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 23-73 1.64e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 52.18  E-value: 1.64e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767980329     23 IFVGREE--CELMLQSRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDMRI 73
Cdd:smart00240    1 VTIGRSSedCDIQLDGPSISRRHAVIVYDGG-GRFYLIDLGSTNGTFVNGKRI 52
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 626-1057 6.71e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.84  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  626 QRMALLQEFASRPLGAAPQA-EHQGLPvPGSPG------GQKWVSRWASLADSYSDPGLTEDG-LGRRGGEPE----GSL 693
Cdd:PTZ00449  494 KKLAPIEEEDSDKHDEPPEGpEASGLP-PKAPGdkegeeGEHEDSKESDEPKEGGKPGETKEGeVGKKPGPAKehkpSKI 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  694 PVRMRRrlPQLPsERADSPAGPESSRRS-GPGPPELDSEQPSRLFGQEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRS 772
Cdd:PTZ00449  573 PTLSKK--PEFP-KDPKHPKDPEEPKKPkRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPE 649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  773 PQEGPTWSRGRRSPRAPGEPTPASFFIGDQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVYVSANgRMVIQLRPgR 852
Cdd:PTZ00449  650 GPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP-RPLPPKLP-R 727

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  853 SP--------EPDGPAPA----FLRQES---FTKEPASGPPAPG------KPPHISSHPLLQDLAATRAARMDFHSqDTH 911
Cdd:PTZ00449  728 DEefpfepigDPDAEQPDdiefFTPPEEertFFHETPADTPLPDilaeefKEEDIHAETGEPDEAMKRPDSPSEHE-DKP 806

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  912 LILKETETALAALEARLLSNSVDAECEGGSTPRPPedalsgdsdvdTASTVSLRSGKSGPSPTTpqpLRAQKEMSPSPPA 991
Cdd:PTZ00449  807 PGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDA-----------SGKIVKLKRSKSFDDLTT---VEEAEEMGAEARK 872

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767980329  992 -AQDPGGTalvsareQSSERQHHPlgPTDMGRGEPVRRSAIRRGHRPRGSLDwPSEERGPVLAHLPS 1057
Cdd:PTZ00449  873 iVVDDDGT-------EADDEDTHP--PEEKHKSEVRRRRPPKKPSKPKKPSK-PKKPKKPDSAFIPS 929
PHA03247 PHA03247
large tegument protein UL36; Provisional
 343-862 4.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  343 PVHTRTLKG-HKHEDGTQSDSEDPLAKAASAAgvPLEASGEQVRLQRQIKRDPQELLHNQQAfvieffDEDTPRKKRSQS 421
Cdd:PHA03247 2528 PVHPRMLTWiRGLEELASDDAGDPPPPLPPAA--PPAAPDRSVPPPRPAPRPSEPAVTSRAR------RPDAPPQSARPR 2599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  422 FTHSPSGDPKADKRRGPTPADRDRPSVPAPVQA--------GGRSSGPQRA--------GSLKREKTEERLGSPSPASRT 485
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSpaanepdpHPPPTVPPPErprddpapGRVSRPRRARRLGRAAQASSP 2679

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  486 PARPfgsvgrRSRLAQDFMAQCLRESSPaarPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLS 565
Cdd:PHA03247 2680 PQRP------RRRAARPTVGSLTSLADP---PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  566 DAGTYTIETEAQDTEVEEARKMIDQVFGVLES-PELSRASSATFRPVIRGDRDESDDGGVAQRMALLQEFASRPLGAAPQ 644
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  645 AEHqglPVPGSPggqkwvsrwaSLADSYSDPGLTEDGLGRRGGepegslPVRmRRRLPQLPSERADSPAGPESSRRSGPG 724
Cdd:PHA03247 2831 PTS---AQPTAP----------PPPPGPPPPSLPLGGSVAPGG------DVR-RRPPSRSPAAKPAAPARPPVRRLARPA 2890

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  725 PPeldseQPSRLFGQEELDPDSLsdasgsdggRGPEPGVEPQDSRRRSPQEGPTwsrgrRSPRAPGEPTPasffigdqng 804
Cdd:PHA03247 2891 VS-----RSTESFALPPDQPERP---------PQPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQP---------- 2941

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767980329  805 davlsrkPLAAPGDGEGLGQTAQPSPPARDGVYVSanGRMVIQLRPGRSPEPDGPAPA 862
Cdd:PHA03247 2942 -------PLAPTTDPAGAGEPSGAVPQPWLGALVP--GRVAVPRFRVPQPAPSREAPA 2990
 
Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
 842-1525 0e+00

CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa (CEP170).


Pssm-ID: 464633  Cd Length: 682  Bit Score: 1000.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   842 GRMVIQL-RPGRSPEPDGPAPA--FLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDfHSQDTHLILKETE 918
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASSksFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLILKETE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   919 TALAALEARLLSNSVDAECEGgSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQP--LRAQKEMSPSPPAAQDPG 996
Cdd:pfam15308   80 TALAALEAKLLSESKGDEGEG-SPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSPSAQDKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   997 GTAlvSAREQSSERQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASNHETPEatgagRL 1076
Cdd:pfam15308  159 SQP--SARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYS-----RP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1077 GSRRKPAAPPPSPAAREEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRP 1156
Cdd:pfam15308  232 SSRRKPFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1157 AAEQAKKLSRLDILAMPRKRAGSFTGTSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSR 1236
Cdd:pfam15308  312 PPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKTARTRANSISKQPFSR 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1237 ARSGSARY--TSNTRRRQQGSDYTSTSEEEYGSRHGSPKHTRSHTSTATQTPRAGSSSRARSRAPGPRDTDDDEEEPDPY 1314
Cdd:pfam15308  392 TRSSSAKYssSSNSRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPGHRETEEEEYQPDPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1315 GFIVQTAEIAEIARLSQTLVKDVAILAQEIHDVAGDGDTLGSSEPAHSASLSNMPSTPASTISAREELVQRIPEASLNFQ 1394
Cdd:pfam15308  472 PFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  1395 KVPPGSLNSRDFDQNMNDSCEDALANKTRPRNREEVIFDNLMLNPVSQLSQAIRENTEHLAEKMKILFQNTGRAWEDLEA 1474
Cdd:pfam15308  552 KVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNKDRNWEEIEA 631

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767980329  1475 RINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGSLDLLTGN 1525
Cdd:pfam15308  632 KINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
 1-106 1.17e-74

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438777 [Multi-domain]  Cd Length: 106  Bit Score: 242.91  E-value: 1.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    1 MSATSWFLVSSSGARHRLPRELIFVGREECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVT 80
Cdd:cd22725     1 MSVTSWFLVSSSGTRHRLPREMIFVGREDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYIT 80

                          90       100
                  ....*....|....*....|....*.
gi 767980329   81 LKLNDVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22725    81 LKLNDVIRFGYDSNMYVLERSQHKVP 106
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
 5-106 7.02e-62

forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438756 [Multi-domain]  Cd Length: 102  Bit Score: 206.02  E-value: 7.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    5 SWFLVSSSGARHRLPRELIFVGREECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLN 84
Cdd:cd22704     1 SWCLVSSDGTRHRLPRSMLFVGREDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIPEQTYITLKLG 80

                          90       100
                  ....*....|....*....|..
gi 767980329   85 DVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22704    81 DSIRFGYDTNVYRFEQLSLTTI 102
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
 1-106 5.54e-58

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438776 [Multi-domain]  Cd Length: 106  Bit Score: 195.19  E-value: 5.54e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    1 MSATSWFLVSSSGARHRLPRELIFVGREECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVT 80
Cdd:cd22724     1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYIT 80

                          90       100
                  ....*....|....*....|....*.
gi 767980329   81 LKLNDVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22724    81 LKLDDKLRFGYDTNLFTVVRGEMRVP 106
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
13-90 1.01e-17

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 79.62  E-value: 1.01e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980329   13 GARHRLPRELIFVGR-EECELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDVIRFG 90
Cdd:COG1716    13 GRRFPLDGGPLTIGRaPDNDIVLDDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRV--TEPAPLRDGDVIRLG 87
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 10-90 2.61e-17

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 78.47  E-value: 2.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   10 SSSGARHRLPRELIFVGR-EECELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDVIR 88
Cdd:cd00060     8 DGGGREFPLTKGVVTIGRsPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRI--TPPVPLQDGDVIR 83


                  ..
gi 767980329   89 FG 90
Cdd:cd00060    84 LG 85
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
 25-99 1.04e-16

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 76.91  E-value: 1.04e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980329   25 VGREECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDqKYVTLKLNDVIRFGYDSNMYVLE 99
Cdd:cd22700    20 IGREGCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQN-AAVRLAPGDVLRFGFGGLPYELV 93
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
 16-98 2.04e-16

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438728 [Multi-domain]  Cd Length: 111  Bit Score: 76.57  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   16 HRLPRELIfvGREE--CELMLQSRSVDKQHAVINY--DQDRDEHWVK--------DLGSLNGTFVNDMRIPDQKYVTLKL 83
Cdd:cd22676    18 HRQSAYLI--GRDRrvADIPLDHPSCSKQHAVIQFreVEKRNEGDVIenirpyiiDLGSTNGTFLNGEKIEPRRYYELRE 95

                          90
                  ....*....|....*
gi 767980329   84 NDVIRFGYDSNMYVL 98
Cdd:cd22676    96 KDVLKFGLSTREYVL 110
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 25-99 1.55e-15

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438729 [Multi-domain]  Cd Length: 106  Bit Score: 73.74  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   25 VGR-EECELMLQSRSVDKQHAVINYDQDRDEH----WVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLE 99
Cdd:cd22677    26 FGRlPGCDVVLEHPSISRYHAVLQYRGDADDHdggfYLYDLGSTHGTFLNKQRIPPKQYYRLRVGHVLKFGGSTRLYILQ 105
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 23-89 3.78e-14

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 68.37  E-value: 3.78e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767980329    23 IFVGRE-ECELMLQSRSVDKQHAVINYDQDRdEHWVKDLGSLNGTFVNDMRIPdQKYVTLKLNDVIRF 89
Cdd:pfam00498    1 VTIGRSpDCDIVLDDPSVSRRHAEIRYDGGG-RFYLEDLGSTNGTFVNGQRLG-PEPVRLKDGDVIRL 66
FHA_SNIP1 cd22718
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and ...
 16-98 4.30e-12

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex, which associates with both the 3'end of the CCND1 gene and its mRNA. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438770  Cd Length: 149  Bit Score: 65.49  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   16 HRLPRELIFVGREECELMLQSRSVDKQHAVINY---DQDRDEH--------WVKDLGSLNGTFVNDMRIPDQKYVTLKLN 84
Cdd:cd22718    53 HRQSAYLLGRDRKIADIPIDHPSCSKQHAVLQYrlvEYTRPDGtkgrrvrpYIIDLESANGTFLNNKKIEPQRYYELKEK 132

                          90
                  ....*....|....
gi 767980329   85 DVIRFGYDSNMYVL 98
Cdd:cd22718   133 DVLKFGFSSREYVL 146
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
 11-90 6.53e-11

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 60.32  E-value: 6.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   11 SSGARHRLPRELIFVGR-EECELMLQSRSVDKQHAVInyDQDRDEHWVKDLGSLNGTFVN-DMRI-PDQKYvTLKLNDVI 87
Cdd:cd22665    11 GPEKDFPLYEGENVIGRdPSCSVVLPDKSVSKQHACI--EVDGGTHLIEDLGSTNGTRIGnKVRLkPNVRY-ELIDGDLL 87


                  ...
gi 767980329   88 RFG 90
Cdd:cd22665    88 LFG 90
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
 26-98 6.78e-11

forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438726 [Multi-domain]  Cd Length: 108  Bit Score: 60.74  E-value: 6.78e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980329   26 GR--EECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVL 98
Cdd:cd22674    32 GRnsDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEPHKPQQLPIDSTLRFGASTRRYIL 106
FHA_DDL-like cd22719
forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein ...
 21-98 5.40e-10

forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins; DDL, also called protein DAWDLE, is involved in microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438771 [Multi-domain]  Cd Length: 130  Bit Score: 59.04  E-value: 5.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   21 ELIFVGREECELMLQSRSV----------DKQHAVINYDQDRDEH-----------WVKDLGSLNGTFVNDMRIPDQKYV 79
Cdd:cd22719    29 EPLHIHRQSCYLFGRERKVadiptdhpscSKQHAVIQYRLTEKEGgdgmmgkavrpYIMDLGSTNGTFLNGERIEPQRYY 108

                          90
                  ....*....|....*....
gi 767980329   80 TLKLNDVIRFGYDSNMYVL 98
Cdd:cd22719   109 ELLEKDTIKFGNSSREYVL 127
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 18-98 1.17e-09

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 57.43  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   18 LPRELIFVGR-EECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMY 96
Cdd:cd22691    26 EEEDILVVGRhPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVY 105


                  ..
gi 767980329   97 VL 98
Cdd:cd22691   106 RL 107
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
 1-90 1.20e-09

forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438738 [Multi-domain]  Cd Length: 123  Bit Score: 57.68  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    1 MSATSWFLVSSSGARhrlprelifVGRE---ECELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQK 77
Cdd:cd22686    15 LQVGSLFIVTATGAT---------IGREkdhGHTIRIPELGVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPK 85

                          90
                  ....*....|....*..
gi 767980329   78 ----YVTLKLNDVIRFG 90
Cdd:cd22686    86 eksdPYPLTHGDELKIG 102
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
 23-98 2.75e-09

forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438733 [Multi-domain]  Cd Length: 129  Bit Score: 56.68  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   23 IFVGREE--------CELMLQSRSVDKQHAVINYDQDRDE--HWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYD 92
Cdd:cd22681    42 YLIGREKgesteivvADIGIPEETCSKQHCVIQFRNVKGIlkPYIMDLDSSNGTCLNDNVIPSSRYVELRSGDVITFSKS 121


                  ....*.
gi 767980329   93 SNMYVL 98
Cdd:cd22681   122 NDYELV 127
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 12-90 1.05e-08

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 54.19  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    12 SGARHRLPRELIFVGR-EECELMLQSRSVDKQHAVInydQDRDEHW-VKDLGSLNGTFVNDMRIPDQKyVTLKLNDVIRF 89
Cdd:pfam16697    8 AGAEFPLEGGRYRIGSdPDCDIVLSDKEVSRVHLKL---EVDDEGWrLDDLGSGNGTLVNGQRVTELG-IALRPGDRIEL 83


                   .
gi 767980329    90 G 90
Cdd:pfam16697   84 G 84
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 11-90 1.11e-08

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 54.14  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   11 SSGARHRLPRELIFVGR-EECELMLQSRSVDKQHAVINYDqDRDEHWVKDLGSLNGTFVNDMRIPDQkyVTLKLNDVIRF 89
Cdd:cd22673    11 TDGSRFPLTKKSCTFGRdLSCDIRIQLPGVSREHCRIEVD-ENGKAYLENLSTTNPTLVNGKAIEKS--AELKDGDVITI 87


                  .
gi 767980329   90 G 90
Cdd:cd22673    88 G 88
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 23-73 1.64e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 52.18  E-value: 1.64e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 767980329     23 IFVGREE--CELMLQSRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDMRI 73
Cdd:smart00240    1 VTIGRSSedCDIQLDGPSISRRHAVIVYDGG-GRFYLIDLGSTNGTFVNGKRI 52
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 20-97 2.20e-08

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 53.11  E-value: 2.20e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980329   20 RELIFVGRE-ECELMLQSRSVDKQHAVINydQDRDEHWVKDLGSLNGTFVNDMRIPDQKYvTLKLNDVIRFGYDSNMYV 97
Cdd:cd22680    20 FSSVSIGRDpENVIVIPDPFVSRNHARIT--VDSNEIYIEDLGSTNGTFVNDFKRIKGPA-KLHPNDIIKLGRTTVLKV 95
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 6-90 2.75e-08

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 53.52  E-value: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    6 WFL--VSSSGARHRLP---RELIFVGREE----CELMLQSRSVDKQHAVINYDQDRdeHW-VKDLGSLNGTFVNDMRIPD 75
Cdd:cd22663     1 WCLrrVGHGIDPLVLLledGKEVTVGRGLgvtyQLVSTCPLMISRNHCVLKKNDEG--QWtIKDNKSLNGVWVNGERIEP 78

                          90
                  ....*....|....*
gi 767980329   76 QKYVTLKLNDVIRFG 90
Cdd:cd22663    79 LKPYPLNEGDLIQLG 93
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 9-99 4.27e-08

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 52.62  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    9 VSSSGARHRLP---RELIFVGR-EECELMLQSRSVDKQHAVINYDQDRDEH----WVKDLgSLNGTFVNDMRIPDQKYVT 80
Cdd:cd22670     7 SSPGSTDIVLPiykNQVITIGRsPSCDIVINDPFVSRTHCRIYSVQFDESSaplvYVEDL-SSNGTYLNGKLIGRNNTVL 85

                          90
                  ....*....|....*....
gi 767980329   81 LKLNDVIRFGYDSNMYVLE 99
Cdd:cd22670    86 LSDGDVIEIAHSATFVYVH 104
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
 43-114 1.97e-07

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 51.65  E-value: 1.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980329   43 HAVINYDQDRDEHW---VKDLgSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVPEEALKHEK 114
Cdd:cd22685    56 HAEIHAERDGNGNWkvlIEDR-STNGTYVNDVRLQDGQRRELSDGDTITFGHKNGRRVKQWPYQKSSEFYFLFQK 129
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
 20-90 5.68e-07

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 49.03  E-value: 5.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980329   20 RELIFVGRE-ECELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpDQKYVTLKLNDVIRFG 90
Cdd:cd22683    20 RNVTTIGRSrSCDLVLSDPSISRFHAELRLEQNG--INVIDNNSANGTFINGKRI-KGKTYILKNGDIIVFG 88
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
 16-100 1.20e-06

forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438727 [Multi-domain]  Cd Length: 113  Bit Score: 48.71  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   16 HRLPRELIfvGREE-CELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSN 94
Cdd:cd22675    26 DRFPFYLF--GRSPvCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIEKGRPLPLPVGSVIQFGFSAR 103


                  ....*.
gi 767980329   95 MYVLER 100
Cdd:cd22675   104 KYKVRK 109
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 12-90 1.36e-06

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 48.09  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   12 SGARHRLPRELIFVGRE-ECELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIPdqkyvTLKLND--VIR 88
Cdd:cd22694     7 GGELRFDPGSSVRIGRDpDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ-----QVKLSDgtRVR 79


                  ..
gi 767980329   89 FG 90
Cdd:cd22694    80 LG 81
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
 23-97 1.50e-06

forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438730 [Multi-domain]  Cd Length: 102  Bit Score: 48.13  E-value: 1.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980329   23 IFVGR-EECELMLQSRSVDKQHAVINYDQDRdEHW-VKDLGSLNGTFVN--DMRIPDQKYVtLKLNDVIRFGYDSNMYV 97
Cdd:cd22678    25 LTIGRiQRGDIALKDDEVSGKHARIEWNSTG-SKWeLVDLGSLNGTLVNgeSISPNGRPVV-LSSGDVITLGSETKILV 101
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 6-90 3.38e-06

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 47.32  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    6 WFLVSSSGA---RHRLP--RELIfVGREECELMLQ-SRSVDKQHAVI---------NYDQDRDEHWVKDLgSLNGTFVND 70
Cdd:cd22667     1 WWLLSEQDGagtSYYLLpgGEYT-VGRKDCDIIIVdDSSISRKHATLtvlhpeanlSDPDTRPELTLKDL-SKYGTFVNG 78

                          90       100
                  ....*....|....*....|
gi 767980329   71 MRIPDQKYVTLKLNDVIRFG 90
Cdd:cd22667    79 EKLKGGSEVTLKDGDVITFG 98
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
 7-90 3.44e-06

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438750 [Multi-domain]  Cd Length: 93  Bit Score: 47.02  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    7 FLVSSSGARHRLPREL----IFVGREE-CELMLQSRSVDKQHAVINYDQDrdeHW-VKDLGSLNGTFVNDMRIPDqkyVT 80
Cdd:cd22698     3 ILIEQKGSEEGKDYELdqdeFTIGRSSnNDIRLNDHSVSRHHARIVRQGD---KCnLTDLGSTNGTFLNGIRVGT---HE 76

                          90
                  ....*....|
gi 767980329   81 LKLNDVIRFG 90
Cdd:cd22698    77 LKHGDRIQLG 86
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
 12-90 4.88e-06

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 46.61  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   12 SGARHRLPRELIFVGRE-ECELMLQSRSVDKQHAviNYDQDRDEHWVKDLGSLNGTFVNDMRIPDqkyVTLKLNDVIRFG 90
Cdd:cd22684    12 AGARFLLDQDVTTAGRHpESDIFLDDVTVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERIDS---AVLRNGDEVQIG 86
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 13-90 5.02e-06

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 46.14  E-value: 5.02e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980329   13 GARHRLPRELIFVGR-EECELMLQSRSVDKQHAVINYDQDrdEHWVKDLGSLNGTFVNDMRIPDQkyVTLKLNDVIRFG 90
Cdd:cd22693    10 GQTFPIDKSGITIGRaDDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRVTQP--VVVQPGDTIRIG 84
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 23-90 5.86e-06

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 46.37  E-value: 5.86e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767980329   23 IFVGRE-ECELMLQSRSVDKQHA--VINYDQDRdehwVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFG 90
Cdd:cd22682    22 IVIGRSvESQVQIDDDSVSRYHAklAVNPSAVS----IIDLGSTNGTIVNGKKIPKLASCDLQNGDQIKIG 88
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 626-1057 6.71e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.84  E-value: 6.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  626 QRMALLQEFASRPLGAAPQA-EHQGLPvPGSPG------GQKWVSRWASLADSYSDPGLTEDG-LGRRGGEPE----GSL 693
Cdd:PTZ00449  494 KKLAPIEEEDSDKHDEPPEGpEASGLP-PKAPGdkegeeGEHEDSKESDEPKEGGKPGETKEGeVGKKPGPAKehkpSKI 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  694 PVRMRRrlPQLPsERADSPAGPESSRRS-GPGPPELDSEQPSRLFGQEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRS 772
Cdd:PTZ00449  573 PTLSKK--PEFP-KDPKHPKDPEEPKKPkRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPE 649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  773 PQEGPTWSRGRRSPRAPGEPTPASFFIGDQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVYVSANgRMVIQLRPgR 852
Cdd:PTZ00449  650 GPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP-RPLPPKLP-R 727

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  853 SP--------EPDGPAPA----FLRQES---FTKEPASGPPAPG------KPPHISSHPLLQDLAATRAARMDFHSqDTH 911
Cdd:PTZ00449  728 DEefpfepigDPDAEQPDdiefFTPPEEertFFHETPADTPLPDilaeefKEEDIHAETGEPDEAMKRPDSPSEHE-DKP 806

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  912 LILKETETALAALEARLLSNSVDAECEGGSTPRPPedalsgdsdvdTASTVSLRSGKSGPSPTTpqpLRAQKEMSPSPPA 991
Cdd:PTZ00449  807 PGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDA-----------SGKIVKLKRSKSFDDLTT---VEEAEEMGAEARK 872

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767980329  992 -AQDPGGTalvsareQSSERQHHPlgPTDMGRGEPVRRSAIRRGHRPRGSLDwPSEERGPVLAHLPS 1057
Cdd:PTZ00449  873 iVVDDDGT-------EADDEDTHP--PEEKHKSEVRRRRPPKKPSKPKKPSK-PKKPKKPDSAFIPS 929
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 18-94 8.36e-06

second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438742 [Multi-domain]  Cd Length: 105  Bit Score: 46.13  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329   18 LPRELIFVGR-EECELMLQSRSVDKQHAVI---NYDQDRDEHWVKDLgSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDS 93
Cdd:cd22690    16 LTQNTTFIGRsKDCDEEITDPRISKHHCIItrkRSGKGLDDVYVTDT-STNGTFINNNRLGKGSQSLLQDGDEIVLIWDK 94


                  .
gi 767980329   94 N 94
Cdd:cd22690    95 N 95
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
 24-90 9.46e-06

forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438748 [Multi-domain]  Cd Length: 97  Bit Score: 45.56  E-value: 9.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980329   24 FVGREE--CELMLQSRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDMRIPDQKyvTLKLNDVIRFG 90
Cdd:cd22696    24 FIGKDPtvCDIVLQDPSISRQHARLSIDQD-NRVFIEDLSSKNGVLVNGKPIEGKE--EISGSDVISLG 89
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 8-90 4.50e-05

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 47.83  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    8 LVSSSGARHRLPRELIFVGR-EECELMLQ--SRSVDKQHAVINYDqdRDEHWVKDLgSLNGTFVN--DMRIPDQKYVTLK 82
Cdd:COG3456    13 LESGSAASATFGRGGGTIGRsADCDWVLPdpDRSVSRRHAEIRFR--DGAFCLTDL-STNGTFLNgsDHPLGPGRPVRLR 89


                  ....*...
gi 767980329   83 LNDVIRFG 90
Cdd:COG3456    90 DGDRLRIG 97
PHA03247 PHA03247
large tegument protein UL36; Provisional
 343-862 4.52e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  343 PVHTRTLKG-HKHEDGTQSDSEDPLAKAASAAgvPLEASGEQVRLQRQIKRDPQELLHNQQAfvieffDEDTPRKKRSQS 421
Cdd:PHA03247 2528 PVHPRMLTWiRGLEELASDDAGDPPPPLPPAA--PPAAPDRSVPPPRPAPRPSEPAVTSRAR------RPDAPPQSARPR 2599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  422 FTHSPSGDPKADKRRGPTPADRDRPSVPAPVQA--------GGRSSGPQRA--------GSLKREKTEERLGSPSPASRT 485
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSpaanepdpHPPPTVPPPErprddpapGRVSRPRRARRLGRAAQASSP 2679

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  486 PARPfgsvgrRSRLAQDFMAQCLRESSPaarPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLS 565
Cdd:PHA03247 2680 PQRP------RRRAARPTVGSLTSLADP---PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  566 DAGTYTIETEAQDTEVEEARKMIDQVFGVLES-PELSRASSATFRPVIRGDRDESDDGGVAQRMALLQEFASRPLGAAPQ 644
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  645 AEHqglPVPGSPggqkwvsrwaSLADSYSDPGLTEDGLGRRGGepegslPVRmRRRLPQLPSERADSPAGPESSRRSGPG 724
Cdd:PHA03247 2831 PTS---AQPTAP----------PPPPGPPPPSLPLGGSVAPGG------DVR-RRPPSRSPAAKPAAPARPPVRRLARPA 2890

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  725 PPeldseQPSRLFGQEELDPDSLsdasgsdggRGPEPGVEPQDSRRRSPQEGPTwsrgrRSPRAPGEPTPasffigdqng 804
Cdd:PHA03247 2891 VS-----RSTESFALPPDQPERP---------PQPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQP---------- 2941

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767980329  805 davlsrkPLAAPGDGEGLGQTAQPSPPARDGVYVSanGRMVIQLRPGRSPEPDGPAPA 862
Cdd:PHA03247 2942 -------PLAPTTDPAGAGEPSGAVPQPWLGALVP--GRVAVPRFRVPQPAPSREAPA 2990
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 633-1047 5.09e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  633 EFASRPLGAAPQAEHQGLPVPGSPGGQKWVSRWASLADSYSDPGLTEDGLGRRGGEPEGS---LPVRMRRRLPQLPSERA 709
Cdd:PHA03307   15 AEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGpgtEAPANESRSTPTWSLST 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  710 DSPAGPESSRRSGPGPPELDSEQPSrlfgqeelDPDSLSDASGSDGGRGPEPGVEPQDSRRRSPQEGPTWSRGRRSPRAP 789
Cdd:PHA03307   95 LAPASPAREGSPTPPGPSSPDPPPP--------TPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  790 GEPTPASFFIgDQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVyvSANGRMVIQLRPGRSPEPDGPAPAFLRQESF 869
Cdd:PHA03307  167 ASSRQAALPL-SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSP--ISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  870 TKEPASGPPAPGKPPHissHPLLQDLAATRAARMDFHSQDTHLILKETETALAALEARLLSNSVDAECeggSTPRPPEDA 949
Cdd:PHA03307  244 SSGCGWGPENECPLPR---PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA---PSSPRASSS 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  950 LSGDSDVDTASTVSLRSGKSGPSPTTPQPL-RAQKEMSPSPPAAQDPGGTALVSAREQSSERQHHP----------LGPT 1018
Cdd:PHA03307  318 SSSSRESSSSSTSSSSESSRGAAVSPGPSPsRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGrptrrraraaVAGR 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 767980329 1019 DMGRGEPVRRSAIRRGHRP------------RGSLDWPSEE 1047
Cdd:PHA03307  398 ARRRDATGRFPAGRPRPSPldagaasgafyaRYPLLTPSGE 438
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 8-90 7.76e-05

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 42.84  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329    8 LVSSSGARHRLPRELIFVGR-EECELMLQSRSVDKQHAVINYDQDrdEHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDV 86
Cdd:cd22668     5 LDDGSGRVYQLREGSNIIGRgSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPV--TPEWRLADGDV 80


                  ....
gi 767980329   87 IRFG 90
Cdd:cd22668    81 ITLG 84
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 479-882 8.73e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 8.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  479 PSPASRTPARPFGSVGRRSRLAQDFMAQCLRESSPAARPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQ 558
Cdd:PHA03307   61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRP 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  559 EEDDSLSDAGTyTIETEAQDTEVEEARKmidqvfgvlESPELSRASSATFRPVIRGDRDESDDGGVAQRMALlqEFASRP 638
Cdd:PHA03307  141 VGSPGPPPAAS-PPAAGASPAAVASDAA---------SSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAA--SPRPPR 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  639 LGAaPQAEHQGLPVPGSPGGQKW-VSRWASLADSYSDPGLTEDGLGRRGGEPEGSLPVRMRRRLPQLPSERA-----DSP 712
Cdd:PHA03307  209 RSS-PISASASSPAPAPGRSAADdAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSsrpgpASS 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  713 AGPESSRRSGPGPP-ELDSEQPSRLFGQEELDPDSLSD----ASGSDGGRGPEPGVEPQDSRRRSPQEGPTWSRGRRSPR 787
Cdd:PHA03307  288 SSSPRERSPSPSPSsPGSGPAPSSPRASSSSSSSRESSssstSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  788 APGEPTPASFfigdqngdavlsrkPLAAPGDGEGLGQTAQPSPPARDGvyvSANGRMVIQLRPGRSPEPDGPAPAFLRQE 867
Cdd:PHA03307  368 RPRPSRAPSS--------------PAASAGRPTRRRARAAVAGRARRR---DATGRFPAGRPRPSPLDAGAASGAFYARY 430

                         410       420
                  ....*....|....*....|
gi 767980329  868 -----SFTKEPASGPPAPGK 882
Cdd:PHA03307  431 plltpSGEPWPGSPPPPPGR 450
FHA_VPS64-like cd22695
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ...
 36-104 1.10e-04

forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438747 [Multi-domain]  Cd Length: 133  Bit Score: 43.83  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980329   36 SRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKyVTLKLNDVIRFGYDsnmyVLERVQHR 104
Cdd:cd22695    62 SRVLSRNHACLSCDPTTGKVYIRDLKSSNGTFVNGQKIRQND-VELKVGDEVDLGTD----IDSKIEHR 125
PHA03247 PHA03247
large tegument protein UL36; Provisional
 695-1120 1.20e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  695 VRMRRRLPQLPSERAdSPAGPESSRRSGPGPPELDSEQPSrlfgQEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRSPQ 774
Cdd:PHA03247 2582 VTSRARRPDAPPQSA-RPRAPVDDRGDPRGPAPPSPLPPD----THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDP 2656

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  775 EGPTWSRGRRSpRAPGEPTPASffigdqngdAVLSR-KPLAAPGDGEGLGQTAQPSPPARDgvyvsangrmviqlrPGRS 853
Cdd:PHA03247 2657 APGRVSRPRRA-RRLGRAAQAS---------SPPQRpRRRAARPTVGSLTSLADPPPPPPT---------------PEPA 2711

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  854 PEPDGPAPAFLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDFHSQDTHLILKETETALAALEARLLSNSV 933
Cdd:PHA03247 2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  934 DAECEGGSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQPLRAQKEMSPSPPAAQDPGGTAlvsareqsserqhh 1013
Cdd:PHA03247 2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA-------------- 2857

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329 1014 PLGPtdmgrgepvrrsaIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASnhetPEATGAGRLGSRRKPAAPPPSPAARE 1093
Cdd:PHA03247 2858 PGGD-------------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRS----TESFALPPDQPERPPQPQAPPPPQPQ 2920

                         410       420
                  ....*....|....*....|....*..
gi 767980329 1094 EQSRSSASSQKGPQALTRSNSLSTPRP 1120
Cdd:PHA03247 2921 PQPPPPPQPQPPPPPPPRPQPPLAPTT 2947
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
 41-92 2.19e-04

forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438731 [Multi-domain]  Cd Length: 126  Bit Score: 42.64  E-value: 2.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767980329   41 KQHAVINYDqdRDEHWVKDLGSLNGTFVNDMRI-PDQKYVT---LKLNDVIRFGYD 92
Cdd:cd22679    51 RNHALLWYD--DGKFYLQDTKSSNGTFVNNQRLsKGSEESEpreLHSGDIVQFGVD 104
PHA03247 PHA03247
large tegument protein UL36; Provisional
 687-1161 3.67e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  687 GEPegsLPVRMR---RRLPQLPSERADSPAGPEssrrsgpgPPELDSEQPSRLFGQEELDPDSLSDASGSdggRGPEPGV 763
Cdd:PHA03247 2526 GEP---VHPRMLtwiRGLEELASDDAGDPPPPL--------PPAAPPAAPDRSVPPPRPAPRPSEPAVTS---RARRPDA 2591

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  764 EPQDSRRRSPQEGptwsrgRRSPRAPGEPTPASffigdQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVYVSANGR 843
Cdd:PHA03247 2592 PPQSARPRAPVDD------RGDPRGPAPPSPLP-----PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGR 2660

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  844 MVIQLR-------PGRSPEPDGPAPAFLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAArmdfhsqdthlilke 916
Cdd:PHA03247 2661 VSRPRRarrlgraAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGP--------------- 2725

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  917 tetalaalearllsnsvdaECEGGSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTP-QPLRAQKEMSPSPPAAQDP 995
Cdd:PHA03247 2726 -------------------AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPpAPAPPAAPAAGPPRRLTRP 2786

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  996 GGTALVSAREQSSErqhhPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERgPVLAHLPSSDVmasnhETPEATGA-- 1073
Cdd:PHA03247 2787 AVASLSESRESLPS----PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-PTAPPPPPGPP-----PPSLPLGGsv 2856

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329 1074 --GRLGSRRKPAAPPPSPAAreEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPE 1151
Cdd:PHA03247 2857 apGGDVRRRPPSRSPAAKPA--APARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP 2934

                         490
                  ....*....|
gi 767980329 1152 PVGRPAAEQA 1161
Cdd:PHA03247 2935 PPPRPQPPLA 2944
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
 25-94 2.56e-03

forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438724 [Multi-domain]  Cd Length: 108  Bit Score: 39.20  E-value: 2.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980329   25 VGR-EECEL-MLQSRSVDKQHAVINYDQDrDEHWVKDLgSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSN 94
Cdd:cd22672    25 IGRaKDCDLsFPGNKLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQKVELKHGDVIYLVYRKN 94
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 930-1298 2.99e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  930 SNSVDAECEGGSTPRPPEDALSGDSdvdTASTVSLRSGKSGPSPTTPQPLRAQKEMSPSPPAAQDPGGTALVSAREQSSE 1009
Cdd:PHA03307   52 AVTVVAGAAACDRFEPPTGPPPGPG---TEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329 1010 RQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSdvMASNHETPEATGAGRLGSRRKPAAPPPSP 1089
Cdd:PHA03307  129 SPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLS--SPEETARAPSSPPAEPPPSTPPAAASPRP 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329 1090 AAREEQSRSSASSqkgpqaltrsnslSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRPAAEQAKKLSRLDI 1169
Cdd:PHA03307  207 PRRSSPISASASS-------------PAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAS 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329 1170 LAMPRKRAGSFTG--TSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSRARSGSARYTSN 1247
Cdd:PHA03307  274 GWNGPSSRPGPASssSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSP 353

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767980329 1248 TRRRqqgsdytstseeeyGSRHGSPKHTRSHTSTATQTPRAGSSSRARSRA 1298
Cdd:PHA03307  354 SRPP--------------PPADPSSPRKRPRPSRAPSSPAASAGRPTRRRA 390
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 430-833 7.69e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  430 PKADKRRGPTPADRDRPSVPAPVQAGGRSSGPQRAGSlkrekteeRLGSPSPASRTPARPFGSVGRRSRLAQDFMAQclR 509
Cdd:PRK07764  365 PSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSA--------AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAP--A 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  510 ESSPAARPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLSDAGTYT---IETEAQDTEVEEARK 586
Cdd:PRK07764  435 PAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAApaaPAAPAGADDAATLRE 514

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  587 MIDQVFGVLesPELSRASSATFRP--VIRGDRDES-----DDGGVAQRM-----------ALLQEFASRplgAAPQAEHQ 648
Cdd:PRK07764  515 RWPEILAAV--PKRSRKTWAILLPeaTVLGVRGDTlvlgfSTGGLARRFaspgnaevlvtALAEELGGD---WQVEAVVG 589

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  649 GLPVPGSPGGQK--WVSRWASLADSYSDPGLTEDGLG-RRGGEPEGSLPVRMRRRLPQLPSER-ADSPAGPESSRRSGPG 724
Cdd:PRK07764  590 PAPGAAGGEGPPapASSGPPEEAARPAAPAAPAAPAApAPAGAAAAPAEASAAPAPGVAAPEHhPKHVAVPDASDGGDGW 669

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  725 PPELDSEQPsrlfgqEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRSPQEGPTWSRGRRSPRAPGEPTPASFFIGDQNG 804
Cdd:PRK07764  670 PAKAGGAAP------AAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPP 743

                         410       420
                  ....*....|....*....|....*....
gi 767980329  805 DAVLSRKPLAAPGDGEGLGQTAQPSPPAR 833
Cdd:PRK07764  744 EPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 785-1255 9.50e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  785 SPRAPGEPTPASFFIGDQNGDAVLSRKPLAAPGDgeglgQTAQPSPPARdgvyvsangrmviqlrPGRSPEPDGPAPAFL 864
Cdd:PHA03307   23 RPPATPGDAADDLLSGSQGQLVSDSAELAAVTVV-----AGAAACDRFE----------------PPTGPPPGPGTEAPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  865 RQESFTKEPASGPPAPGKPPHISShpllqDLAATRAARMDFHSqdthlilkeTETALAALEARLLSNSVDAECEGGSTPR 944
Cdd:PHA03307   82 NESRSTPTWSLSTLAPASPAREGS-----PTPPGPSSPDPPPP---------TPPPASPPPSPAPDLSEMLRPVGSPGPP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329  945 PP-EDALSGDSDVDTASTVSLRSGKSGPSPTTPQPLRAQKEMSPSPPAAQDPGGTALVSAREQSSERQHHPLGPTDMGRG 1023
Cdd:PHA03307  148 PAaSPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRS 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329 1024 EPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMAsnheTPEATGAGRLGSRRKPAAPPPSPAAREEQSRSSASSQ 1103
Cdd:PHA03307  228 AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLP----TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980329 1104 KGPqaltrsnSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPvgrpaaeqakklsrldilamPRKRAGSFTGT 1183
Cdd:PHA03307  304 GSG-------PAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP--------------------SPSRSPSPSRP 356

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980329 1184 SDPEAAPARtsfsgrsvelccasrkptmaearavSRKAANTATTTGPRQPFSRARSGSARYTSNTRRRQQGS 1255
Cdd:PHA03307  357 PPPADPSSP-------------------------RKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDA 403
 
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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