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Conserved domains on  [gi|1034586860|ref|XP_016876717|]
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centrosomal protein of 170 kDa protein B isoform X2 [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 ...
 918-1566 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: 925.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  918 GRMVIQL-RPGRSPEPDGPAPA--FLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDfHSQDTHLILKETE 994
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASSksFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLILKETE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  995 TALAALEARLLSNSVDAECEGgSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQP--LRAQKEMSPSPPAAQDPG 1072
Cdd:pfam15308   80 TALAALEAKLLSESKGDEGEG-SPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSPSAQDKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1073 GTAlvSAREQSSERQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASNHETPEatgagRL 1152
Cdd:pfam15308  159 SQP--SARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYS-----RP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1153 GSRRKPAAPPPSPAAREEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRP 1232
Cdd:pfam15308  232 SSRRKPFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1233 AAEQAKKLSRLDILAMPRKRAGSFTGTSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSR 1312
Cdd:pfam15308  312 PPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKTARTRANSISKQPFSR 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1313 ARSGSARYTST-------------------------------------TQTPRAGSSSRARSRAPGPRDTDDDEEEPDPY 1355
Cdd:pfam15308  392 TRSSSAKYSSSsnsrrrqqgsdytstseeeygsnhnspkhkrshtstaTQTPRAQGTGTARQKPPGHRETEEEEYQPDPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1356 GFIVQTAEIAEIARLSQTLVKDVAILAQEIHDVAGDGDTLGSSEPAHSASLSNMPSTPASTISAREELVQRIPEASLNFQ 1435
Cdd:pfam15308  472 PFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1436 KVPPGSLNSRDFDQNMNDSCEDALANKTRPRNREEVIFDNLMLNPVSQLSQAIRENTEHLAEKMKILFQNTGRAWEDLEA 1515
Cdd:pfam15308  552 KVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNKDRNWEEIEA 631

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034586860 1516 RINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGSLDLLTGN 1566
Cdd:pfam15308  632 KINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA super family cl00062
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 111-182 2.29e-47

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.


The actual alignment was detected with superfamily member cd22725:

Pssm-ID: 469597 [Multi-domain]  Cd Length: 106  Bit Score: 164.71  E-value: 2.29e-47
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  111 ESRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVP 182
Cdd:cd22725     35 QSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYITLKLNDVIRFGYDSNMYVLERSQHKVP 106
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 419-938 6.68e-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: 48.01  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  419 PVHTRTLKG-HKHEDGTQSDSEDPLAKAASAAgvPLEASGEQVRLQRQIKRDPQELLHNQQAfvieffDEDTPRKKRSQS 497
Cdd:PHA03247  2528 PVHPRMLTWiRGLEELASDDAGDPPPPLPPAA--PPAAPDRSVPPPRPAPRPSEPAVTSRAR------RPDAPPQSARPR 2599

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  498 FTHSPSGDPKADKRRGPTPADRDRPSVPAPVQA--------GGRSSGPQRA--------GSLKREKTEERLGSPSPASRT 561
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSpaanepdpHPPPTVPPPErprddpapGRVSRPRRARRLGRAAQASSP 2679

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  562 PARPfgsvgrRSRLAQDFMAQCLRESSPaarPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLS 641
Cdd:PHA03247  2680 PQRP------RRRAARPTVGSLTSLADP---PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  642 DAGTYTIETEAQDTEVEEARKMIDQVFGVLES-PELSRASSATFRPVIRGDRDESDDGGVAQRMALLQEFASRPLGAAPQ 720
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  721 AEHqglPVPGSPggqkwvsrwaSLADSYSDPGLTEDGLGRRGGepegslPVRmRRRLPQLPSERADSPAGPESSRRSGPG 800
Cdd:PHA03247  2831 PTS---AQPTAP----------PPPPGPPPPSLPLGGSVAPGG------DVR-RRPPSRSPAAKPAAPARPPVRRLARPA 2890

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  801 PPeldseQPSRLFGQEELDPDSLsdasgsdggRGPEPGVEPQDSRRRSPQEGPTwsrgrRSPRAPGEPTPasffigdqng 880
Cdd:PHA03247  2891 VS-----RSTESFALPPDQPERP---------PQPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQP---------- 2941

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034586860  881 davlsrkPLAAPGDGEGLGQTAQPSPPARDGVYVSanGRMVIQLRPGRSPEPDGPAPA 938
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 ...
 918-1566 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: 925.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  918 GRMVIQL-RPGRSPEPDGPAPA--FLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDfHSQDTHLILKETE 994
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASSksFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLILKETE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  995 TALAALEARLLSNSVDAECEGgSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQP--LRAQKEMSPSPPAAQDPG 1072
Cdd:pfam15308   80 TALAALEAKLLSESKGDEGEG-SPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSPSAQDKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1073 GTAlvSAREQSSERQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASNHETPEatgagRL 1152
Cdd:pfam15308  159 SQP--SARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYS-----RP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1153 GSRRKPAAPPPSPAAREEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRP 1232
Cdd:pfam15308  232 SSRRKPFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1233 AAEQAKKLSRLDILAMPRKRAGSFTGTSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSR 1312
Cdd:pfam15308  312 PPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKTARTRANSISKQPFSR 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1313 ARSGSARYTST-------------------------------------TQTPRAGSSSRARSRAPGPRDTDDDEEEPDPY 1355
Cdd:pfam15308  392 TRSSSAKYSSSsnsrrrqqgsdytstseeeygsnhnspkhkrshtstaTQTPRAQGTGTARQKPPGHRETEEEEYQPDPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1356 GFIVQTAEIAEIARLSQTLVKDVAILAQEIHDVAGDGDTLGSSEPAHSASLSNMPSTPASTISAREELVQRIPEASLNFQ 1435
Cdd:pfam15308  472 PFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1436 KVPPGSLNSRDFDQNMNDSCEDALANKTRPRNREEVIFDNLMLNPVSQLSQAIRENTEHLAEKMKILFQNTGRAWEDLEA 1515
Cdd:pfam15308  552 KVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNKDRNWEEIEA 631

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034586860 1516 RINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGSLDLLTGN 1566
Cdd:pfam15308  632 KINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
 111-182 2.29e-47

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: 164.71  E-value: 2.29e-47
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  111 ESRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVP 182
Cdd:cd22725     35 QSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYITLKLNDVIRFGYDSNMYVLERSQHKVP 106
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
111-166 3.52e-12

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 63.82  E-value: 3.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586860  111 ESRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDVIRFG 166
Cdd:COG1716     36 DDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRV--TEPAPLRDGDVIRLG 87
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 112-165 5.49e-11

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 59.51  E-value: 5.49e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034586860  112 SRSVDKQHAVINYDQDRdEHWVKDLGSLNGTFVNDMRIPdQKYVTLKLNDVIRF 165
Cdd:pfam00498   15 DPSVSRRHAEIRYDGGG-RFYLEDLGSTNGTFVNGQRLG-PEPVRLKDGDVIRL 66
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 702-1133 2.91e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  702 QRMALLQEFASRPLGAAPQA-EHQGLPvPGSPG------GQKWVSRWASLADSYSDPGLTEDG-LGRRGGEPE----GSL 769
Cdd:PTZ00449   494 KKLAPIEEEDSDKHDEPPEGpEASGLP-PKAPGdkegeeGEHEDSKESDEPKEGGKPGETKEGeVGKKPGPAKehkpSKI 572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  770 PVRMRRrlPQLPsERADSPAGPESSRRS-GPGPPELDSEQPSRLFGQEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRS 848
Cdd:PTZ00449   573 PTLSKK--PEFP-KDPKHPKDPEEPKKPkRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPE 649

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  849 PQEGPTWSRGRRSPRAPGEPTPASFFIGDQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVYVSANgRMVIQLRPgR 928
Cdd:PTZ00449   650 GPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP-RPLPPKLP-R 727

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  929 SP--------EPDGPAPA----FLRQES---FTKEPASGPPAPG------KPPHISSHPLLQDLAATRAARMDFHSqDTH 987
Cdd:PTZ00449   728 DEefpfepigDPDAEQPDdiefFTPPEEertFFHETPADTPLPDilaeefKEEDIHAETGEPDEAMKRPDSPSEHE-DKP 806

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  988 LILKETETALAALEARLLSNSVDAECEGGSTPRPPedalsgdsdvdTASTVSLRSGKSGPSPTTpqpLRAQKEMSPSPPA 1067
Cdd:PTZ00449   807 PGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDA-----------SGKIVKLKRSKSFDDLTT---VEEAEEMGAEARK 872

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034586860 1068 -AQDPGGTalvsareQSSERQHHPlgPTDMGRGEPVRRSAIRRGHRPRGSLDwPSEERGPVLAHLPS 1133
Cdd:PTZ00449   873 iVVDDDGT-------EADDEDTHP--PEEKHKSEVRRRRPPKKPSKPKKPSK-PKKPKKPDSAFIPS 929
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 111-149 2.27e-05

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 43.32  E-value: 2.27e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1034586860   111 ESRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDMRI 149
Cdd:smart00240   15 DGPSISRRHAVIVYDGG-GRFYLIDLGSTNGTFVNGKRI 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 419-938 6.68e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  419 PVHTRTLKG-HKHEDGTQSDSEDPLAKAASAAgvPLEASGEQVRLQRQIKRDPQELLHNQQAfvieffDEDTPRKKRSQS 497
Cdd:PHA03247  2528 PVHPRMLTWiRGLEELASDDAGDPPPPLPPAA--PPAAPDRSVPPPRPAPRPSEPAVTSRAR------RPDAPPQSARPR 2599

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  498 FTHSPSGDPKADKRRGPTPADRDRPSVPAPVQA--------GGRSSGPQRA--------GSLKREKTEERLGSPSPASRT 561
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSpaanepdpHPPPTVPPPErprddpapGRVSRPRRARRLGRAAQASSP 2679

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  562 PARPfgsvgrRSRLAQDFMAQCLRESSPaarPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLS 641
Cdd:PHA03247  2680 PQRP------RRRAARPTVGSLTSLADP---PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  642 DAGTYTIETEAQDTEVEEARKMIDQVFGVLES-PELSRASSATFRPVIRGDRDESDDGGVAQRMALLQEFASRPLGAAPQ 720
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  721 AEHqglPVPGSPggqkwvsrwaSLADSYSDPGLTEDGLGRRGGepegslPVRmRRRLPQLPSERADSPAGPESSRRSGPG 800
Cdd:PHA03247  2831 PTS---AQPTAP----------PPPPGPPPPSLPLGGSVAPGG------DVR-RRPPSRSPAAKPAAPARPPVRRLARPA 2890

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  801 PPeldseQPSRLFGQEELDPDSLsdasgsdggRGPEPGVEPQDSRRRSPQEGPTwsrgrRSPRAPGEPTPasffigdqng 880
Cdd:PHA03247  2891 VS-----RSTESFALPPDQPERP---------PQPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQP---------- 2941

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034586860  881 davlsrkPLAAPGDGEGLGQTAQPSPPARDGVYVSanGRMVIQLRPGRSPEPDGPAPA 938
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 ...
 918-1566 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: 925.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  918 GRMVIQL-RPGRSPEPDGPAPA--FLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDfHSQDTHLILKETE 994
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASSksFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLILKETE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  995 TALAALEARLLSNSVDAECEGgSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQP--LRAQKEMSPSPPAAQDPG 1072
Cdd:pfam15308   80 TALAALEAKLLSESKGDEGEG-SPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSPSAQDKG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1073 GTAlvSAREQSSERQHHPLGPTDMGRGEPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASNHETPEatgagRL 1152
Cdd:pfam15308  159 SQP--SARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYS-----RP 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1153 GSRRKPAAPPPSPAAREEQSRSSASSQKGPQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPVGRP 1232
Cdd:pfam15308  232 SSRRKPFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSK 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1233 AAEQAKKLSRLDILAMPRKRAGSFTGTSDPEAAPARTSFSGRSVELCCASRKPTMAEARAVSRKAANTATTTGPRQPFSR 1312
Cdd:pfam15308  312 PPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKTARTRANSISKQPFSR 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1313 ARSGSARYTST-------------------------------------TQTPRAGSSSRARSRAPGPRDTDDDEEEPDPY 1355
Cdd:pfam15308  392 TRSSSAKYSSSsnsrrrqqgsdytstseeeygsnhnspkhkrshtstaTQTPRAQGTGTARQKPPGHRETEEEEYQPDPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1356 GFIVQTAEIAEIARLSQTLVKDVAILAQEIHDVAGDGDTLGSSEPAHSASLSNMPSTPASTISAREELVQRIPEASLNFQ 1435
Cdd:pfam15308  472 PFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1436 KVPPGSLNSRDFDQNMNDSCEDALANKTRPRNREEVIFDNLMLNPVSQLSQAIRENTEHLAEKMKILFQNTGRAWEDLEA 1515
Cdd:pfam15308  552 KVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNKDRNWEEIEA 631

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034586860 1516 RINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGSLDLLTGN 1566
Cdd:pfam15308  632 KINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
 111-182 2.29e-47

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: 164.71  E-value: 2.29e-47
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  111 ESRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVP 182
Cdd:cd22725     35 QSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYITLKLNDVIRFGYDSNMYVLERSQHKVP 106
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
 112-182 3.01e-40

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: 144.38  E-value: 3.01e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034586860  112 SRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVP 182
Cdd:cd22704     32 SRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIPEQTYITLKLGDSIRFGYDTNVYRFEQLSLTTI 102
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
 111-182 1.39e-33

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: 125.47  E-value: 1.39e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  111 ESRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVP 182
Cdd:cd22724     35 QSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYITLKLDDKLRFGYDTNLFTVVRGEMRVP 106
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
 114-174 2.10e-15

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: 73.87  E-value: 2.10e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034586860  114 SVDKQHAVINY--DQDRDEHWVK--------DLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVL 174
Cdd:cd22676     40 SCSKQHAVIQFreVEKRNEGDVIenirpyiiDLGSTNGTFLNGEKIEPRRYYELREKDVLKFGLSTREYVL 110
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 114-175 1.65e-13

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: 67.97  E-value: 1.65e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586860  114 SVDKQHAVINYDQDRDEH----WVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLE 175
Cdd:cd22677     40 SISRYHAVLQYRGDADDHdggfYLYDLGSTHGTFLNKQRIPPKQYYRLRVGHVLKFGGSTRLYILQ 105
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
111-166 3.52e-12

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 63.82  E-value: 3.52e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586860  111 ESRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDVIRFG 166
Cdd:COG1716     36 DDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRV--TEPAPLRDGDVIRLG 87
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 111-166 7.39e-12

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: 63.06  E-value: 7.39e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586860  111 ESRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDVIRFG 166
Cdd:cd00060     34 DDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRI--TPPVPLQDGDVIRLG 85
FHA_SNIP1 cd22718
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and ...
 114-174 1.13e-11

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: 64.34  E-value: 1.13e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  114 SVDKQHAVINY---DQDRDEH--------WVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVL 174
Cdd:cd22718     75 SCSKQHAVLQYrlvEYTRPDGtkgrrvrpYIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGFSSREYVL 146
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 112-165 5.49e-11

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 59.51  E-value: 5.49e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034586860  112 SRSVDKQHAVINYDQDRdEHWVKDLGSLNGTFVNDMRIPdQKYVTLKLNDVIRF 165
Cdd:pfam00498   15 DPSVSRRHAEIRYDGGG-RFYLEDLGSTNGTFVNGQRLG-PEPVRLKDGDVIRL 66
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
 111-175 1.44e-10

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: 59.58  E-value: 1.44e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034586860  111 ESRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDqKYVTLKLNDVIRFGYDSNMYVLE 175
Cdd:cd22700     30 QSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQN-AAVRLAPGDVLRFGFGGLPYELV 93
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
 114-174 1.88e-10

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: 59.59  E-value: 1.88e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034586860  114 SVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVL 174
Cdd:cd22674     46 SCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEPHKPQQLPIDSTLRFGASTRRYIL 106
FHA_DDL-like cd22719
forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein ...
 114-174 7.35e-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: 58.66  E-value: 7.35e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  114 SVDKQHAVINYDQDRDEH-----------WVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVL 174
Cdd:cd22719     56 SCSKQHAVIQYRLTEKEGgdgmmgkavrpYIMDLGSTNGTFLNGERIEPQRYYELLEKDTIKFGNSSREYVL 127
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
 114-166 6.50e-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: 55.75  E-value: 6.50e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034586860  114 SVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQK----YVTLKLNDVIRFG 166
Cdd:cd22686     46 GVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKeksdPYPLTHGDELKIG 102
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
 111-166 1.57e-08

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: 53.77  E-value: 1.57e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034586860  111 ESRSVDKQHAVInyDQDRDEHWVKDLGSLNGTFVN-DMRI-PDQKYvTLKLNDVIRFG 166
Cdd:cd22665     36 PDKSVSKQHACI--EVDGGTHLIEDLGSTNGTRIGnKVRLkPNVRY-ELIDGDLLLFG 90
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
 115-174 1.04e-07

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: 52.44  E-value: 1.04e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  115 VDKQHAVINYDQDRDE--HWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVL 174
Cdd:cd22681     66 CSKQHCVIQFRNVKGIlkPYIMDLDSSNGTCLNDNVIPSSRYVELRSGDVITFSKSNDYELV 127
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
 119-190 1.70e-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: 1.70e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034586860  119 HAVINYDQDRDEHW---VKDLgSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLERVQHRVPEEALKHEK 190
Cdd:cd22685     56 HAEIHAERDGNGNWkvlIEDR-STNGTYVNDVRLQDGQRRELSDGDTITFGHKNGRRVKQWPYQKSSEFYFLFQK 129
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 115-166 1.52e-06

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: 48.51  E-value: 1.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034586860  115 VDKQHAVINYDQDRdeHW-VKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFG 166
Cdd:cd22663     43 ISRNHCVLKKNDEG--QWtIKDNKSLNGVWVNGERIEPLKPYPLNEGDLIQLG 93
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 114-174 2.07e-06

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: 48.18  E-value: 2.07e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034586860  114 SVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVL 174
Cdd:cd22691     47 SISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVYRL 107
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 702-1133 2.91e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.38  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  702 QRMALLQEFASRPLGAAPQA-EHQGLPvPGSPG------GQKWVSRWASLADSYSDPGLTEDG-LGRRGGEPE----GSL 769
Cdd:PTZ00449   494 KKLAPIEEEDSDKHDEPPEGpEASGLP-PKAPGdkegeeGEHEDSKESDEPKEGGKPGETKEGeVGKKPGPAKehkpSKI 572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  770 PVRMRRrlPQLPsERADSPAGPESSRRS-GPGPPELDSEQPSRLFGQEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRS 848
Cdd:PTZ00449   573 PTLSKK--PEFP-KDPKHPKDPEEPKKPkRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPERPE 649

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  849 PQEGPTWSRGRRSPRAPGEPTPASFFIGDQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVYVSANgRMVIQLRPgR 928
Cdd:PTZ00449   650 GPKIIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTP-RPLPPKLP-R 727

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  929 SP--------EPDGPAPA----FLRQES---FTKEPASGPPAPG------KPPHISSHPLLQDLAATRAARMDFHSqDTH 987
Cdd:PTZ00449   728 DEefpfepigDPDAEQPDdiefFTPPEEertFFHETPADTPLPDilaeefKEEDIHAETGEPDEAMKRPDSPSEHE-DKP 806

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  988 LILKETETALAALEARLLSNSVDAECEGGSTPRPPedalsgdsdvdTASTVSLRSGKSGPSPTTpqpLRAQKEMSPSPPA 1067
Cdd:PTZ00449   807 PGDHPSLPKKRHRLDGLALSTTDLESDAGRIAKDA-----------SGKIVKLKRSKSFDDLTT---VEEAEEMGAEARK 872

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034586860 1068 -AQDPGGTalvsareQSSERQHHPlgPTDMGRGEPVRRSAIRRGHRPRGSLDwPSEERGPVLAHLPS 1133
Cdd:PTZ00449   873 iVVDDDGT-------EADDEDTHP--PEEKHKSEVRRRRPPKKPSKPKKPSK-PKKPKKPDSAFIPS 929
FHA_VPS64-like cd22695
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ...
 108-180 3.78e-06

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: 48.07  E-value: 3.78e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034586860  108 GLWESRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKyVTLKLNDVIRFGYDsnmyVLERVQHR 180
Cdd:cd22695     58 GNFDSRVLSRNHACLSCDPTTGKVYIRDLKSSNGTFVNGQKIRQND-VELKVGDEVDLGTD----IDSKIEHR 125
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
 114-173 3.89e-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: 46.97  E-value: 3.89e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034586860  114 SVDKQHAVINYDQDRdEHW-VKDLGSLNGTFVN--DMRIPDQKYVtLKLNDVIRFGYDSNMYV 173
Cdd:cd22678     41 EVSGKHARIEWNSTG-SKWeLVDLGSLNGTLVNgeSISPNGRPVV-LSSGDVITLGSETKILV 101
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 114-173 5.81e-06

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: 46.18  E-value: 5.81e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  114 SVDKQHAVINydQDRDEHWVKDLGSLNGTFVNDMRIPDQKYvTLKLNDVIRFGYDSNMYV 173
Cdd:cd22680     39 FVSRNHARIT--VDSNEIYIEDLGSTNGTFVNDFKRIKGPA-KLHPNDIIKLGRTTVLKV 95
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 111-149 2.27e-05

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 43.32  E-value: 2.27e-05
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1034586860   111 ESRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDMRI 149
Cdd:smart00240   15 DGPSISRRHAVIVYDGG-GRFYLIDLGSTNGTFVNGKRI 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
 419-938 6.68e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 6.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  419 PVHTRTLKG-HKHEDGTQSDSEDPLAKAASAAgvPLEASGEQVRLQRQIKRDPQELLHNQQAfvieffDEDTPRKKRSQS 497
Cdd:PHA03247  2528 PVHPRMLTWiRGLEELASDDAGDPPPPLPPAA--PPAAPDRSVPPPRPAPRPSEPAVTSRAR------RPDAPPQSARPR 2599

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  498 FTHSPSGDPKADKRRGPTPADRDRPSVPAPVQA--------GGRSSGPQRA--------GSLKREKTEERLGSPSPASRT 561
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSpaanepdpHPPPTVPPPErprddpapGRVSRPRRARRLGRAAQASSP 2679

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  562 PARPfgsvgrRSRLAQDFMAQCLRESSPaarPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQEEDDSLS 641
Cdd:PHA03247  2680 PQRP------RRRAARPTVGSLTSLADP---PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  642 DAGTYTIETEAQDTEVEEARKMIDQVFGVLES-PELSRASSATFRPVIRGDRDESDDGGVAQRMALLQEFASRPLGAAPQ 720
Cdd:PHA03247  2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  721 AEHqglPVPGSPggqkwvsrwaSLADSYSDPGLTEDGLGRRGGepegslPVRmRRRLPQLPSERADSPAGPESSRRSGPG 800
Cdd:PHA03247  2831 PTS---AQPTAP----------PPPPGPPPPSLPLGGSVAPGG------DVR-RRPPSRSPAAKPAAPARPPVRRLARPA 2890

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  801 PPeldseQPSRLFGQEELDPDSLsdasgsdggRGPEPGVEPQDSRRRSPQEGPTwsrgrRSPRAPGEPTPasffigdqng 880
Cdd:PHA03247  2891 VS-----RSTESFALPPDQPERP---------PQPQAPPPPQPQPQPPPPPQPQ-----PPPPPPPRPQP---------- 2941

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034586860  881 davlsrkPLAAPGDGEGLGQTAQPSPPARDGVYVSanGRMVIQLRPGRSPEPDGPAPA 938
Cdd:PHA03247  2942 -------PLAPTTDPAGAGEPSGAVPQPWLGALVP--GRVAVPRFRVPQPAPSREAPA 2990
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 709-1123 8.68e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  709 EFASRPLGAAPQAEHQGLPVPGSPGGQKWVSRWASLADSYSDPGLTEDGLGRRGGEPEGS---LPVRMRRRLPQLPSERA 785
Cdd:PHA03307    15 AEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGpgtEAPANESRSTPTWSLST 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  786 DSPAGPESSRRSGPGPPELDSEQPSrlfgqeelDPDSLSDASGSDGGRGPEPGVEPQDSRRRSPQEGPTWSRGRRSPRAP 865
Cdd:PHA03307    95 LAPASPAREGSPTPPGPSSPDPPPP--------TPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDA 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  866 GEPTPASFFIgDQNGDAVLSRKPLAAPGDGEGLGQTAQPSPPARDGVyvSANGRMVIQLRPGRSPEPDGPAPAFLRQESF 945
Cdd:PHA03307   167 ASSRQAALPL-SSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSP--ISASASSPAPAPGRSAADDAGASSSDSSSSE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  946 TKEPASGPPAPGKPPHissHPLLQDLAATRAARMDFHSQDTHLILKETETALAALEARLLSNSVDAECeggSTPRPPEDA 1025
Cdd:PHA03307   244 SSGCGWGPENECPLPR---PAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA---PSSPRASSS 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1026 LSGDSDVDTASTVSLRSGKSGPSPTTPQPL-RAQKEMSPSPPAAQDPGGTALVSAREQSSERQHHP----------LGPT 1094
Cdd:PHA03307   318 SSSSRESSSSSTSSSSESSRGAAVSPGPSPsRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGrptrrraraaVAGR 397

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1034586860 1095 DMGRGEPVRRSAIRRGHRP------------RGSLDWPSEE 1123
Cdd:PHA03307   398 ARRRDATGRFPAGRPRPSPldagaasgafyaRYPLLTPSGE 438
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
 111-176 9.20e-05

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: 43.31  E-value: 9.20e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586860  111 ESRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSNMYVLER 176
Cdd:cd22675     44 EHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIEKGRPLPLPVGSVIQFGFSARKYKVRK 109
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 555-958 1.58e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  555 PSPASRTPARPFGSVGRRSRLAQDFMAQCLRESSPAARPSPEKVPPVLPAPLTPHGTSPVGPPTPPPAPTDPQLTKARKQ 634
Cdd:PHA03307    61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRP 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  635 EEDDSLSDAGTyTIETEAQDTEVEEARKmidqvfgvlESPELSRASSATFRPVIRGDRDESDDGGVAQRMALlqEFASRP 714
Cdd:PHA03307   141 VGSPGPPPAAS-PPAAGASPAAVASDAA---------SSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAA--SPRPPR 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  715 LGAaPQAEHQGLPVPGSPGGQKW-VSRWASLADSYSDPGLTEDGLGRRGGEPEGSLPVRMRRRLPQLPSERA-----DSP 788
Cdd:PHA03307   209 RSS-PISASASSPAPAPGRSAADdAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSsrpgpASS 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  789 AGPESSRRSGPGPP-ELDSEQPSRLFGQEELDPDSLSD----ASGSDGGRGPEPGVEPQDSRRRSPQEGPTWSRGRRSPR 863
Cdd:PHA03307   288 SSSPRERSPSPSPSsPGSGPAPSSPRASSSSSSSRESSssstSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  864 APGEPTPASFfigdqngdavlsrkPLAAPGDGEGLGQTAQPSPPARDGvyvSANGRMVIQLRPGRSPEPDGPAPAFLRQE 943
Cdd:PHA03307   368 RPRPSRAPSS--------------PAASAGRPTRRRARAAVAGRARRR---DATGRFPAGRPRPSPLDAGAASGAFYARY 430

                          410       420
                   ....*....|....*....|
gi 1034586860  944 -----SFTKEPASGPPAPGK 958
Cdd:PHA03307   431 plltpSGEPWPGSPPPPPGR 450
PHA03247 PHA03247
large tegument protein UL36; Provisional
 771-1196 1.79e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  771 VRMRRRLPQLPSERAdSPAGPESSRRSGPGPPELDSEQPSrlfgQEELDPDSLSDASGSDGGRGPEPGVEPQDSRRRSPQ 850
Cdd:PHA03247  2582 VTSRARRPDAPPQSA-RPRAPVDDRGDPRGPAPPSPLPPD----THAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDP 2656

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  851 EGPTWSRGRRSpRAPGEPTPASffigdqngdAVLSR-KPLAAPGDGEGLGQTAQPSPPARDgvyvsangrmviqlrPGRS 929
Cdd:PHA03247  2657 APGRVSRPRRA-RRLGRAAQAS---------SPPQRpRRRAARPTVGSLTSLADPPPPPPT---------------PEPA 2711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  930 PEPDGPAPAFLRQESFTKEPASGPPAPGKPPHISSHPLLQDLAATRAARMDFHSQDTHLILKETETALAALEARLLSNSV 1009
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1010 DAECEGGSTPRPPEDALSGDSDVDTASTVSLRSGKSGPSPTTPQPLRAQKEMSPSPPAAQDPGGTAlvsareqsserqhh 1089
Cdd:PHA03247  2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA-------------- 2857

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1090 PLGPtdmgrgepvrrsaIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMASnhetPEATGAGRLGSRRKPAAPPPSPAARE 1169
Cdd:PHA03247  2858 PGGD-------------VRRRPPSRSPAAKPAAPARPPVRRLARPAVSRS----TESFALPPDQPERPPQPQAPPPPQPQ 2920

                          410       420
                   ....*....|....*....|....*..
gi 1034586860 1170 EQSRSSASSQKGPQALTRSNSLSTPRP 1196
Cdd:PHA03247  2921 PQPPPPPQPQPPPPPPPRPQPPLAPTT 2947
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 111-166 2.13e-04

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: 41.93  E-value: 2.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034586860  111 ESRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIPdqkyvTLKLND--VIRFG 166
Cdd:cd22694     31 DDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ-----QVKLSDgtRVRLG 81
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
 117-168 2.14e-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: 2.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586860  117 KQHAVINYDqdRDEHWVKDLGSLNGTFVNDMRI-PDQKYVT---LKLNDVIRFGYD 168
Cdd:cd22679     51 RNHALLWYD--DGKFYLQDTKSSNGTFVNNQRLsKGSEESEpreLHSGDIVQFGVD 104
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 112-166 3.09e-04

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: 41.43  E-value: 3.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034586860  112 SRSVDKQHAVINYDqDRDEHWVKDLGSLNGTFVNDMRIPDQkyVTLKLNDVIRFG 166
Cdd:cd22673     37 LPGVSREHCRIEVD-ENGKAYLENLSTTNPTLVNGKAIEKS--AELKDGDVITIG 88
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 115-166 4.02e-04

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: 41.13  E-value: 4.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034586860  115 VDKQHAVINYDQDrdEHWVKDLGSLNGTFVNDMRIPDQkyVTLKLNDVIRFG 166
Cdd:cd22693     37 VSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRVTQP--VVVQPGDTIRIG 84
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 861-1340 4.06e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 4.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  861 SPRAPGEPTPASFFIGDQNGDAVLSRKPLAAPGDgeglgQTAQPSPPARdgvyvsangrmviqlrPGRSPEPDGPAPAFL 940
Cdd:PHA03307    23 RPPATPGDAADDLLSGSQGQLVSDSAELAAVTVV-----AGAAACDRFE----------------PPTGPPPGPGTEAPA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860  941 RQESFTKEPASGPPAPGKPPHISShpllqDLAATRAARMDFHSqdthlilkeTETALAALEARLLSNSVDAECEGGSTPR 1020
Cdd:PHA03307    82 NESRSTPTWSLSTLAPASPAREGS-----PTPPGPSSPDPPPP---------TPPPASPPPSPAPDLSEMLRPVGSPGPP 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1021 PP-EDALSGDSDVDTASTVSLRSGKSGPSPTTPQPLRAQKEMSPSPPAAQDPGGTALVSAREQSSERQHHPLGPTDMGRG 1099
Cdd:PHA03307   148 PAaSPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRS 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1100 EPVRRSAIRRGHRPRGSLDWPSEERGPVLAHLPSSDVMAsnheTPEATGAGRLGSRRKPAAPPPSPAAREEQSRSSASSQ 1179
Cdd:PHA03307   228 AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLP----TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSP 303

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1180 KGPqaltrsnSLSTPRPTRASRLRRARLGDASDTEAADGERGSLGNPEPvgrpaaeqakklsrldilamPRKRAGSFTGT 1259
Cdd:PHA03307   304 GSG-------PAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP--------------------SPSRSPSPSRP 356

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586860 1260 SDPEAAPARtsfsgrsvelccasrkptmaEARAVSRKAANTATTTGPRQPFSRARSGSARYTSTTQTPRAGSSSRARSRA 1339
Cdd:PHA03307   357 PPPADPSSP--------------------RKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSP 416


                   .
gi 1034586860 1340 P 1340
Cdd:PHA03307   417 L 417
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
 111-166 6.35e-04

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: 40.55  E-value: 6.35e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586860  111 ESRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDMRIpDQKYVTLKLNDVIRFG 166
Cdd:cd22683     36 SDPSISRFHAELRLEQNG--INVIDNNSANGTFINGKRI-KGKTYILKNGDIIVFG 88
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 113-166 6.71e-04

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: 40.77  E-value: 6.71e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034586860  113 RSVDKQHAVI---------NYDQDRDEHWVKDLgSLNGTFVNDMRIPDQKYVTLKLNDVIRFG 166
Cdd:cd22667     37 SSISRKHATLtvlhpeanlSDPDTRPELTLKDL-SKYGTFVNGEKLKGGSEVTLKDGDVITFG 98
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 111-166 1.61e-03

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: 39.43  E-value: 1.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034586860  111 ESRSVDKQHA--VINYDQDRdehwVKDLGSLNGTFVNDMRIPDQKYVTLKLNDVIRFG 166
Cdd:cd22682     35 DDDSVSRYHAklAVNPSAVS----IIDLGSTNGTIVNGKKIPKLASCDLQNGDQIKIG 88
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 114-166 4.46e-03

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: 37.83  E-value: 4.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034586860  114 SVDKQHAVINYDQDrdEHWVKDLGSLNGTFVNDMRIpdQKYVTLKLNDVIRFG 166
Cdd:cd22668     36 GVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPV--TPEWRLADGDVITLG 84
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 113-166 4.72e-03

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: 38.01  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034586860  113 RSVDKQHAVInydQDRDEHW-VKDLGSLNGTFVNDMRIPDQKyVTLKLNDVIRFG 166
Cdd:pfam16697   34 KEVSRVHLKL---EVDDEGWrLDDLGSGNGTLVNGQRVTELG-IALRPGDRIELG 84
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 111-170 5.56e-03

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: 38.04  E-value: 5.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034586860  111 ESRSVDKQHAVI---NYDQDRDEHWVKDLgSLNGTFVNDMRIPDQKYVTLKLNDVIRFGYDSN 170
Cdd:cd22690     34 TDPRISKHHCIItrkRSGKGLDDVYVTDT-STNGTFINNNRLGKGSQSLLQDGDEIVLIWDKN 95
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 112-166 7.44e-03

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: 40.52  E-value: 7.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034586860  112 SRSVDKQHAVINYDqdRDEHWVKDLgSLNGTFVN--DMRIPDQKYVTLKLNDVIRFG 166
Cdd:COG3456     44 DRSVSRRHAEIRFR--DGAFCLTDL-STNGTFLNgsDHPLGPGRPVRLRDGDRLRIG 97
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
 114-166 9.11e-03

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: 37.36  E-value: 9.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034586860  114 SVDKQHAviNYDQDRDEHWVKDLGSLNGTFVNDMRIPDqkyVTLKLNDVIRFG 166
Cdd:cd22684     39 TVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERIDS---AVLRNGDEVQIG 86
 
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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