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Conserved domains on  [gi|1811067939|ref|XP_032338712|]
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centrosomal protein of 170 kDa protein B isoform X2 [Camelus ferus]

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 ...
836-1532 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: 971.89  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  836 GRMVIQL-RTERSPEPESSCPAppkeaLAFVRQDSFTKEPTSGSAAPGQLPHIPSHPLLQDLAAARASCVDlHSQDTHLI 914
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASS-----KSFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  915 LKETETALAALEARLLSKSVEGPEGemGSAPRPPEDSLSGDSDVDTSSTVSLLSGKNGPSPTGPQP--TGLRKEKAPSPP 992
Cdd:pfam15308   75 LKETETALAALEAKLLSESKGDEGE--GSPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSP 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  993 AVQDPGtvALSSARERLSEKQRHPLGLPDVGRGEPTRRPVMRRSHGPQGSRDWPEEEQGSSLAHLPSADMVTSDHETPTA 1072
Cdd:pfam15308  153 SAQDKG--SQPSARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYSR 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1073 TGAGRPgprrkpMAPPPPPAAAREEQPRSSASVQKGQQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADSERGPPVN 1152
Cdd:pfam15308  231 PSSRRK------PFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVAS 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1153 PEPVGRPPLEQAKRLSRLDILAMPRKRAGSFTGPGDSEATPTRAGFSGRSVELYCTGRKPTVAEARATARK--ATNTAAV 1230
Cdd:pfam15308  305 EVSATSKPPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKtaRTRANSI 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1231 SHQPFSRARPGSARYSSSRTnsltrdTRRRQQGSDCTSTSEEEYGSHHGSPKHTRSHASTATQTPRASGSGRARPRAPGH 1310
Cdd:pfam15308  385 SKQPFSRTRSSSAKYSSSSN------SRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPGH 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1311 RDTDEEEE--DPCGFLVQTSDIAEIARLSQTLVKDVAILAREIHDVAGDGDSLGSPGSARSLSINNVPSTPASTISAREE 1388
Cdd:pfam15308  459 RETEEEEYqpDPYPFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREE 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1389 LVQRIPEASLNFQKVPPGSLSSRDLDQNMNDRCEDPLANRMRPRNREEVIFDNLMLNPVSQLSHAIRENTEHLAEKMKIL 1468
Cdd:pfam15308  539 LVQHIPEASLNFQKVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKIL 618
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1811067939 1469 FQNTGRAWEDLEARINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGNLDLLTGN 1532
Cdd:pfam15308  619 FQNKDRNWEEIEAKINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
1-106 1.09e-75

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: 245.61  E-value: 1.09e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    1 MSVTSWFLVSSSGTRHRLPRELIFVGREDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVT 80
Cdd:cd22725      1 MSVTSWFLVSSSGTRHRLPREMIFVGREDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYIT 80
                           90       100
                   ....*....|....*....|....*.
gi 1811067939   81 LKLNDVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22725     81 LKLNDVIRFGYDSNMYVLERSQHKVP 106
PHA03247 super family cl33720
large tegument protein UL36; Provisional
412-837 6.55e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 6.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  412 TPRKKRSQSFTHTPPGDPRPDRRRGPGPADRDRPAAPAPAPTLARGAGSGSGPQRAGSLKREKAEERLGSPAPAPRASAR 491
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  492 PFGSVGRRSRLAQDFMAQCLQ--DSSPAQRPGPEKATPALPAPLTP---RGASPVAPST-LPPPSTDPQVTKArkqeedd 565
Cdd:PHA03247  2680 PQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPaaaRQASPALPAApAPPAVPAGPATPG------- 2752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  566 slSDAGTYTIETEAQDQEVEEARKMIDQVFGVLEAPELSRASSATFRPVIRGDRDEPGDGVAQRMALLQEFASRPVGVPP 645
Cdd:PHA03247  2753 --GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  646 QVELQGLPVPGSPGgqkwvsrwasladsYSDPGLSEDGPGRRTGELegalpvrQRRLLPQLPSDRADSPAGPEAARKSGP 725
Cdd:PHA03247  2831 PTSAQPTAPPPPPG--------------PPPPSLPLGGSVAPGGDV-------RRRPPSRSPAAKPAAPARPPVRRLARP 2889
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  726 GPPELGSEQAglllgQEDLEPDSLSDASGSDGGRGPEPSRGPQEGQAWTRGRRSPRGPGEPAPTTFFIGDQNGEAALPKK 805
Cdd:PHA03247  2890 AVSRSTESFA-----LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1811067939  806 PPVAPREAEGPGRVAQPSPPARDGMYVSTSGR 837
Cdd:PHA03247  2965 GALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
126-254 7.81e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  126 PAPKRGEalPGHTPHCESSAPRPERGDRRPgAEAAAYRTPLYGQPSWWGEDEGTLPEYPrQEEPCMERPKELAQKDGDLT 205
Cdd:PRK10263   364 PGPQTGE--PVIAPAPEGYPQQSQYAQPAV-QYNEPLQQPVQPQQPYYAPAAEQPAQQP-YYAPAPEQPAQQPYYAPAPE 439
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1811067939  206 GTVAGFRAPAEPQGYSFRREPSY-FEIPTKETPPPRPLEVPVHEAPPRDV 254
Cdd:PRK10263   440 QPVAGNAWQAEEQQSTFAPQSTYqTEQTYQQPAAQEPLYQQPQPVEQQPV 489
 
Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
836-1532 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: 971.89  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  836 GRMVIQL-RTERSPEPESSCPAppkeaLAFVRQDSFTKEPTSGSAAPGQLPHIPSHPLLQDLAAARASCVDlHSQDTHLI 914
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASS-----KSFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  915 LKETETALAALEARLLSKSVEGPEGemGSAPRPPEDSLSGDSDVDTSSTVSLLSGKNGPSPTGPQP--TGLRKEKAPSPP 992
Cdd:pfam15308   75 LKETETALAALEAKLLSESKGDEGE--GSPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSP 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  993 AVQDPGtvALSSARERLSEKQRHPLGLPDVGRGEPTRRPVMRRSHGPQGSRDWPEEEQGSSLAHLPSADMVTSDHETPTA 1072
Cdd:pfam15308  153 SAQDKG--SQPSARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYSR 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1073 TGAGRPgprrkpMAPPPPPAAAREEQPRSSASVQKGQQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADSERGPPVN 1152
Cdd:pfam15308  231 PSSRRK------PFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVAS 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1153 PEPVGRPPLEQAKRLSRLDILAMPRKRAGSFTGPGDSEATPTRAGFSGRSVELYCTGRKPTVAEARATARK--ATNTAAV 1230
Cdd:pfam15308  305 EVSATSKPPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKtaRTRANSI 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1231 SHQPFSRARPGSARYSSSRTnsltrdTRRRQQGSDCTSTSEEEYGSHHGSPKHTRSHASTATQTPRASGSGRARPRAPGH 1310
Cdd:pfam15308  385 SKQPFSRTRSSSAKYSSSSN------SRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPGH 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1311 RDTDEEEE--DPCGFLVQTSDIAEIARLSQTLVKDVAILAREIHDVAGDGDSLGSPGSARSLSINNVPSTPASTISAREE 1388
Cdd:pfam15308  459 RETEEEEYqpDPYPFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREE 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1389 LVQRIPEASLNFQKVPPGSLSSRDLDQNMNDRCEDPLANRMRPRNREEVIFDNLMLNPVSQLSHAIRENTEHLAEKMKIL 1468
Cdd:pfam15308  539 LVQHIPEASLNFQKVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKIL 618
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1811067939 1469 FQNTGRAWEDLEARINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGNLDLLTGN 1532
Cdd:pfam15308  619 FQNKDRNWEEIEAKINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
1-106 1.09e-75

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: 245.61  E-value: 1.09e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    1 MSVTSWFLVSSSGTRHRLPRELIFVGREDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVT 80
Cdd:cd22725      1 MSVTSWFLVSSSGTRHRLPREMIFVGREDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYIT 80
                           90       100
                   ....*....|....*....|....*.
gi 1811067939   81 LKLNDVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22725     81 LKLNDVIRFGYDSNMYVLERSQHKVP 106
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
13-90 1.61e-18

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 81.93  E-value: 1.61e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811067939   13 GTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDVRIpdQKYVTLKLNDVIRFG 90
Cdd:COG1716     13 GRRFPLDGGPLTIGRaPDNDIVLDDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRV--TEPAPLRDGDVIRLG 87
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
23-89 2.72e-15

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 71.84  E-value: 2.72e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811067939   23 IFVGRE-DCELMLQSRSVDKQHAVINYDQDRdEHWVKDLGSLNGTFVNDVRIPdQKYVTLKLNDVIRF 89
Cdd:pfam00498    1 VTIGRSpDCDIVLDDPSVSRRHAEIRYDGGG-RFYLEDLGSTNGTFVNGQRLG-PEPVRLKDGDVIRL 66
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
23-73 6.56e-10

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 56.03  E-value: 6.56e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1811067939    23 IFVGR--EDCELMLQSRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDVRI 73
Cdd:smart00240    1 VTIGRssEDCDIQLDGPSISRRHAVIVYDGG-GRFYLIDLGSTNGTFVNGKRI 52
PHA03247 PHA03247
large tegument protein UL36; Provisional
412-837 6.55e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 6.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  412 TPRKKRSQSFTHTPPGDPRPDRRRGPGPADRDRPAAPAPAPTLARGAGSGSGPQRAGSLKREKAEERLGSPAPAPRASAR 491
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  492 PFGSVGRRSRLAQDFMAQCLQ--DSSPAQRPGPEKATPALPAPLTP---RGASPVAPST-LPPPSTDPQVTKArkqeedd 565
Cdd:PHA03247  2680 PQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPaaaRQASPALPAApAPPAVPAGPATPG------- 2752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  566 slSDAGTYTIETEAQDQEVEEARKMIDQVFGVLEAPELSRASSATFRPVIRGDRDEPGDGVAQRMALLQEFASRPVGVPP 645
Cdd:PHA03247  2753 --GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  646 QVELQGLPVPGSPGgqkwvsrwasladsYSDPGLSEDGPGRRTGELegalpvrQRRLLPQLPSDRADSPAGPEAARKSGP 725
Cdd:PHA03247  2831 PTSAQPTAPPPPPG--------------PPPPSLPLGGSVAPGGDV-------RRRPPSRSPAAKPAAPARPPVRRLARP 2889
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  726 GPPELGSEQAglllgQEDLEPDSLSDASGSDGGRGPEPSRGPQEGQAWTRGRRSPRGPGEPAPTTFFIGDQNGEAALPKK 805
Cdd:PHA03247  2890 AVSRSTESFA-----LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1811067939  806 PPVAPREAEGPGRVAQPSPPARDGMYVSTSGR 837
Cdd:PHA03247  2965 GALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
PHA03247 PHA03247
large tegument protein UL36; Provisional
620-1088 6.73e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  620 DEP-GDGVAQRMAL----LQEFASRPVGVPPQVeLQGLPVPGSPGGQKWVSRwasladsysdPGLSEDGPGRRTGELEGA 694
Cdd:PHA03247  2522 DEPvGEPVHPRMLTwirgLEELASDDAGDPPPP-LPPAAPPAAPDRSVPPPR----------PAPRPSEPAVTSRARRPD 2590
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  695 LPVRQRRllPQLPSDRADSPAGPEAARKSGPG------PPELGSEQAGLLLGQEDL-EPDSLSDASGSDGGRGPEPSRGP 767
Cdd:PHA03247  2591 APPQSAR--PRAPVDDRGDPRGPAPPSPLPPDthapdpPPPSPSPAANEPDPHPPPtVPPPERPRDDPAPGRVSRPRRAR 2668
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  768 QEGQAwTRGRRSPRGPGEPApttffIGDQNGEAALPKKPPVAPREAEGPGRVAQPSPPARDGMYVStsgrmviqlRTERS 847
Cdd:PHA03247  2669 RLGRA-AQASSPPQRPRRRA-----ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA---------RQASP 2733
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  848 PEPESSCPAPPKEALAfvrqdsftkepTSGSAAPGQLPHIPSHPLLQDLAAARAScvdlhsqdthlilketetaLAALEA 927
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPA-----------TPGGPARPARPPTTAGPPAPAPPAAPAA-------------------GPPRRL 2783
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  928 RLLSKSVEGPEGEMGSAPRPPEDSLSGDSDVDTSSTVSLLSGKNGPSPTGPQPTGLRKEKAPSPPAVQDPGTVALSSARE 1007
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1008 RlsekqRHPLGLPDVGRGEPTRRPVMRRSHGPQGSRDWPEEEQGSSLAHLPSADMVTSDHETPTATGAGRPGPRRKPMAP 1087
Cdd:PHA03247  2864 R-----RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938

                   .
gi 1811067939 1088 P 1088
Cdd:PHA03247  2939 P 2939
PRK10263 PRK10263
DNA translocase FtsK; Provisional
126-254 7.81e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  126 PAPKRGEalPGHTPHCESSAPRPERGDRRPgAEAAAYRTPLYGQPSWWGEDEGTLPEYPrQEEPCMERPKELAQKDGDLT 205
Cdd:PRK10263   364 PGPQTGE--PVIAPAPEGYPQQSQYAQPAV-QYNEPLQQPVQPQQPYYAPAAEQPAQQP-YYAPAPEQPAQQPYYAPAPE 439
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1811067939  206 GTVAGFRAPAEPQGYSFRREPSY-FEIPTKETPPPRPLEVPVHEAPPRDV 254
Cdd:PRK10263   440 QPVAGNAWQAEEQQSTFAPQSTYqTEQTYQQPAAQEPLYQQPQPVEQQPV 489
 
Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
836-1532 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: 971.89  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  836 GRMVIQL-RTERSPEPESSCPAppkeaLAFVRQDSFTKEPTSGSAAPGQLPHIPSHPLLQDLAAARASCVDlHSQDTHLI 914
Cdd:pfam15308    1 GRSAIQLqTQDKSPEPDKEASS-----KSFVRQESFTKEKPSGNVPIEKLPHISSHPLLRDLERSRSARMD-HSQDTHLI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  915 LKETETALAALEARLLSKSVEGPEGemGSAPRPPEDSLSGDSDVDTSSTVSLLSGKNGPSPTGPQP--TGLRKEKAPSPP 992
Cdd:pfam15308   75 LKETETALAALEAKLLSESKGDEGE--GSPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKsiSSLQKEKSSSSP 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  993 AVQDPGtvALSSARERLSEKQRHPLGLPDVGRGEPTRRPVMRRSHGPQGSRDWPEEEQGSSLAHLPSADMVTSDHETPTA 1072
Cdd:pfam15308  153 SAQDKG--SQPSARERLSEKRRKSRTPDDGGRAEAARRFQSRRSRGPRGSLDLTDDEQTSSLPHLPISDIVSSDHETYSR 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1073 TGAGRPgprrkpMAPPPPPAAAREEQPRSSASVQKGQQALTRSNSLSTPRPTRASRLRRARLGDASDTEAADSERGPPVN 1152
Cdd:pfam15308  231 PSSRRK------PFTSPDLLAQKEEQSKSSKSSQKVQQVLTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVAS 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1153 PEPVGRPPLEQAKRLSRLDILAMPRKRAGSFTGPGDSEATPTRAGFSGRSVELYCTGRKPTVAEARATARK--ATNTAAV 1230
Cdd:pfam15308  305 EVSATSKPPTEAKKLSRLDILAMPRKRAGSFTAPSDSEATTSRSGFSGRSVELYCSSRKGTVSEARAAARKtaRTRANSI 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1231 SHQPFSRARPGSARYSSSRTnsltrdTRRRQQGSDCTSTSEEEYGSHHGSPKHTRSHASTATQTPRASGSGRARPRAPGH 1310
Cdd:pfam15308  385 SKQPFSRTRSSSAKYSSSSN------SRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPGH 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1311 RDTDEEEE--DPCGFLVQTSDIAEIARLSQTLVKDVAILAREIHDVAGDGDSLGSPGSARSLSINNVPSTPASTISAREE 1388
Cdd:pfam15308  459 RETEEEEYqpDPYPFQDWTAHSAEIARLSQDLAKDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREE 538
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1389 LVQRIPEASLNFQKVPPGSLSSRDLDQNMNDRCEDPLANRMRPRNREEVIFDNLMLNPVSQLSHAIRENTEHLAEKMKIL 1468
Cdd:pfam15308  539 LVQHIPEASLNFQKVPPGSNGRKDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKIL 618
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1811067939 1469 FQNTGRAWEDLEARINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPSGNLDLLTGN 1532
Cdd:pfam15308  619 FQNKDRNWEEIEAKINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
1-106 1.09e-75

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: 245.61  E-value: 1.09e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    1 MSVTSWFLVSSSGTRHRLPRELIFVGREDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVT 80
Cdd:cd22725      1 MSVTSWFLVSSSGTRHRLPREMIFVGREDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYIT 80
                           90       100
                   ....*....|....*....|....*.
gi 1811067939   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 3.40e-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: 206.79  E-value: 3.40e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    5 SWFLVSSSGTRHRLPRELIFVGREDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVTLKLN 84
Cdd:cd22704      1 SWCLVSSDGTRHRLPRSMLFVGREDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIPEQTYITLKLG 80
                           90       100
                   ....*....|....*....|..
gi 1811067939   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 3.23e-60

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: 201.35  E-value: 3.23e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    1 MSVTSWFLVSSSGTRHRLPRELIFVGREDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVT 80
Cdd:cd22724      1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYIT 80
                           90       100
                   ....*....|....*....|....*.
gi 1811067939   81 LKLNDVIRFGYDSNMYVLERVQHRVP 106
Cdd:cd22724     81 LKLDDKLRFGYDTNLFTVVRGEMRVP 106
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
13-90 1.61e-18

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 81.93  E-value: 1.61e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811067939   13 GTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDVRIpdQKYVTLKLNDVIRFG 90
Cdd:COG1716     13 GRRFPLDGGPLTIGRaPDNDIVLDDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRV--TEPAPLRDGDVIRLG 87
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
10-90 5.42e-18

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: 80.40  E-value: 5.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   10 SSSGTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDVRIpdQKYVTLKLNDVIR 88
Cdd:cd00060      8 DGGGREFPLTKGVVTIGRsPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRI--TPPVPLQDGDVIR 83

                   ..
gi 1811067939   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 1.26e-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: 76.52  E-value: 1.26e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811067939   25 VGREDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDqKYVTLKLNDVIRFGYDSNMYVLE 99
Cdd:cd22700     20 IGREGCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQN-AAVRLAPGDVLRFGFGGLPYELV 93
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
25-99 1.80e-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: 1.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   25 VGR-EDCELMLQSRSVDKQHAVINYDQDRDEH----WVKDLGSLNGTFVNDVRIPDQKYVTLKLNDVIRFGYDSNMYVLE 99
Cdd:cd22677     26 FGRlPGCDVVLEHPSISRYHAVLQYRGDADDHdggfYLYDLGSTHGTFLNKQRIPPKQYYRLRVGHVLKFGGSTRLYILQ 105
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
23-89 2.72e-15

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 71.84  E-value: 2.72e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811067939   23 IFVGRE-DCELMLQSRSVDKQHAVINYDQDRdEHWVKDLGSLNGTFVNDVRIPdQKYVTLKLNDVIRF 89
Cdd:pfam00498    1 VTIGRSpDCDIVLDDPSVSRRHAEIRYDGGG-RFYLEDLGSTNGTFVNGQRLG-PEPVRLKDGDVIRL 66
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
16-98 5.10e-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: 72.72  E-value: 5.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   16 HRLPRELIfvGRED--CELMLQSRSVDKQHAVINY--DQDRDEHWVK--------DLGSLNGTFVNDVRIPDQKYVTLKL 83
Cdd:cd22676     18 HRQSAYLI--GRDRrvADIPLDHPSCSKQHAVIQFreVEKRNEGDVIenirpyiiDLGSTNGTFLNGEKIEPRRYYELRE 95
                           90
                   ....*....|....*
gi 1811067939   84 NDVIRFGYDSNMYVL 98
Cdd:cd22676     96 KDVLKFGLSTREYVL 110
FHA_SNIP1 cd22718
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and ...
16-98 6.91e-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: 64.72  E-value: 6.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   16 HRLPRELIFVGREDCELMLQSRSVDKQHAVINY---DQDRDEH--------WVKDLGSLNGTFVNDVRIPDQKYVTLKLN 84
Cdd:cd22718     53 HRQSAYLLGRDRKIADIPIDHPSCSKQHAVLQYrlvEYTRPDGtkgrrvrpYIIDLESANGTFLNNKKIEPQRYYELKEK 132
                           90
                   ....*....|....
gi 1811067939   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 2.62e-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: 61.48  E-value: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   11 SSGTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVInyDQDRDEHWVKDLGSLNGTFVN-DVRI-PDQKYvTLKLNDVI 87
Cdd:cd22665     11 GPEKDFPLYEGENVIGRdPSCSVVLPDKSVSKQHACI--EVDGGTHLIEDLGSTNGTRIGnKVRLkPNVRY-ELIDGDLL 87

                   ...
gi 1811067939   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 7.71e-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: 7.71e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811067939   26 GR--EDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVTLKLNDVIRFGYDSNMYVL 98
Cdd:cd22674     32 GRnsDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEPHKPQQLPIDSTLRFGASTRRYIL 106
FHA_DDL-like cd22719
forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein ...
21-98 2.40e-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: 59.81  E-value: 2.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   21 ELIFVGREDCELMLQSRSV----------DKQHAVINYDQDRDEH-----------WVKDLGSLNGTFVNDVRIPDQKYV 79
Cdd:cd22719     29 EPLHIHRQSCYLFGRERKVadiptdhpscSKQHAVIQYRLTEKEGgdgmmgkavrpYIMDLGSTNGTFLNGERIEPQRYY 108
                           90
                   ....*....|....*....
gi 1811067939   80 TLKLNDVIRFGYDSNMYVL 98
Cdd:cd22719    109 ELLEKDTIKFGNSSREYVL 127
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
25-90 3.18e-10

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: 59.22  E-value: 3.18e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811067939   25 VGRE-DCELMLQ--SRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQK----YVTLKLNDVIRFG 90
Cdd:cd22686     30 IGREkDHGHTIRipELGVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKeksdPYPLTHGDELKIG 102
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
23-73 6.56e-10

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 56.03  E-value: 6.56e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1811067939    23 IFVGR--EDCELMLQSRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDVRI 73
Cdd:smart00240    1 VTIGRssEDCDIQLDGPSISRRHAVIVYDGG-GRFYLIDLGSTNGTFVNGKRI 52
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
18-98 2.09e-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: 56.66  E-value: 2.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   18 LPRELIFVGR-EDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVTLKLNDVIRFGYDSNMY 96
Cdd:cd22691     26 EEEDILVVGRhPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVY 105

                   ..
gi 1811067939   97 VL 98
Cdd:cd22691    106 RL 107
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
23-98 2.41e-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: 57.06  E-value: 2.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   23 IFVGRED--------CELMLQSRSVDKQHAVINYDQDRDE--HWVKDLGSLNGTFVNDVRIPDQKYVTLKLNDVIRFGYD 92
Cdd:cd22681     42 YLIGREKgesteivvADIGIPEETCSKQHCVIQFRNVKGIlkPYIMDLDSSNGTCLNDNVIPSSRYVELRSGDVITFSKS 121

                   ....*.
gi 1811067939   93 SNMYVL 98
Cdd:cd22681    122 NDYELV 127
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
11-90 3.76e-09

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: 55.30  E-value: 3.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   11 SSGTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVINYDqDRDEHWVKDLGSLNGTFVNDVRIPDQkyVTLKLNDVIRF 89
Cdd:cd22673     11 TDGSRFPLTKKSCTFGRdLSCDIRIQLPGVSREHCRIEVD-ENGKAYLENLSTTNPTLVNGKAIEKS--AELKDGDVITI 87

                   .
gi 1811067939   90 G 90
Cdd:cd22673     88 G 88
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
6-90 1.80e-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: 53.90  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    6 WFL--VSSSGTRHRLP---RELIFVGR---------EDCELMLqSRsvdkQHAVINYDQDRdeHW-VKDLGSLNGTFVND 70
Cdd:cd22663      1 WCLrrVGHGIDPLVLLledGKEVTVGRglgvtyqlvSTCPLMI-SR----NHCVLKKNDEG--QWtIKDNKSLNGVWVNG 73
                           90       100
                   ....*....|....*....|
gi 1811067939   71 VRIPDQKYVTLKLNDVIRFG 90
Cdd:cd22663     74 ERIEPLKPYPLNEGDLIQLG 93
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
6-90 2.02e-08

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: 53.48  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    6 WFLVSSSG---TRHRLP--RELIfVGREDCELMLQ-SRSVDKQHAVI---------NYDQDRDEHWVKDLgSLNGTFVND 70
Cdd:cd22667      1 WWLLSEQDgagTSYYLLpgGEYT-VGRKDCDIIIVdDSSISRKHATLtvlhpeanlSDPDTRPELTLKDL-SKYGTFVNG 78
                           90       100
                   ....*....|....*....|
gi 1811067939   71 VRIPDQKYVTLKLNDVIRFG 90
Cdd:cd22667     79 EKLKGGSEVTLKDGDVITFG 98
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
12-90 2.97e-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: 52.65  E-value: 2.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   12 SGTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVInydQDRDEHW-VKDLGSLNGTFVNDVRIPDQKyVTLKLNDVIRF 89
Cdd:pfam16697    8 AGAEFPLEGGRYRIGSdPDCDIVLSDKEVSRVHLKL---EVDDEGWrLDDLGSGNGTLVNGQRVTELG-IALRPGDRIEL 83

                   .
gi 1811067939   90 G 90
Cdd:pfam16697   84 G 84
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
9-99 6.37e-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: 52.23  E-value: 6.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    9 VSSSGTRHRLP---RELIFVGR-EDCELMLQSRSVDKQHAVINYDQDRDEH----WVKDLgSLNGTFVNDVRIPDQKYVT 80
Cdd:cd22670      7 SSPGSTDIVLPiykNQVITIGRsPSCDIVINDPFVSRTHCRIYSVQFDESSaplvYVEDL-SSNGTYLNGKLIGRNNTVL 85
                           90
                   ....*....|....*....
gi 1811067939   81 LKLNDVIRFGYDSNMYVLE 99
Cdd:cd22670     86 LSDGDVIEIAHSATFVYVH 104
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
25-114 6.77e-08

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: 52.80  E-value: 6.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   25 VGR--EDCELMLQSRS----VDKQHAVINYDQDRDEHW---VKDLgSLNGTFVNDVRIPDQKYVTLKLNDVIRFGYDSNM 95
Cdd:cd22685     32 IGRnpEVCDVFLCSSQhpnlISREHAEIHAERDGNGNWkvlIEDR-STNGTYVNDVRLQDGQRRELSDGDTITFGHKNGR 110
                           90
                   ....*....|....*....
gi 1811067939   96 YVLERVQHRVPEEALRHEK 114
Cdd:cd22685    111 RVKQWPYQKSSEFYFLFQK 129
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
20-97 1.07e-07

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: 51.19  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   20 RELIFVGRED-CELMLQSRSVDKQHAVINydQDRDEHWVKDLGSLNGTFVND-VRIPDQKyvTLKLNDVIRFGYDSNMYV 97
Cdd:cd22680     20 FSSVSIGRDPeNVIVIPDPFVSRNHARIT--VDSNEIYIEDLGSTNGTFVNDfKRIKGPA--KLHPNDIIKLGRTTVLKV 95
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
12-90 2.04e-07

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: 50.40  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   12 SGTRHRLPRELIFVGRE-DCELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDVRIPdqkyvTLKLND--VIR 88
Cdd:cd22694      7 GGELRFDPGSSVRIGRDpDADVRLDDPRVSRRHALLEFDGDG--WVYTDLGSRNGTYLNGRRVQ-----QVKLSDgtRVR 79

                   ..
gi 1811067939   89 FG 90
Cdd:cd22694     80 LG 81
PHA03247 PHA03247
large tegument protein UL36; Provisional
412-837 6.55e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 6.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  412 TPRKKRSQSFTHTPPGDPRPDRRRGPGPADRDRPAAPAPAPTLARGAGSGSGPQRAGSLKREKAEERLGSPAPAPRASAR 491
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  492 PFGSVGRRSRLAQDFMAQCLQ--DSSPAQRPGPEKATPALPAPLTP---RGASPVAPST-LPPPSTDPQVTKArkqeedd 565
Cdd:PHA03247  2680 PQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPaaaRQASPALPAApAPPAVPAGPATPG------- 2752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  566 slSDAGTYTIETEAQDQEVEEARKMIDQVFGVLEAPELSRASSATFRPVIRGDRDEPGDGVAQRMALLQEFASRPVGVPP 645
Cdd:PHA03247  2753 --GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  646 QVELQGLPVPGSPGgqkwvsrwasladsYSDPGLSEDGPGRRTGELegalpvrQRRLLPQLPSDRADSPAGPEAARKSGP 725
Cdd:PHA03247  2831 PTSAQPTAPPPPPG--------------PPPPSLPLGGSVAPGGDV-------RRRPPSRSPAAKPAAPARPPVRRLARP 2889
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  726 GPPELGSEQAglllgQEDLEPDSLSDASGSDGGRGPEPSRGPQEGQAWTRGRRSPRGPGEPAPTTFFIGDQNGEAALPKK 805
Cdd:PHA03247  2890 AVSRSTESFA-----LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL 2964
                          410       420       430
                   ....*....|....*....|....*....|..
gi 1811067939  806 PPVAPREAEGPGRVAQPSPPARDGMYVSTSGR 837
Cdd:PHA03247  2965 GALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
6-94 7.01e-07

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: 49.21  E-value: 7.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    6 WFLVSSSGTRHR---LPRELIFVGR-EDCELMLQSRSVDKQHAVI---NYDQDRDEHWVKDLgSLNGTFVNDVRIPDQKY 78
Cdd:cd22690      1 WGRLKSLNPSYPdieLTQNTTFIGRsKDCDEEITDPRISKHHCIItrkRSGKGLDDVYVTDT-STNGTFINNNRLGKGSQ 79
                           90
                   ....*....|....*.
gi 1811067939   79 VTLKLNDVIRFGYDSN 94
Cdd:cd22690     80 SLLQDGDEIVLIWDKN 95
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
13-90 9.67e-07

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: 48.45  E-value: 9.67e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811067939   13 GTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVINYDQDrdEHWVKDLGSLNGTFVNDVRIPDQkyVTLKLNDVIRFG 90
Cdd:cd22693     10 GQTFPIDKSGITIGRaDDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRVTQP--VVVQPGDTIRIG 84
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
7-90 1.02e-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: 48.18  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    7 FLVSSSGTRHRLPREL----IFVGR-EDCELMLQSRSVDKQHAVINYDQDrdeHW-VKDLGSLNGTFVNDVRIPDqkyVT 80
Cdd:cd22698      3 ILIEQKGSEEGKDYELdqdeFTIGRsSNNDIRLNDHSVSRHHARIVRQGD---KCnLTDLGSTNGTFLNGIRVGT---HE 76
                           90
                   ....*....|
gi 1811067939   81 LKLNDVIRFG 90
Cdd:cd22698     77 LKHGDRIQLG 86
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
20-90 1.93e-06

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: 47.87  E-value: 1.93e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811067939   20 RELIFVGRE-DCELMLQSRSVDKQHAVINYDQDRdeHWVKDLGSLNGTFVNDVRIpDQKYVTLKLNDVIRFG 90
Cdd:cd22683     20 RNVTTIGRSrSCDLVLSDPSISRFHAELRLEQNG--INVIDNNSANGTFINGKRI-KGKTYILKNGDIIVFG 88
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
31-97 2.24e-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: 47.74  E-value: 2.24e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   31 ELMLQSRSVDKQHAVINYDQDRdEHW-VKDLGSLNGTFVN--DVRIPDQKYVtLKLNDVIRFGYDSNMYV 97
Cdd:cd22678     34 DIALKDDEVSGKHARIEWNSTG-SKWeLVDLGSLNGTLVNgeSISPNGRPVV-LSSGDVITLGSETKILV 101
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
16-100 2.51e-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: 47.94  E-value: 2.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   16 HRLPRELIfvGRED-CELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKYVTLKLNDVIRFGYDSN 94
Cdd:cd22675     26 DRFPFYLF--GRSPvCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIEKGRPLPLPVGSVIQFGFSAR 103

                   ....*.
gi 1811067939   95 MYVLER 100
Cdd:cd22675    104 KYKVRK 109
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
425-827 2.82e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.48  E-value: 2.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  425 PPGDPRPdRRRGPGPADRDRPAAPAPAPTLARGAGSGSGPQRAGSLKREKAEERLGSPAPAPRASARPFGSVGRRSRLAQ 504
Cdd:PHA03307    71 PPPGPGT-EAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPA 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  505 DFMAQCLQDSSPAQRPGPEKATPALPAPLTPRGA-SPVAPSTLPPPSTDPQVTKARKQEEDDSLSDAGTYTIETEAQDQE 583
Cdd:PHA03307   150 ASPPAAGASPAAVASDAASSRQAALPLSSPEETArAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  584 VEEARKMIDQVF---------GVLEAPELSRASSATFRPVIRGDRDEPGDGVAQRMALLQEFASRPVGVPPQVELQGLPV 654
Cdd:PHA03307   230 DDAGASSSDSSSsessgcgwgPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAP 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  655 PGSPGGQKWVSRWASLADSYSDPGLSEDGPGRRTGELEGALPVRQRrllpqlPSDRADSPAGPEAARKSGPGPpelgseq 734
Cdd:PHA03307   310 SSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSR------PPPPADPSSPRKRPRPSRAPS------- 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  735 aglllgqedlepdslsdASGSDGGRGPEPSRGPQEGQAWTRGRRSPRGPGEPAPTTFFIGDQNGEAALPKKPPVAPREAE 814
Cdd:PHA03307   377 -----------------SPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTPSGEP 439
                          410
                   ....*....|...
gi 1811067939  815 GPGrvAQPSPPAR 827
Cdd:PHA03307   440 WPG--SPPPPPGR 450
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
24-90 4.22e-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: 46.72  E-value: 4.22e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811067939   24 FVGRED--CELMLQSRSVDKQHAVINYDQDrDEHWVKDLGSLNGTFVNDVRIPDQKyvTLKLNDVIRFG 90
Cdd:cd22696     24 FIGKDPtvCDIVLQDPSISRQHARLSIDQD-NRVFIEDLSSKNGVLVNGKPIEGKE--EISGSDVISLG 89
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
12-90 1.29e-05

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: 45.45  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   12 SGTRHRLPRELIFVGRE-DCELMLQSRSVDKQHAviNYDQDRDEHWVKDLGSLNGTFVNDVRIPDqkyVTLKLNDVIRFG 90
Cdd:cd22684     12 AGARFLLDQDVTTAGRHpESDIFLDDVTVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERIDS---AVLRNGDEVQIG 86
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
8-90 1.91e-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: 44.76  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    8 LVSSSGTRHRLPRELIFVGR-EDCELMLQSRSVDKQHAVINYDQDrdEHWVKDLGSLNGTFVNDVRIpdQKYVTLKLNDV 86
Cdd:cd22668      5 LDDGSGRVYQLREGSNIIGRgSDADFRLPDTGVSRRHAEIRWDGQ--VAHLTDLGSTNGTTVNNAPV--TPEWRLADGDV 80

                   ....
gi 1811067939   87 IRFG 90
Cdd:cd22668     81 ITLG 84
FHA_VPS64-like cd22695
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ...
10-104 2.29e-05

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: 45.76  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939   10 SSSGTRHRLPRELIFVGREDCELMLQSRSVDKQHAVINYDQDRDEHWVKDLGSLNGTFVNDVRIPDQKyVTLKLNDVIRF 89
Cdd:cd22695     36 SVNKNNSGSKRDLFSQQVRPDNGNFDSRVLSRNHACLSCDPTTGKVYIRDLKSSNGTFVNGQKIRQND-VELKVGDEVDL 114
                           90
                   ....*....|....*
gi 1811067939   90 GYDsnmyVLERVQHR 104
Cdd:cd22695    115 GTD----IDSKIEHR 125
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
23-90 3.98e-05

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: 44.06  E-value: 3.98e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811067939   23 IFVGRE-DCELMLQSRSVDKQHA--VINYDQDRdehwVKDLGSLNGTFVNDVRIPDQKYVTLKLNDVIRFG 90
Cdd:cd22682     22 IVIGRSvESQVQIDDDSVSRYHAklAVNPSAVS----IIDLGSTNGTIVNGKKIPKLASCDLQNGDQIKIG 88
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
22-92 4.17e-05

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: 44.57  E-value: 4.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811067939   22 LIFvgreDCELMlqSRsvdkQHAVINYDqdRDEHWVKDLGSLNGTFVNDVRI-PDQKYVT---LKLNDVIRFGYD 92
Cdd:cd22679     42 AIF----DCKVL--SR----NHALLWYD--DGKFYLQDTKSSNGTFVNNQRLsKGSEESEpreLHSGDIVQFGVD 104
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
8-90 6.06e-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: 47.45  E-value: 6.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939    8 LVSSSGTRHRLPRELIFVGR-EDCELMLQ--SRSVDKQHAVINYDqdRDEHWVKDLgSLNGTFVN--DVRIPDQKYVTLK 82
Cdd:COG3456     13 LESGSAASATFGRGGGTIGRsADCDWVLPdpDRSVSRRHAEIRFR--DGAFCLTDL-STNGTFLNgsDHPLGPGRPVRLR 89

                   ....*...
gi 1811067939   83 LNDVIRFG 90
Cdd:COG3456     90 DGDRLRIG 97
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
25-94 6.53e-05

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: 43.82  E-value: 6.53e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811067939   25 VGR-EDCEL-MLQSRSVDKQHAVINYDQDrDEHWVKDLgSLNGTFVNDVRIPDQKYVTLKLNDVIRFGYDSN 94
Cdd:cd22672     25 IGRaKDCDLsFPGNKLVSGDHCKIIRDEK-GQVWLEDT-STNGTLVNKVKVVKGQKVELKHGDVIYLVYRKN 94
PHA03247 PHA03247
large tegument protein UL36; Provisional
620-1088 6.73e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  620 DEP-GDGVAQRMAL----LQEFASRPVGVPPQVeLQGLPVPGSPGGQKWVSRwasladsysdPGLSEDGPGRRTGELEGA 694
Cdd:PHA03247  2522 DEPvGEPVHPRMLTwirgLEELASDDAGDPPPP-LPPAAPPAAPDRSVPPPR----------PAPRPSEPAVTSRARRPD 2590
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  695 LPVRQRRllPQLPSDRADSPAGPEAARKSGPG------PPELGSEQAGLLLGQEDL-EPDSLSDASGSDGGRGPEPSRGP 767
Cdd:PHA03247  2591 APPQSAR--PRAPVDDRGDPRGPAPPSPLPPDthapdpPPPSPSPAANEPDPHPPPtVPPPERPRDDPAPGRVSRPRRAR 2668
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  768 QEGQAwTRGRRSPRGPGEPApttffIGDQNGEAALPKKPPVAPREAEGPGRVAQPSPPARDGMYVStsgrmviqlRTERS 847
Cdd:PHA03247  2669 RLGRA-AQASSPPQRPRRRA-----ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA---------RQASP 2733
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  848 PEPESSCPAPPKEALAfvrqdsftkepTSGSAAPGQLPHIPSHPLLQDLAAARAScvdlhsqdthlilketetaLAALEA 927
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPA-----------TPGGPARPARPPTTAGPPAPAPPAAPAA-------------------GPPRRL 2783
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  928 RLLSKSVEGPEGEMGSAPRPPEDSLSGDSDVDTSSTVSLLSGKNGPSPTGPQPTGLRKEKAPSPPAVQDPGTVALSSARE 1007
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939 1008 RlsekqRHPLGLPDVGRGEPTRRPVMRRSHGPQGSRDWPEEEQGSSLAHLPSADMVTSDHETPTATGAGRPGPRRKPMAP 1087
Cdd:PHA03247  2864 R-----RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938

                   .
gi 1811067939 1088 P 1088
Cdd:PHA03247  2939 P 2939
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
482-829 9.68e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.47  E-value: 9.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  482 PAPAPRASARPFGSVGRRSRLAQDFMAQCLQDSSPAQRPGPEKATPALPAPLTPRGASPVAPSTLPPPSTDPQVTKARKQ 561
Cdd:PHA03307    61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRP 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  562 EEDDSLSDAGTYTIETEAQDQEVEEARKMIDQVFGVLEAPELSRA-SSATFRPVIRGDRDEPGDGVAQRMALLQEFASRP 640
Cdd:PHA03307   141 VGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARApSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  641 VGVPPqvELQGLPVPGSPGGQKWVSRWASLADSYSDPGLSEDGPGRR-TGELEGALPVRQRRLLPQLPSDRADSPAGPEA 719
Cdd:PHA03307   221 APAPG--RSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLpTRIWEASGWNGPSSRPGPASSSSSPRERSPSP 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  720 AR-KSGPGPPELGSEQAGLLLGQEDLEPDSLSDASGSDGGRGPEPSRGPQEGQAWTRGRRSPRGPGEPAPTTFFIGDQNG 798
Cdd:PHA03307   299 SPsSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSP 378
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1811067939  799 EAALPKKPPVAPREAEGPGRVAQPSPPARDG 829
Cdd:PHA03307   379 AASAGRPTRRRARAAVAGRARRRDATGRFPA 409
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
458-828 1.69e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  458 AGSGSGPQRAGSLKREKAeerlGSPAPAPRASARPFGSVGRRSRLAQDFMAQclqdSSPAQRPGPEKATPALPAPLTPRG 537
Cdd:PRK07764   388 AGGAGAPAAAAPSAAAAA----PAAAPAPAAAAPAAAAAPAPAAAPQPAPAP----APAPAPPSPAGNAPAGGAPSPPPA 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  538 ASPVAPSTLPPPSTDPQVTKARKQEEDDSLSDAGTYTIETEAQDQ---EVEEARKMIDQVFGVLeaPELSRASSATFRP- 613
Cdd:PRK07764   460 AAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAgadDAATLRERWPEILAAV--PKRSRKTWAILLPe 537
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  614 -VIRGDRDE------PGDGVAQRMA------LLQEFASRPVGVPPQVELQGLPVPGSPGGQK----WVSRWASLADSYSD 676
Cdd:PRK07764   538 aTVLGVRGDtlvlgfSTGGLARRFAspgnaeVLVTALAEELGGDWQVEAVVGPAPGAAGGEGppapASSGPPEEAARPAA 617
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  677 PGLSED--GPGRRTGELEGALPVRQRRLLPQLPSDRADSPAGPEAARKSGPGPPELGSEQ----------AGLLLGQEDL 744
Cdd:PRK07764   618 PAAPAApaAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAApaapppapapAAPAAPAGAA 697
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  745 EPDSLSDASGSDGGRGPEPSRGPQEGQAWTRGRRSPRG----PGEPAPTTFFIGDQNGEAALPKKPPVAPREAEGPGRVA 820
Cdd:PRK07764   698 PAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAAddpvPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPS 777

                   ....*...
gi 1811067939  821 QPSPPARD 828
Cdd:PRK07764   778 PPSEEEEM 785
PHA03378 PHA03378
EBNA-3B; Provisional
512-898 7.37e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 7.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  512 QDSSPAQRPGPEKATPALPAPLTPRGASPVAPSTLP------PPSTDPQVTKARKQEEDDSLSDAGTYTIETEAQDQEVE 585
Cdd:PHA03378   437 RTEQPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQaplepwQPLPHPQVTPVILHQPPAQGVQAHGSMLDLLEKDDEDM 516
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  586 EARKMIDQVFGVLEAPELSRASSATFRPVIRGDRDEPGDGVAQRMALLqefasrPVGVPPQVELQGLPVPGSPGGQKWVS 665
Cdd:PHA03378   517 EQRVMATLLPPSPPQPRAGRRAPCVYTEDLDIESDEPASTEPVHDQLL------PAPGLGPLQIQPLTSPTTSQLASSAP 590
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  666 RWASLADSYSDPGLSEDGPGRRTGELEGALPVRQRRLLPQLPSDRADSPAGP--EAARKSGPGPPELGSEQAGLLLGQED 743
Cdd:PHA03378   591 SYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITfnVLVFPTPHQPPQVEITPYKPTWTQIG 670
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  744 LEPDSLSDAsgsdggrGPEPSRGPQegQAWTRGRRSPRGPGEPAPttffigdqngeaalPKKPPVA---PREAEGPGRVA 820
Cdd:PHA03378   671 HIPYQPSPT-------GANTMLPIQ--WAPGTMQPPPRAPTPMRP--------------PAAPPGRaqrPAAATGRARPP 727
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811067939  821 QPSP-PARDGMYVSTSGRMVIQLRTERSPEPESSCPAPPKEAlafvrqdsftkepTSGSAAPGQLPHIPSHPLLQDLAA 898
Cdd:PHA03378   728 AAAPgRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAA-------------APGAPTPQPPPQAPPAPQQRPRGA 793
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
480-762 1.15e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  480 GSPAPAPRASARPfgsvgrRSRLAQDFMAQCLQDSSPAQRPGPEKATPALPAPLTPRGASPVAPSTLPPPSTDpQVTKAR 559
Cdd:PRK07003   371 GVPARVAGAVPAP------GARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATAD-RGDDAA 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  560 KQEEDDSLSDAGTYTIETEAQDQEVEEARKMIDQVFGVLEAPELSRASSATfrpviRGDRDEPGDGVAQRMALLQEFASR 639
Cdd:PRK07003   444 DGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAP-----RAAAPSAATPAAVPDARAPAAASR 518
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  640 PVGVPPQVELQGLPVPGSPGGQKWVSRWASLADSY-----------SDPGLSEDGPGRRTGELEGALPVRQRRLLPQLPS 708
Cdd:PRK07003   519 EDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAALdvlrnagmrvsSDRGARAAAAAKPAAAPAAAPKPAAPRVAVQVPT 598
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1811067939  709 DRADSPAGPEAARKSGPGPPelGSEQAGLLLGQEDLEPDSLSDASGSDGGRGPE 762
Cdd:PRK07003   599 PRARAATGDAPPNGAARAEQ--AAESRGAPPPWEDIPPDDYVPLSADEGFGGPD 650
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
482-593 2.03e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.84  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  482 PAPAPRASARPFGSVGRRsrlaqdfmaqclQDSSPAQRPGPEKATPALPAPLT----PRGASPVAPSTLPPPSTDPQVTK 557
Cdd:PRK14971   386 PAAAPQPSAAAAASPSPS------------QSSAAAQPSAPQSATQPAGTPPTvsvdPPAAVPVNPPSTAPQAVRPAQFK 453
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1811067939  558 ARKQEEDDSLSDAGTYTI-----ETEAQDQEVEEARKMIDQ 593
Cdd:PRK14971   454 EEKKIPVSKVSSLGPSTLrpiqeKAEQATGNIKEAPTGTQK 494
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
462-754 5.38e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  462 SGPQRAGSLKREKAEERLGSPAPAPRASARPFGSVGRRSRLAQDfMAQCLQDSSPAQRPGPEKatpalpaPLTP-RGASP 540
Cdd:PTZ00449   580 EFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKS-PKRPESPKSPKRPPPPQR-------PSSPeRPEGP 651
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  541 VAP-STLPPPSTDPQVTKARKQEEDDSLSDAGTYTIETEAQDQEVEEARKMIDQVFGVLEA----------PELSRASSA 609
Cdd:PTZ00449   652 KIIkSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGtpfttprplpPKLPRDEEF 731
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  610 TFRPVIRGDRDEPGDgvaqrmallQEFASRPvgVPPQVELQGLPVPGSPGGqkwvsrwaSLADSYSDPGLSEDgpgrrTG 689
Cdd:PTZ00449   732 PFEPIGDPDAEQPDD---------IEFFTPP--EEERTFFHETPADTPLPD--------ILAEEFKEEDIHAE-----TG 787
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811067939  690 ELEGALpvrqRRllPQLPSDRADSPAGpeaarkSGPGPPELGSEQAGLLLGQEDLEPDS---LSDASG 754
Cdd:PTZ00449   788 EPDEAM----KR--PDSPSEHEDKPPG------DHPSLPKKRHRLDGLALSTTDLESDAgriAKDASG 843
PRK10263 PRK10263
DNA translocase FtsK; Provisional
126-254 7.81e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  126 PAPKRGEalPGHTPHCESSAPRPERGDRRPgAEAAAYRTPLYGQPSWWGEDEGTLPEYPrQEEPCMERPKELAQKDGDLT 205
Cdd:PRK10263   364 PGPQTGE--PVIAPAPEGYPQQSQYAQPAV-QYNEPLQQPVQPQQPYYAPAAEQPAQQP-YYAPAPEQPAQQPYYAPAPE 439
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1811067939  206 GTVAGFRAPAEPQGYSFRREPSY-FEIPTKETPPPRPLEVPVHEAPPRDV 254
Cdd:PRK10263   440 QPVAGNAWQAEEQQSTFAPQSTYqTEQTYQQPAAQEPLYQQPQPVEQQPV 489
PHA03247 PHA03247
large tegument protein UL36; Provisional
414-975 8.31e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 8.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  414 RKKRSQSFTHTPPGDPRPDRRRGPGPADRDRPAAPAPA----------------------PTLARGAGSGSGPQRAGSLK 471
Cdd:PHA03247  2481 RRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdepvgepvhprmltwirglEELASDDAGDPPPPLPPAAP 2560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  472 REKAEERLGSPAPAPRASARPFGSVGRRSrlaqDFMAQCLQDSSPAQRPGPEKATPAlPAPLTPRGASPVAPSTLPPPS- 550
Cdd:PHA03247  2561 PAAPDRSVPPPRPAPRPSEPAVTSRARRP----DAPPQSARPRAPVDDRGDPRGPAP-PSPLPPDTHAPDPPPPSPSPAa 2635
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  551 ---TDPQVTKARKQEEDDSLSDAGTYTIETEAQDQEVEEARKMIDQVFGVLEAPELSRASSATFRPVIRGDRDEPGDGVA 627
Cdd:PHA03247  2636 nepDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHAL 2715
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  628 QRMALLQEFASRPVGVPPQVELQGLP-----VPGSPGGQKWVSRWASLA--DSYSDPGLSEDGPGRRTGELEGALPVRQR 700
Cdd:PHA03247  2716 VSATPLPPGPAAARQASPALPAAPAPpavpaGPATPGGPARPARPPTTAgpPAPAPPAAPAAGPPRRLTRPAVASLSESR 2795
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  701 RLLPqLPSDRADSPAG--------PEAARKSGPGPPELGSEQAGLLLGQEDLEPDSLSDASGSDGG--RGPEPSRGPQEG 770
Cdd:PHA03247  2796 ESLP-SPWDPADPPAAvlapaaalPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGdvRRRPPSRSPAAK 2874
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  771 QAWT---RGRRSPRGPGEPAPTTFFIGDQNGEAALPKKPPVAPREAEGPGRVAQPSPPARdgmyvsTSGRMVIQL----R 843
Cdd:PHA03247  2875 PAAParpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP------PPPRPQPPLapttD 2948
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811067939  844 TERSPEPESSCPAPPKEALAFVRQdSFTKEPTSGSAAPGQLPHIPSHPlLQDLAAAR----ASCVDLHSQDTH--LILKE 917
Cdd:PHA03247  2949 PAGAGEPSGAVPQPWLGALVPGRV-AVPRFRVPQPAPSREAPASSTPP-LTGHSLSRvsswASSLALHEETDPppVSLKQ 3026
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811067939  918 T-----ETALAALEARLLSKSVEGPEGEMGSAPRPPEDSLSGDSDVDTSSTVSLLSGKN--GPSP 975
Cdd:PHA03247  3027 TlwppdDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSqfGPPP 3091
 
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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