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Conserved domains on  [gi|2207671062|gb|UNC91103|]
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type VII secretion protein EssC [Candidatus Contubernalis alkalaceticus]

Protein Classification

FHA and TrwB_TraG_TraD_VirD4 domain-containing protein( domain architecture ID 12811272)

FHA and TrwB_TraG_TraD_VirD4 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
T7_EssCb_Firm super family cl37349
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
227-1548 0e+00

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


The actual alignment was detected with superfamily member TIGR03928:

Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 1068.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  227 YYQQSPRRIELLDDETIEIEAPPN-PNLSRRQpLIFTIGPSMTMVIpmATGVLFAMwsvqqtnhtmtSPFMFMgIITSVT 305
Cdd:TIGR03928    5 DYHRSPRIIYEEPTDKVKISKPPQePDKPKRG-LLRIILPPLVMIA--VTVLISIF-----------QPRGIF-IIASIA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  306 AAFIGVFWALTNYNYNKSIERESEERRCVLFRKYLDKIRRLLSQKHSYNKEILDKKYPETHECLRFMQVNSRRLWERNVN 385
Cdd:TIGR03928   70 MSLVTIIFSTTTYFREKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPSVEELKEMVENVNSRIWEKTPE 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  386 HLDFLTIRLGRGDMISPNAVTIPKERFSLIDDVLAEEPLNIKNEYRKLKEIPVCISLReHLLVGVIGDSmNTCISTVQVM 465
Cdd:TIGR03928  150 HHDFLHVRLGTGNVPSSFEIKFPEEEFSQRKDELLDEAQELKEKYNTIENVPIVLDLS-NGPIGYVGKR-SLVLEELQNL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  466 AAQIAAYHCYTDVKMVFIFNEKDTALFEFPKWLPHTWSLDGSLRMMACDSNGVGEVFYHLSDLLRQRLDERD--NPAEAV 543
Cdd:TIGR03928  228 VGQLAFFHSYHDVQFVTIFPEEEKKKWEWMRWLPHFWLRDINVRGFVYNERTRDQLLNSLYQILKERKLALDdaNSKEKK 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  544 RPLPHYVVFITDPSLVENEAVMKHLLAPTEQMGISTVLLYGQIGQLPNNCTVIIQNDNEYSGYYSLDSSFTGYEDVTIDY 623
Cdd:TIGR03928  308 RFSPHYVFLITDRKLILDHVIMEYLNEDPSELGISLIFVQDVMESLPENVKTVIDIKNRNEGEIVLEEGELVEKSFTPDH 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  624 VEETMLSSFARGLSGVRVREvHSAGAIPEMLTFLDMYKTTRLEDIDIQRRWLENRTYESMKAIIGYRGADTPLYLDIHEK 703
Cdd:TIGR03928  388 LDNEDLEEYSRTLAPLNHLQ-NLKNSIPESVTFLEMYGVKKVEELNIQERWAKNETYKSLAVPIGLRGKDDIVYLNLHEK 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  704 YHGPHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKGGGMAGSFEKLPHVAGIITNLGGNQTNRALASINSE 783
Cdd:TIGR03928  467 AHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFKNLPHLLGTITNLDGAQSMRALASIKAE 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  784 IKRRQAIFNEFKIKHIDTYIEIYRSGKATIPMPHLLIIADEFAELKKEQPEFVRELVSASRVGRSLGVHLILATQKPSGV 863
Cdd:TIGR03928  547 LKKRQRLFGENNVNHINQYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMKELVSTARIGRSLGVHLILATQKPSGV 626
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  864 VDDEIWGNSKSRLCLRVQDKQDSNEMIKRPDAAYITNAGRGFFQVGNDEIFEAFQSGWSGAPYEPEtqysDEKQGDVKI- 942
Cdd:TIGR03928  627 VDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRAYLQVGNNEVYELFQSAWSGAPYDPD----KDKKEEEDIy 702
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  943 -INLWGKPQV--VRSKKTAPQEEKAKKQTQLEAAVLHIAEISEKQNIRPIDNIWLPPLPVRICLQDIEEYTERAffngAW 1019
Cdd:TIGR03928  703 mINDLGQYELlnEDLSGLKRKKEIKEVPTELEAVIDEIQAYTEELNIEALPSPWLPPLEEKIYLDDLHAVEFDK----LW 778
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1020 EKTPWELKPAVGIVDDPVNQRQIPLIIDLLTEGHLLISGSG--GKTTFLQTLLYSLVTTYSPNRFNLYIADYGSRTMGVF 1097
Cdd:TIGR03928  779 SKPKEPLQATIGLLDDPELQSQEPLTLDLSKDGHLAIFGSPgyGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPL 858
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1098 GVLPHVGGVVFDNETDKINKLIAMLIKELNKRKVVFSEKGIGSFKEYVRLYDD-VPAIVLAVDNFAAFNDNCPMQ--EDN 1174
Cdd:TIGR03928  859 KKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASGEkLPQIVIIIDNYDAVKEEPFYEdfEEL 938
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1175 MVMLSREAASYGIYLVITCTNINDIRNKIRQNIGFGIGLQLADRFEYEEVLNeKTDITAENkIPGRGLVCYPKPLEFQTA 1254
Cdd:TIGR03928  939 LIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLIDKSEYRSIVG-RTKFTIEE-IPGRGLIKKDEPTLFQTA 1016
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1255 LCLSAGDAVELNMTLKKQFDIITNSWQGKKAPVIPQVPEDMSLNSFLLLPEVAKILQGSRYlPLGYDLAGASLESIDLAK 1334
Cdd:TIGR03928 1017 LPVKGEDDLEVIENIKAEIQKMNEAWTGERPKPIPMVPEELSLEEFRERYEVRKILEEGSI-PIGLDEETVEPVYIDLTE 1095
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1335 TYCYSISGTGRSGKTNLLKAF-MIMAKSQGSKVYVFDGTARELESFSWEIATDNYMVTSDELFDFMQmTLLPEFTRRNEG 1413
Cdd:TIGR03928 1096 NPHLLIVGESDDGKTNVLKSLlKTLAKQEKEKIGLIDSIDRGLLAYRDLKEVATYIEEKEDLKEILA-ELKEEIELREAA 1174
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1414 KAEFIKNGRKDVdeylkSEQKIYLFIGEITAFCEAVYSSQRDMkgfMEQMVSRGDQHIVYLFACISQSdmlgELSMKR-- 1491
Cdd:TIGR03928 1175 YKEALQNETGEP-----AFKPILLIIDDLEDFIQRTDLEIQDI---LALIMKNGKKLGIHFIVAGTHS----ELSKSYdg 1242
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2207671062 1492 LMRGFVSWKEGIhLGGDVEHQRLFDFdvPVMERSKKLPSGIGQTIIDGVTKKVVTPE 1548
Cdd:TIGR03928 1243 VPKEIKQLRTGI-LGMRKSDQSFFKL--PFTRSEKELEPGEGYFVVNGKYQKIKIPE 1296
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
108-180 9.22e-18

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


:

Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 80.00  E-value: 9.22e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  108 YILNHSRITIGSAEGNSIIYNNRnLVSRKHTVIERDaNGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIYI 180
Cdd:COG1716     16 FPLDGGPLTIGRAPDNDIVLDDP-TVSRRHARIRRD-GGGWVLEDLGSTNGTFVNGQRVTEPAPLRDGDVIRL 86
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
227-1548 0e+00

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 1068.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  227 YYQQSPRRIELLDDETIEIEAPPN-PNLSRRQpLIFTIGPSMTMVIpmATGVLFAMwsvqqtnhtmtSPFMFMgIITSVT 305
Cdd:TIGR03928    5 DYHRSPRIIYEEPTDKVKISKPPQePDKPKRG-LLRIILPPLVMIA--VTVLISIF-----------QPRGIF-IIASIA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  306 AAFIGVFWALTNYNYNKSIERESEERRCVLFRKYLDKIRRLLSQKHSYNKEILDKKYPETHECLRFMQVNSRRLWERNVN 385
Cdd:TIGR03928   70 MSLVTIIFSTTTYFREKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPSVEELKEMVENVNSRIWEKTPE 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  386 HLDFLTIRLGRGDMISPNAVTIPKERFSLIDDVLAEEPLNIKNEYRKLKEIPVCISLReHLLVGVIGDSmNTCISTVQVM 465
Cdd:TIGR03928  150 HHDFLHVRLGTGNVPSSFEIKFPEEEFSQRKDELLDEAQELKEKYNTIENVPIVLDLS-NGPIGYVGKR-SLVLEELQNL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  466 AAQIAAYHCYTDVKMVFIFNEKDTALFEFPKWLPHTWSLDGSLRMMACDSNGVGEVFYHLSDLLRQRLDERD--NPAEAV 543
Cdd:TIGR03928  228 VGQLAFFHSYHDVQFVTIFPEEEKKKWEWMRWLPHFWLRDINVRGFVYNERTRDQLLNSLYQILKERKLALDdaNSKEKK 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  544 RPLPHYVVFITDPSLVENEAVMKHLLAPTEQMGISTVLLYGQIGQLPNNCTVIIQNDNEYSGYYSLDSSFTGYEDVTIDY 623
Cdd:TIGR03928  308 RFSPHYVFLITDRKLILDHVIMEYLNEDPSELGISLIFVQDVMESLPENVKTVIDIKNRNEGEIVLEEGELVEKSFTPDH 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  624 VEETMLSSFARGLSGVRVREvHSAGAIPEMLTFLDMYKTTRLEDIDIQRRWLENRTYESMKAIIGYRGADTPLYLDIHEK 703
Cdd:TIGR03928  388 LDNEDLEEYSRTLAPLNHLQ-NLKNSIPESVTFLEMYGVKKVEELNIQERWAKNETYKSLAVPIGLRGKDDIVYLNLHEK 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  704 YHGPHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKGGGMAGSFEKLPHVAGIITNLGGNQTNRALASINSE 783
Cdd:TIGR03928  467 AHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFKNLPHLLGTITNLDGAQSMRALASIKAE 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  784 IKRRQAIFNEFKIKHIDTYIEIYRSGKATIPMPHLLIIADEFAELKKEQPEFVRELVSASRVGRSLGVHLILATQKPSGV 863
Cdd:TIGR03928  547 LKKRQRLFGENNVNHINQYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMKELVSTARIGRSLGVHLILATQKPSGV 626
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  864 VDDEIWGNSKSRLCLRVQDKQDSNEMIKRPDAAYITNAGRGFFQVGNDEIFEAFQSGWSGAPYEPEtqysDEKQGDVKI- 942
Cdd:TIGR03928  627 VDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRAYLQVGNNEVYELFQSAWSGAPYDPD----KDKKEEEDIy 702
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  943 -INLWGKPQV--VRSKKTAPQEEKAKKQTQLEAAVLHIAEISEKQNIRPIDNIWLPPLPVRICLQDIEEYTERAffngAW 1019
Cdd:TIGR03928  703 mINDLGQYELlnEDLSGLKRKKEIKEVPTELEAVIDEIQAYTEELNIEALPSPWLPPLEEKIYLDDLHAVEFDK----LW 778
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1020 EKTPWELKPAVGIVDDPVNQRQIPLIIDLLTEGHLLISGSG--GKTTFLQTLLYSLVTTYSPNRFNLYIADYGSRTMGVF 1097
Cdd:TIGR03928  779 SKPKEPLQATIGLLDDPELQSQEPLTLDLSKDGHLAIFGSPgyGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPL 858
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1098 GVLPHVGGVVFDNETDKINKLIAMLIKELNKRKVVFSEKGIGSFKEYVRLYDD-VPAIVLAVDNFAAFNDNCPMQ--EDN 1174
Cdd:TIGR03928  859 KKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASGEkLPQIVIIIDNYDAVKEEPFYEdfEEL 938
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1175 MVMLSREAASYGIYLVITCTNINDIRNKIRQNIGFGIGLQLADRFEYEEVLNeKTDITAENkIPGRGLVCYPKPLEFQTA 1254
Cdd:TIGR03928  939 LIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLIDKSEYRSIVG-RTKFTIEE-IPGRGLIKKDEPTLFQTA 1016
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1255 LCLSAGDAVELNMTLKKQFDIITNSWQGKKAPVIPQVPEDMSLNSFLLLPEVAKILQGSRYlPLGYDLAGASLESIDLAK 1334
Cdd:TIGR03928 1017 LPVKGEDDLEVIENIKAEIQKMNEAWTGERPKPIPMVPEELSLEEFRERYEVRKILEEGSI-PIGLDEETVEPVYIDLTE 1095
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1335 TYCYSISGTGRSGKTNLLKAF-MIMAKSQGSKVYVFDGTARELESFSWEIATDNYMVTSDELFDFMQmTLLPEFTRRNEG 1413
Cdd:TIGR03928 1096 NPHLLIVGESDDGKTNVLKSLlKTLAKQEKEKIGLIDSIDRGLLAYRDLKEVATYIEEKEDLKEILA-ELKEEIELREAA 1174
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1414 KAEFIKNGRKDVdeylkSEQKIYLFIGEITAFCEAVYSSQRDMkgfMEQMVSRGDQHIVYLFACISQSdmlgELSMKR-- 1491
Cdd:TIGR03928 1175 YKEALQNETGEP-----AFKPILLIIDDLEDFIQRTDLEIQDI---LALIMKNGKKLGIHFIVAGTHS----ELSKSYdg 1242
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2207671062 1492 LMRGFVSWKEGIhLGGDVEHQRLFDFdvPVMERSKKLPSGIGQTIIDGVTKKVVTPE 1548
Cdd:TIGR03928 1243 VPKEIKQLRTGI-LGMRKSDQSFFKL--PFTRSEKELEPGEGYFVVNGKYQKIKIPE 1296
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
669-861 1.29e-31

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 124.03  E-value: 1.29e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  669 DIQRRWLENRTYESMKAIIGYRGADTPLYLDihEKYHGPHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKG 748
Cdd:pfam01580    3 EVLESKPFDTDYSRLPIALGKDISGNPEVFD--LKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  749 GGMaGSFEKLPHV--AGIITNLGGnqTNRALASINSEIKRRQAIFNEFKIKHIDTY-----------------------I 803
Cdd:pfam01580   81 GEL-SAYEDIPHLlsVPVATDPKR--ALRALEWLVDEMERRYALFRALGVRSIAGYngeiaedpldgfgdvflviygvhV 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  804 EIYRSGKATIPmPHLLIIADEFAELK----KEQPEFVRELVS-ASRVGRSLGVHLILATQKPS 861
Cdd:pfam01580  158 MCTAGRWLEIL-PYLVVIVDERAELRlaapKDSEMRVEDAIVrLAQKGRAAGIHLLLATQRPS 219
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
707-886 2.91e-25

DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441280 [Multi-domain]  Cd Length: 611  Bit Score: 113.10  E-value: 2.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  707 PHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKgggMA--GSFEKLPH-VAGIITNLggNQTNRALASINSE 783
Cdd:COG1674    282 PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPK---MVelSVYNGIPHlLTPVVTDP--KKAANALKWAVRE 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  784 IKRRQAIFNEFKIKHIDTYIEIYRSGKATI-------PMPHLLIIADEFAEL----KKEqpefVRELVsaSRV---GRSL 849
Cdd:COG1674    357 MERRYKLFAKAGVRNIAGYNEKVREAKAKGeeeeglePLPYIVVIIDELADLmmvaGKE----VEEAI--ARLaqkARAA 430
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2207671062  850 GVHLILATQKPS-GVVDDEIWGNSKSRLCLRVQDKQDS 886
Cdd:COG1674    431 GIHLILATQRPSvDVITGLIKANIPSRIAFAVSSKIDS 468
PRK10263 PRK10263
DNA translocase FtsK; Provisional
632-902 1.21e-20

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 99.39  E-value: 1.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  632 FARGLSGVRVREVHSAGAIPEMLTFLDMYK--TTRLEDIDIQRRWLENRTyeSMKAIIGYRGADTPLYLDIHEKyhgPHG 709
Cdd:PRK10263   939 LARSLSTVAVRVVEVIPGKPYVGLELPNKKrqTVYLREVLDNAKFRDNPS--PLTVVLGKDIAGEPVVADLAKM---PHL 1013
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  710 LVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKGGGMAgSFEKLPH-VAGIITNLgGNQTNRALASINsEIKRRQ 788
Cdd:PRK10263  1014 LVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELS-VYEGIPHlLTEVVTDM-KDAANALRWCVN-EMERRY 1090
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  789 AIFNEFKIKHIDTY----IEIYRSGKAtIP-------------------MPHLLIIADEFAELKKEQPEFVRELVSA-SR 844
Cdd:PRK10263  1091 KLMSALGVRNLAGYnekiAEADRMMRP-IPdpywkpgdsmdaqhpvlkkEPYIVVLVDEFADLMMTVGKKVEELIARlAQ 1169
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2207671062  845 VGRSLGVHLILATQKPS-GVVDDEIWGNSKSRLCLRVQDKQDSNEMIKRPDAAYITNAG 902
Cdd:PRK10263  1170 KARAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMG 1228
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
108-180 9.22e-18

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 80.00  E-value: 9.22e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  108 YILNHSRITIGSAEGNSIIYNNRnLVSRKHTVIERDaNGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIYI 180
Cdd:COG1716     16 FPLDGGPLTIGRAPDNDIVLDDP-TVSRRHARIRRD-GGGWVLEDLGSTNGTFVNGQRVTEPAPLRDGDVIRL 86
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
107-187 1.38e-17

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


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 79.24  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  107 KYILNHSRITIGSAEGNSIIYNNRNlVSRKHTVIERDaNGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIYIIGLKIV 186
Cdd:cd00060     13 EFPLTKGVVTIGRSPDCDIVLDDPS-VSRRHARIEVD-GGGVYLEDLGSTNGTFVNGKRITPPVPLQDGDVIRLGDTTFR 90

                   .
gi 2207671062  187 Y 187
Cdd:cd00060     91 F 91
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
115-180 4.47e-14

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 68.37  E-value: 4.47e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2207671062  115 ITIGSAEGNSIIYNNRnLVSRKHTVIERDANGNYFVIDQKSSNSTFVNGRRILG-SHKLSYGDVIYI 180
Cdd:pfam00498    1 VTIGRSPDCDIVLDDP-SVSRRHAEIRYDGGGRFYLEDLGSTNGTFVNGQRLGPePVRLKDGDVIRL 66
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
708-880 4.78e-09

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 56.46  E-value: 4.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  708 HGLVAGTTGSGKSetlqTYILSLALNYHPYEVSFILIDYKGggmagsfeklphvAGIITNLGGNQTNRALASInseikrr 787
Cdd:cd01127      1 NTLVLGTTGSGKT----TSIVIPLLDQAARGGSVIITDPKG-------------ELFLVIPDRDDSFAALRAL------- 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  788 qaIFNefkikHIDTYIEIYRSGKATIPMPHLLIIADEFAELKKeqpefVRELVSASRVGRSLGVHLILATQ------KPS 861
Cdd:cd01127     57 --FFN-----QLFRALTELASLSPGRLPRRVWFILDEFANLGR-----IPNLPNLLATGRKRGISVVLILQslaqleAVY 124
                          170       180
                   ....*....|....*....|
gi 2207671062  862 GVVDDE-IWGNSKSRLCLRV 880
Cdd:cd01127    125 GKDGAQtILGNCNTKLYLGT 144
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
115-166 1.76e-08

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 51.80  E-value: 1.76e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2207671062   115 ITIGSAEGNSIIYNNRNLVSRKHTVIERDANGNYFVIDQKSSNSTFVNGRRI 166
Cdd:smart00240    1 VTIGRSSEDCDIQLDGPSISRRHAVIVYDGGGRFYLIDLGSTNGTFVNGKRI 52
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
227-1548 0e+00

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 1068.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  227 YYQQSPRRIELLDDETIEIEAPPN-PNLSRRQpLIFTIGPSMTMVIpmATGVLFAMwsvqqtnhtmtSPFMFMgIITSVT 305
Cdd:TIGR03928    5 DYHRSPRIIYEEPTDKVKISKPPQePDKPKRG-LLRIILPPLVMIA--VTVLISIF-----------QPRGIF-IIASIA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  306 AAFIGVFWALTNYNYNKSIERESEERRCVLFRKYLDKIRRLLSQKHSYNKEILDKKYPETHECLRFMQVNSRRLWERNVN 385
Cdd:TIGR03928   70 MSLVTIIFSTTTYFREKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPSVEELKEMVENVNSRIWEKTPE 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  386 HLDFLTIRLGRGDMISPNAVTIPKERFSLIDDVLAEEPLNIKNEYRKLKEIPVCISLReHLLVGVIGDSmNTCISTVQVM 465
Cdd:TIGR03928  150 HHDFLHVRLGTGNVPSSFEIKFPEEEFSQRKDELLDEAQELKEKYNTIENVPIVLDLS-NGPIGYVGKR-SLVLEELQNL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  466 AAQIAAYHCYTDVKMVFIFNEKDTALFEFPKWLPHTWSLDGSLRMMACDSNGVGEVFYHLSDLLRQRLDERD--NPAEAV 543
Cdd:TIGR03928  228 VGQLAFFHSYHDVQFVTIFPEEEKKKWEWMRWLPHFWLRDINVRGFVYNERTRDQLLNSLYQILKERKLALDdaNSKEKK 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  544 RPLPHYVVFITDPSLVENEAVMKHLLAPTEQMGISTVLLYGQIGQLPNNCTVIIQNDNEYSGYYSLDSSFTGYEDVTIDY 623
Cdd:TIGR03928  308 RFSPHYVFLITDRKLILDHVIMEYLNEDPSELGISLIFVQDVMESLPENVKTVIDIKNRNEGEIVLEEGELVEKSFTPDH 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  624 VEETMLSSFARGLSGVRVREvHSAGAIPEMLTFLDMYKTTRLEDIDIQRRWLENRTYESMKAIIGYRGADTPLYLDIHEK 703
Cdd:TIGR03928  388 LDNEDLEEYSRTLAPLNHLQ-NLKNSIPESVTFLEMYGVKKVEELNIQERWAKNETYKSLAVPIGLRGKDDIVYLNLHEK 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  704 YHGPHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKGGGMAGSFEKLPHVAGIITNLGGNQTNRALASINSE 783
Cdd:TIGR03928  467 AHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFKNLPHLLGTITNLDGAQSMRALASIKAE 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  784 IKRRQAIFNEFKIKHIDTYIEIYRSGKATIPMPHLLIIADEFAELKKEQPEFVRELVSASRVGRSLGVHLILATQKPSGV 863
Cdd:TIGR03928  547 LKKRQRLFGENNVNHINQYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMKELVSTARIGRSLGVHLILATQKPSGV 626
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  864 VDDEIWGNSKSRLCLRVQDKQDSNEMIKRPDAAYITNAGRGFFQVGNDEIFEAFQSGWSGAPYEPEtqysDEKQGDVKI- 942
Cdd:TIGR03928  627 VDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRAYLQVGNNEVYELFQSAWSGAPYDPD----KDKKEEEDIy 702
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  943 -INLWGKPQV--VRSKKTAPQEEKAKKQTQLEAAVLHIAEISEKQNIRPIDNIWLPPLPVRICLQDIEEYTERAffngAW 1019
Cdd:TIGR03928  703 mINDLGQYELlnEDLSGLKRKKEIKEVPTELEAVIDEIQAYTEELNIEALPSPWLPPLEEKIYLDDLHAVEFDK----LW 778
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1020 EKTPWELKPAVGIVDDPVNQRQIPLIIDLLTEGHLLISGSG--GKTTFLQTLLYSLVTTYSPNRFNLYIADYGSRTMGVF 1097
Cdd:TIGR03928  779 SKPKEPLQATIGLLDDPELQSQEPLTLDLSKDGHLAIFGSPgyGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPL 858
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1098 GVLPHVGGVVFDNETDKINKLIAMLIKELNKRKVVFSEKGIGSFKEYVRLYDD-VPAIVLAVDNFAAFNDNCPMQ--EDN 1174
Cdd:TIGR03928  859 KKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASGEkLPQIVIIIDNYDAVKEEPFYEdfEEL 938
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1175 MVMLSREAASYGIYLVITCTNINDIRNKIRQNIGFGIGLQLADRFEYEEVLNeKTDITAENkIPGRGLVCYPKPLEFQTA 1254
Cdd:TIGR03928  939 LIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLIDKSEYRSIVG-RTKFTIEE-IPGRGLIKKDEPTLFQTA 1016
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1255 LCLSAGDAVELNMTLKKQFDIITNSWQGKKAPVIPQVPEDMSLNSFLLLPEVAKILQGSRYlPLGYDLAGASLESIDLAK 1334
Cdd:TIGR03928 1017 LPVKGEDDLEVIENIKAEIQKMNEAWTGERPKPIPMVPEELSLEEFRERYEVRKILEEGSI-PIGLDEETVEPVYIDLTE 1095
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1335 TYCYSISGTGRSGKTNLLKAF-MIMAKSQGSKVYVFDGTARELESFSWEIATDNYMVTSDELFDFMQmTLLPEFTRRNEG 1413
Cdd:TIGR03928 1096 NPHLLIVGESDDGKTNVLKSLlKTLAKQEKEKIGLIDSIDRGLLAYRDLKEVATYIEEKEDLKEILA-ELKEEIELREAA 1174
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1414 KAEFIKNGRKDVdeylkSEQKIYLFIGEITAFCEAVYSSQRDMkgfMEQMVSRGDQHIVYLFACISQSdmlgELSMKR-- 1491
Cdd:TIGR03928 1175 YKEALQNETGEP-----AFKPILLIIDDLEDFIQRTDLEIQDI---LALIMKNGKKLGIHFIVAGTHS----ELSKSYdg 1242
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2207671062 1492 LMRGFVSWKEGIhLGGDVEHQRLFDFdvPVMERSKKLPSGIGQTIIDGVTKKVVTPE 1548
Cdd:TIGR03928 1243 VPKEIKQLRTGI-LGMRKSDQSFFKL--PFTRSEKELEPGEGYFVVNGKYQKIKIPE 1296
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
269-926 1.79e-83

type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274858 [Multi-domain]  Cd Length: 658  Bit Score: 288.80  E-value: 1.79e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  269 MVIPMATG-----VLFAMWSVQQTNhTMTSPFMFMGIITSVTAAFIGvfwalTNYNYNKSIERESEERRcvlFRKYLDKI 343
Cdd:TIGR03924    8 LPVVMVVAvvgmvVMMFASGGRQRN-PMFLIFPLMMLVSMLGMLAGG-----RGGGGKKTPELDEDRRD---YLRYLDQL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  344 RRLLSQKHSYNKEILDKKYPEThECLrFMQVNSRRLWERNVNHLDFLTIRLGRGDMisPNAVTIPKERFSLIDDVlaeEP 423
Cdd:TIGR03924   79 RREVRETAAAQRAALEWRHPDP-DTL-WALVGTPRMWERRPGDPDFLEVRVGVGVQ--PLATRLVVPETGPVEDL---EP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  424 LNIK------NEYRKLKEIPVCISLREHLLVGVIGDsMNTCISTVQVMAAQIAAYHCYTDVKMVFIFNEkDTALFEFPKW 497
Cdd:TIGR03924  152 VTAValrrflRAHSTVPDLPVAVSLRGFARISLVGD-RDQARALARAMLCQLAVFHGPDDVGIAVVTSD-PDRDWDWLKW 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  498 LPHTWS---LD--GSLRMMACDSNGvgevfyhLSDLLRQRLDER-DNPAEAVRPLPHYVVfITDPSLVENEAvmkhLLAP 571
Cdd:TIGR03924  230 LPHNQHptrFDaaGPARLVYTSLAE-------LEAALAELLADRgRFSPDDAASLPHLVV-VVDGGDLPGWE----DLIG 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  572 TEQMGISTVL-LYGQIGQLPNNCTVIIQNDNEYSGYYSLDSSFTgyEDVTIDYVEETMLSSFARGLSGVRVRE-VHSAGA 649
Cdd:TIGR03924  298 ESGLDGVTVIdLGGSLPGLPDRRGLRLVVEADRLDARTADGVEE--FGVAPDQLSIAEAEALARRLARWRAATaGTVDAP 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  650 IPEMLTFLDMYKTTRLEDIDIQRRWLENRTYESMKAIIGyRGAD-TPLYLDIHEKYH---GPHGLVAGTTGSGKSETLQT 725
Cdd:TIGR03924  376 LTGARDLLELLGIGDPATLDVDRLWRPRPGRDRLRVPIG-VGDDgEPVELDLKESAEggmGPHGLCIGATGSGKSELLRT 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  726 YILSLALNYHPYEVSFILIDYKGGGMAGSFEKLPHVAGIITNLGGNQT--NRALASINSEIKRRQAIFNEF-KIKHIDTY 802
Cdd:TIGR03924  455 LVLGLAATHSPEQLNLVLVDFKGGATFLGLEGLPHVSAVITNLADEAPlvDRMQDALAGEMNRRQELLRAAgNFANVAEY 534
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  803 IEIYRSGKATIPMPHLLIIADEFAELKKEQPEFVRELVSASRVGRSLGVHLILATQKPSGVVDDEIWGNSKSRLCLRVQD 882
Cdd:TIGR03924  535 EKARAAGADLPPLPALFVVVDEFSELLSQHPDFADLFVAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFS 614
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 2207671062  883 KQDSNEMIKRPDAAYITNA-GRGFFQVGNDEIfEAFQSGWSGAPY 926
Cdd:TIGR03924  615 ASESRAVLGVPDAYHLPSTpGAGYLKVDTAEP-VRFRAAYVSGPY 658
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
992-1356 1.43e-47

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 180.19  E-value: 1.43e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  992 IWLPPLPVRICLQDIEEYTERAFFNGAWEKTPwELKPAVGIVDDPVNQRQIPLIIDLLT-EGHLLISGS--GGKTTFLQT 1068
Cdd:TIGR03925   20 VWLPPLPEPPALDDLLPRLDVDPWRVDYGQRG-RLTVPVGIVDRPFEQRQDPLVVDLSGaAGHVAIVGApqSGKSTALRT 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1069 LLYSLVTTYSPNRFNLYIADYGSRTMGVFGVLPHVGGVVFDNETDKINKLIAMLIKELNKRKVVFSEKGIGSFKEYVRLY 1148
Cdd:TIGR03925   99 LILALALTHTPEEVQFYCLDFGGGGLASLADLPHVGGVAGRLDPERVRRTVAEVEGLLRRRERLFRTHGIDSMAQYRARR 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1149 DDVPA-------IVLAVDNFAAFNDNCPMQEDNMVMLSREAASYGIYLVITCTNINDIRNKIRQNIGFGIGLQLADRFEY 1221
Cdd:TIGR03925  179 AAGRLpedpfgdVFLVIDGWGTLRQDFEDLEDKVTDLAARGLAYGVHVVLTASRWSEIRPALRDLIGTRIELRLGDPMDS 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1222 EEVLNEKTDITAENkiPGRGLVcyPKPLEFQTALCLSAGDAVELNMTLKKQFDIITNSWQGKKAPVIPQVPEDMSLNSFL 1301
Cdd:TIGR03925  259 EIDRRAAARVPAGR--PGRGLT--PDGLHMLIALPRLDGIASVDDLGTRGLVAVIRDVWGGPPAPPVRLLPARLPLSALP 334
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2207671062 1302 LLPEvakilQGSRYLPLGydLAGASLE--SIDLAKTYCYSISGTGRSGKTNLLKAFM 1356
Cdd:TIGR03925  335 AGGG-----APRLRVPLG--LGESDLApvYVDFAESPHLLIFGDSESGKTTLLRTIA 384
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
669-861 1.29e-31

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 124.03  E-value: 1.29e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  669 DIQRRWLENRTYESMKAIIGYRGADTPLYLDihEKYHGPHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKG 748
Cdd:pfam01580    3 EVLESKPFDTDYSRLPIALGKDISGNPEVFD--LKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  749 GGMaGSFEKLPHV--AGIITNLGGnqTNRALASINSEIKRRQAIFNEFKIKHIDTY-----------------------I 803
Cdd:pfam01580   81 GEL-SAYEDIPHLlsVPVATDPKR--ALRALEWLVDEMERRYALFRALGVRSIAGYngeiaedpldgfgdvflviygvhV 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  804 EIYRSGKATIPmPHLLIIADEFAELK----KEQPEFVRELVS-ASRVGRSLGVHLILATQKPS 861
Cdd:pfam01580  158 MCTAGRWLEIL-PYLVVIVDERAELRlaapKDSEMRVEDAIVrLAQKGRAAGIHLLLATQRPS 219
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
695-1129 3.73e-30

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 127.80  E-value: 3.73e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  695 PLYLDIHEkyHGPHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKGGGMAgSFEKLPHVAGIITNLGGNQTN 774
Cdd:TIGR03925   70 PLVVDLSG--AAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLA-SLADLPHVGGVAGRLDPERVR 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  775 RALASINSEIKRRQAIFNEFKIKHIDTYIEIYRSGKA-TIPMPHLLIIADEFAELKKEQPEFVRELVSASRVGRSLGVHL 853
Cdd:TIGR03925  147 RTVAEVEGLLRRRERLFRTHGIDSMAQYRARRAAGRLpEDPFGDVFLVIDGWGTLRQDFEDLEDKVTDLAARGLAYGVHV 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  854 ILATQKPSGV---VDDEIwgnsKSRLCLRVQDKQDSneMIKRPDAAYITNA--GRG------FFQVGndeifeafqsgws 922
Cdd:TIGR03925  227 VLTASRWSEIrpaLRDLI----GTRIELRLGDPMDS--EIDRRAAARVPAGrpGRGltpdglHMLIA------------- 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  923 gapyEPETQYSdekqGDVKIINLWGKPQVVRSKKTAPQeekakkqtqleAAVLHIaeisekqnirpidniwlppLPVRIC 1002
Cdd:TIGR03925  288 ----LPRLDGI----ASVDDLGTRGLVAVIRDVWGGPP-----------APPVRL-------------------LPARLP 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1003 LQDIEEYTERAffngawektpwELKPAVGIvddpvNQRQI-PLIIDLLTEGHLLISGSG--GKTTFLQTLLYSLVTTYSP 1079
Cdd:TIGR03925  330 LSALPAGGGAP-----------RLRVPLGL-----GESDLaPVYVDFAESPHLLIFGDSesGKTTLLRTIARGIVRRYSP 393
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2207671062 1080 NRFNLYIADYgSRTMgvFGVLP--HVGGVVFDneTDKINKLIAMLIKELNKR 1129
Cdd:TIGR03925  394 DQARLVVVDY-RRTL--LGAVPedYLAGYAAT--SAALTELIAALAALLERR 440
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
707-886 2.91e-25

DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441280 [Multi-domain]  Cd Length: 611  Bit Score: 113.10  E-value: 2.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  707 PHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKgggMA--GSFEKLPH-VAGIITNLggNQTNRALASINSE 783
Cdd:COG1674    282 PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPK---MVelSVYNGIPHlLTPVVTDP--KKAANALKWAVRE 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  784 IKRRQAIFNEFKIKHIDTYIEIYRSGKATI-------PMPHLLIIADEFAEL----KKEqpefVRELVsaSRV---GRSL 849
Cdd:COG1674    357 MERRYKLFAKAGVRNIAGYNEKVREAKAKGeeeeglePLPYIVVIIDELADLmmvaGKE----VEEAI--ARLaqkARAA 430
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2207671062  850 GVHLILATQKPS-GVVDDEIWGNSKSRLCLRVQDKQDS 886
Cdd:COG1674    431 GIHLILATQRPSvDVITGLIKANIPSRIAFAVSSKIDS 468
PRK10263 PRK10263
DNA translocase FtsK; Provisional
632-902 1.21e-20

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 99.39  E-value: 1.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  632 FARGLSGVRVREVHSAGAIPEMLTFLDMYK--TTRLEDIDIQRRWLENRTyeSMKAIIGYRGADTPLYLDIHEKyhgPHG 709
Cdd:PRK10263   939 LARSLSTVAVRVVEVIPGKPYVGLELPNKKrqTVYLREVLDNAKFRDNPS--PLTVVLGKDIAGEPVVADLAKM---PHL 1013
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  710 LVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYKGGGMAgSFEKLPH-VAGIITNLgGNQTNRALASINsEIKRRQ 788
Cdd:PRK10263  1014 LVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELS-VYEGIPHlLTEVVTDM-KDAANALRWCVN-EMERRY 1090
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  789 AIFNEFKIKHIDTY----IEIYRSGKAtIP-------------------MPHLLIIADEFAELKKEQPEFVRELVSA-SR 844
Cdd:PRK10263  1091 KLMSALGVRNLAGYnekiAEADRMMRP-IPdpywkpgdsmdaqhpvlkkEPYIVVLVDEFADLMMTVGKKVEELIARlAQ 1169
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2207671062  845 VGRSLGVHLILATQKPS-GVVDDEIWGNSKSRLCLRVQDKQDSNEMIKRPDAAYITNAG 902
Cdd:PRK10263  1170 KARAAGIHLVLATQRPSvDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMG 1228
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
108-180 9.22e-18

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 80.00  E-value: 9.22e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  108 YILNHSRITIGSAEGNSIIYNNRnLVSRKHTVIERDaNGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIYI 180
Cdd:COG1716     16 FPLDGGPLTIGRAPDNDIVLDDP-TVSRRHARIRRD-GGGWVLEDLGSTNGTFVNGQRVTEPAPLRDGDVIRL 86
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
107-187 1.38e-17

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


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 79.24  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  107 KYILNHSRITIGSAEGNSIIYNNRNlVSRKHTVIERDaNGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIYIIGLKIV 186
Cdd:cd00060     13 EFPLTKGVVTIGRSPDCDIVLDDPS-VSRRHARIEVD-GGGVYLEDLGSTNGTFVNGKRITPPVPLQDGDVIRLGDTTFR 90

                   .
gi 2207671062  187 Y 187
Cdd:cd00060     91 F 91
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
1023-1191 2.02e-17

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 82.81  E-value: 2.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1023 PWELKPAVGIVDDPVNQRQIPLIIDLLT-EGHLLISGSG--GKTTFLQTLLYSLVTTYSPNRFNLYIADYGSRTMGVFGV 1099
Cdd:pfam01580    9 PFDTDYSRLPIALGKDISGNPEVFDLKKmPVHLLIAGATgsGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYED 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062 1100 LPHVGGVVFDNETDKINKLIAMLIKELNKRKVVFSEKGI-------GSFKEYVRLYDDV--------------------- 1151
Cdd:pfam01580   89 IPHLLSVPVATDPKRALRALEWLVDEMERRYALFRALGVrsiagynGEIAEDPLDGFGDvflviygvhvmctagrwleil 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2207671062 1152 PAIVLAVDNFA-----AFNDNCPMQEDNMVMLSREAASYGIYLVI 1191
Cdd:pfam01580  169 PYLVVIVDERAelrlaAPKDSEMRVEDAIVRLAQKGRAAGIHLLL 213
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
115-180 4.47e-14

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 68.37  E-value: 4.47e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2207671062  115 ITIGSAEGNSIIYNNRnLVSRKHTVIERDANGNYFVIDQKSSNSTFVNGRRILG-SHKLSYGDVIYI 180
Cdd:pfam00498    1 VTIGRSPDCDIVLDDP-SVSRRHAEIRYDGGGRFYLEDLGSTNGTFVNGQRLGPePVRLKDGDVIRL 66
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
109-184 6.17e-11

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: 60.77  E-value: 6.17e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2207671062  109 ILNHSRITIGSAEGNSIIYNNRNLVSRKHTVIERDANGNYFVIDQkSSNSTFVNGRRILG--SHKLSYGDVIYIIGLK 184
Cdd:cd22672     17 LLRKDEFTIGRAKDCDLSFPGNKLVSGDHCKIIRDEKGQVWLEDT-STNGTLVNKVKVVKgqKVELKHGDVIYLVYRK 93
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
107-182 1.42e-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: 56.45  E-value: 1.42e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2207671062  107 KYILNHSRITIGSAEGNSIIYNNRNlVSRKHTVIERDANGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIYIIG 182
Cdd:cd22673     15 RFPLTKKSCTFGRDLSCDIRIQLPG-VSREHCRIEVDENGKAYLENLSTTNPTLVNGKAIEKSAELKDGDVITIGG 89
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
107-180 4.24e-09

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: 55.11  E-value: 4.24e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2207671062  107 KYILNHSRITIGSAEGNSIIYNNRNlVSRKHTVIERdANGNYFVIDQKSSNSTFVNGRRIlGSHKLSYGDVIYI 180
Cdd:cd22698     15 DYELDQDEFTIGRSSNNDIRLNDHS-VSRHHARIVR-QGDKCNLTDLGSTNGTFLNGIRV-GTHELKHGDRIQL 85
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
708-880 4.78e-09

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 56.46  E-value: 4.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  708 HGLVAGTTGSGKSetlqTYILSLALNYHPYEVSFILIDYKGggmagsfeklphvAGIITNLGGNQTNRALASInseikrr 787
Cdd:cd01127      1 NTLVLGTTGSGKT----TSIVIPLLDQAARGGSVIITDPKG-------------ELFLVIPDRDDSFAALRAL------- 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  788 qaIFNefkikHIDTYIEIYRSGKATIPMPHLLIIADEFAELKKeqpefVRELVSASRVGRSLGVHLILATQ------KPS 861
Cdd:cd01127     57 --FFN-----QLFRALTELASLSPGRLPRRVWFILDEFANLGR-----IPNLPNLLATGRKRGISVVLILQslaqleAVY 124
                          170       180
                   ....*....|....*....|
gi 2207671062  862 GVVDDE-IWGNSKSRLCLRV 880
Cdd:cd01127    125 GKDGAQtILGNCNTKLYLGT 144
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
675-904 6.38e-09

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 60.01  E-value: 6.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  675 LENRTYESMKAIIG-YRGADTPLYLDIhEKYHGPHGLVAGTTGSGKSETLQTYILSLALNyhpyEVSFILIDYKG--GGM 751
Cdd:COG0433     16 LEELLGDGGGILIGkLLSPGVPVYLDL-DKLLNRHILILGATGSGKSNTLQVLLEELSRA----GVPVLVFDPHGeySGL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  752 AG----------------------------SFEKLPHVAGIITNLGGNQTN----------------------RALASIN 781
Cdd:COG0433     91 AEpgaeradvgvfdpgagrplpinpwdlfaTASELGPLLLSRLDLNDTQRGvlrealrladdkglllldlkdlIALLEEG 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  782 SEIKR---------RQAIFNE----------FKIKHIDTYIEIYRSGKATI----------------------------- 813
Cdd:COG0433    171 EELGEeygnvsaasAGALLRRleslesadglFGEPGLDLEDLLRTDGRVTVidlsglpeelqstfvlwllrelfearpev 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  814 ------PMPHLLIIaDE---FAelKKEQPEFVRELVSASRVGRSLGVHLILATQKPSGvVDDEIWGNSKSRLCLRVQDKQ 884
Cdd:COG0433    251 gdaddrKLPLVLVI-DEahlLA--PAAPSALLEILERIAREGRKFGVGLILATQRPSD-IDEDVLSQLGTQIILRLFNPR 326
                          330       340
                   ....*....|....*....|....*.
gi 2207671062  885 D------SNEMIKRPDAAYITNAGRG 904
Cdd:COG0433    327 DqkavkaAAETLSEDLLERLPSLGTG 352
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
109-180 6.88e-09

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: 54.42  E-value: 6.88e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  109 ILNHSRITIGSAEGNSIIYNNRNlVSRKHTVIERDANGnYFVIDQKSSNSTFVNGRRILG-SHKLSYGDVIYI 180
Cdd:cd22683     17 ITNRNVTTIGRSRSCDLVLSDPS-ISRFHAELRLEQNG-INVIDNNSANGTFINGKRIKGkTYILKNGDIIVF 87
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
115-166 1.76e-08

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 51.80  E-value: 1.76e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2207671062   115 ITIGSAEGNSIIYNNRNLVSRKHTVIERDANGNYFVIDQKSSNSTFVNGRRI 166
Cdd:smart00240    1 VTIGRSSEDCDIQLDGPSISRRHAVIVYDGGGRFYLIDLGSTNGTFVNGKRI 52
FHA_Slr1951-like cd22697
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ...
108-179 2.80e-08

forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438749 [Multi-domain]  Cd Length: 102  Bit Score: 53.24  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  108 YILNHSRITIGSAEGNSIIYNNRNlVSRKHTVIERDAN----GNYFVID-----QKSSNSTFVNGRRILgSHKLSYGDVI 178
Cdd:cd22697     13 IRLDEPIYTIGRHPGNDIQIPSQQ-ISRRHATLRRKINpnldISFWIIDgdlegAESLNGLWVNGERIL-QHELVNGDEI 90

                   .
gi 2207671062  179 Y 179
Cdd:cd22697     91 A 91
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
113-178 3.10e-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: 53.13  E-value: 3.10e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  113 SRITIGSAEGNS--IIYNNRNLVSRKHTVIERDANGNYFVIDQKSSNSTFVNGRRI--LGSHKLSYGDVI 178
Cdd:cd22663     21 KEVTVGRGLGVTyqLVSTCPLMISRNHCVLKKNDEGQWTIKDNKSLNGVWVNGERIepLKPYPLNEGDLI 90
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
694-911 9.71e-08

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 56.49  E-value: 9.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  694 TPLYLDIHEKYHGPHGLVAGTTGSGKSETLQTyilsLALNYHPYEVSFILIDYKGG-----------------GMAGSF- 755
Cdd:COG3451    192 TPVFFDFHDGLDNGNTLILGPSGSGKSFLLKL----LLLQLLRYGARIVIFDPGGSyeilvralggtyidlspGSPTGLn 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  756 --------EKLPHVAGIITNLGGNQTNRALASINSEIKR--------------------RQAIFNEFKIKHIDTYIEIYR 807
Cdd:COG3451    268 pfdledteEKRDFLLELLELLLGREGEPLTPEERAAIDRavralyrradpeerttlsdlYELLKEQPEAKDLAARLEPYT 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  808 S---------GKATIPMPH-----------------------------------------LLIIADEFAELKKEqPEFVR 837
Cdd:COG3451    348 KggsygwlfdGPTNLDLSDarfvvfdltelldnpelrppvllyllhriwnrlrknndgrpTLIVIDEAWLLLDN-PAFAE 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  838 ELVSASRVGRSLGVHLILATQKPSGVVDDE----IWGNSKSRLCLRvQDKQDSNEMIKR---PDA--AYITNAGRG---- 904
Cdd:COG3451    427 FLEEWLKTLRKYNGAVIFATQSVEDFLSSPiaeaIIENSATKILLP-QPKADIEDYAELlglSERelELIRSAGRGkrdf 505

                   ....*..
gi 2207671062  905 FFQVGND 911
Cdd:COG3451    506 LIKQGNG 512
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
108-188 4.97e-07

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: 49.53  E-value: 4.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  108 YILNHSRITIGSAEGNSIIYNNRnLVSRKHTVI-----ERDANGNYFVIDQkSSNSTFVNGRRIlGSHK---LSYGDVIY 179
Cdd:cd22670     17 PIYKNQVITIGRSPSCDIVINDP-FVSRTHCRIysvqfDESSAPLVYVEDL-SSNGTYLNGKLI-GRNNtvlLSDGDVIE 93
                           90
                   ....*....|
gi 2207671062  180 I-IGLKIVYM 188
Cdd:cd22670     94 IaHSATFVYV 103
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
116-202 4.97e-07

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: 54.00  E-value: 4.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  116 TIGSAEGNS-IIYNNRNLVSRKHTVIERDaNGNYFVIDQkSSNSTFVNG--RRIL--GSHKLSYGDVI----YIIGLKIV 186
Cdd:COG3456     29 TIGRSADCDwVLPDPDRSVSRRHAEIRFR-DGAFCLTDL-STNGTFLNGsdHPLGpgRPVRLRDGDRLrigdYEIRVEIS 106
                           90
                   ....*....|....*.
gi 2207671062  187 YMGDLIAINQPKNPAK 202
Cdd:COG3456    107 GEDEGADDPLAAAPEP 122
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
100-187 8.67e-07

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: 48.77  E-value: 8.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  100 ESYSDFNKYILNHSRITIGSAEGNSIIYNNRNlVSRKHTVIERDAnGNYFVIDQKSSNSTFVNGRRILG---SHKLSYGD 176
Cdd:cd22665      8 QAHGPEKDFPLYEGENVIGRDPSCSVVLPDKS-VSKQHACIEVDG-GTHLIEDLGSTNGTRIGNKVRLKpnvRYELIDGD 85
                           90
                   ....*....|.
gi 2207671062  177 VIYIIGLKIVY 187
Cdd:cd22665     86 LLLFGDVKCQY 96
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
107-180 1.51e-06

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


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 48.11  E-value: 1.51e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2207671062  107 KYILNHSRITIGSAEGNSIIYNNrNLVSRKHTVIERDANGnYFVIDQKSSNSTFVN-GRRILGSHKLSYGDVIYI 180
Cdd:cd22680     15 KFPFDFSSVSIGRDPENVIVIPD-PFVSRNHARITVDSNE-IYIEDLGSTNGTFVNdFKRIKGPAKLHPNDIIKL 87
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
115-180 1.52e-06

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


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 47.71  E-value: 1.52e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2207671062  115 ITIGSAEGNSIIYNNrNLVSRKHTVIERDANGnYFVIDQKSSNSTFVNGRRIlGSHKLSYGDVIYI 180
Cdd:cd22694     18 VRIGRDPDADVRLDD-PRVSRRHALLEFDGDG-WVYTDLGSRNGTYLNGRRV-QQVKLSDGTRVRL 80
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
115-180 1.90e-06

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


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 47.30  E-value: 1.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2207671062  115 ITIGSAEGNSIIYNNrNLVSRKHTVIERDaNGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIYI 180
Cdd:cd22693     20 ITIGRADDNDLVLSD-DFVSSRHARIYLQ-GSSWYLEDLGSTNGTFVNGNRVTQPVVVQPGDTIRI 83
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
110-187 1.33e-05

second 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 second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 45.18  E-value: 1.33e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2207671062  110 LNHSRITIGSAEGNSIIYNNrNLVSRKHTVIERdANGNYFVIDQKSSNSTFVNGRRIlGSHKLSYGDVIYIIGLKIVY 187
Cdd:cd22737     18 LPPQAVRIGRASDNDIVIPE-GSVSRHHATLVP-TPGGTQIRDLRSTNGTFVNGLRV-DAALLHDGDVVTIGDIDFVF 92
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
93-180 1.37e-05

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: 46.12  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062   93 IIVEESyESYSDFNKYILNHSRITIG--SAEGNSIIYNNRNlVSRKHTVIERDAN-GNYFVIDQKSSNSTFVNGRRIL-- 167
Cdd:cd22686      7 VIVVES-PSLQVGSLFIVTATGATIGreKDHGHTIRIPELG-VSKFHAEIYYDDDeQSYTIVDLGSQNGTYLNGVRISqp 84
                           90
                   ....*....|....*..
gi 2207671062  168 --GSHK--LSYGDVIYI 180
Cdd:cd22686     85 keKSDPypLTHGDELKI 101
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
816-889 1.55e-05

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 49.21  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  816 PHLLIIADEFAELKKeqpefVRELVSASRVGRSLGVHLILATQKPSGVVD-------DEIWGNSKSRLCLRVQDKQDSNE 888
Cdd:COG3505    247 RPVLLLLDEFANLGR-----LPSLETLLATGRGYGIRLVLILQSLAQLEAiygeegaETILGNCGTKIFLGVNDPETAEY 321

                   .
gi 2207671062  889 M 889
Cdd:COG3505    322 L 322
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
131-178 1.89e-05

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: 45.87  E-value: 1.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  131 NLVSRKHTVI--ERDANGNYFV-IDQKSSNSTFVNGRRILG--SHKLSYGDVI 178
Cdd:cd22685     50 NLISREHAEIhaERDGNGNWKVlIEDRSTNGTYVNDVRLQDgqRRELSDGDTI 102
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
133-178 2.37e-05

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: 44.41  E-value: 2.37e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2207671062  133 VSRKHTVIERDANGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVI 178
Cdd:cd22696     41 ISRQHARLSIDQDNRVFIEDLSSKNGVLVNGKPIEGKEEISGSDVI 86
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
108-178 7.75e-05

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: 43.01  E-value: 7.75e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2207671062  108 YILNHSRITIGSaEGNSIIYNNRNlVSRKHTVIERDANGNYFVI-DQKSSNSTFVNGRRIL-GSHKLSYGDVI 178
Cdd:cd22700     11 FQLDPKVTTIGR-EGCDLVLQSPG-VEEQHAVIEYSEQENCFVLqDLNTAQGTYVNDCRIQnAAVRLAPGDVL 81
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
110-206 1.55e-04

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: 42.28  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  110 LNHSRITIGSAEGNSIIYNNrNLVSRKHTVIERDANGNY----FVIDQkSSNSTFVNGRRIlGSHKLSygdviyiiglkI 185
Cdd:cd22690     16 LTQNTTFIGRSKDCDEEITD-PRISKHHCIITRKRSGKGlddvYVTDT-STNGTFINNNRL-GKGSQS-----------L 81
                           90       100
                   ....*....|....*....|.
gi 2207671062  186 VYMGDLIAINQPKNPAKMEGF 206
Cdd:cd22690     82 LQDGDEIVLIWDKNNKEKIGF 102
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
108-180 5.32e-04

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: 40.59  E-value: 5.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2207671062  108 YILNHSRITIGSAEGNSIIYNNrNLVSRKHTVIERDANGNYfVIDQKSSNSTFVNGRRI--LGSHKLSYGDVIYI 180
Cdd:cd22682     15 FPITESTIVIGRSVESQVQIDD-DSVSRYHAKLAVNPSAVS-IIDLGSTNGTIVNGKKIpkLASCDLQNGDQIKI 87
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
115-178 6.94e-04

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: 40.42  E-value: 6.94e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2207671062  115 ITIGSAEGNSIIYNNRNlVSRKHTVIERDANG-NYFVIDQKSSNSTFVNGRRI---LGSHKLSYGDVI 178
Cdd:cd22678     25 LTIGRIQRGDIALKDDE-VSGKHARIEWNSTGsKWELVDLGSLNGTLVNGESIspnGRPVVLSSGDVI 91
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
687-747 7.12e-04

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 44.21  E-value: 7.12e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2207671062  687 IGYRGAD-TPLYLDIHEKyhgPHGLVAGTTGSGKSETLQTYILSLALNYHPYEVSFILIDYK 747
Cdd:TIGR03925  346 LGLGESDlAPVYVDFAES---PHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR 404
TraG-D_C pfam12696
TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as ...
817-890 8.61e-04

TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as VirD4 proteins. TraG is essential for DNA transfer in bacterial conjugation. These proteins are thought to mediate interactions between the DNA-processing (Dtr) and the mating pair formation (Mpf) systems. This domain interacts with the relaxosome component TraM via the latter's tetramerization domain. TraD is a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore.


Pssm-ID: 432726 [Multi-domain]  Cd Length: 125  Bit Score: 40.71  E-value: 8.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062  817 HLLIIADEFAELKKeqpefVRELVSASRVGRSLGVHLILATQKPSGVVD-------DEIWGNSKSRLCLRVQDKqDSNEM 889
Cdd:pfam12696    1 PVLFVLDEFANLGK-----IPDLEKLISTGRSRGISLMLILQSIAQLEElygkdgaETILGNCNTKVFLGGGDE-ETAKY 74

                   .
gi 2207671062  890 I 890
Cdd:pfam12696   75 L 75
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
108-182 1.09e-03

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 39.94  E-value: 1.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2207671062  108 YILNHSRITIGSAEGNSI--IYNNRNLVSRKHTVIERdaNGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVIyIIG 182
Cdd:cd22707     25 YMLKEGQTRVGRSKASSShdIQLSGALIADDHCTIEN--NGGKVTIIPVGDAETYVNGELISEPTVLHHGDRV-ILG 98
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
134-178 1.10e-03

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: 40.71  E-value: 1.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2207671062  134 SRKHTVIERDaNGNYFVIDQKSSNSTFVNGRRIL-GS-----HKLSYGDVI 178
Cdd:cd22679     50 SRNHALLWYD-DGKFYLQDTKSSNGTFVNNQRLSkGSeesepRELHSGDIV 99
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
108-178 1.50e-03

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


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 39.37  E-value: 1.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2207671062  108 YILNHSRITIGSAEGNSIIYNNrNLVSRKHTVIERDAnGNYFVIDQKSSNSTFVNGRRILGSHKLSYGDVI 178
Cdd:cd22668     13 YQLREGSNIIGRGSDADFRLPD-TGVSRRHAEIRWDG-QVAHLTDLGSTNGTTVNNAPVTPEWRLADGDVI 81
FHA_CHK2 cd22666
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ...
86-178 1.73e-03

forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; Chk2, also called Hucds1, Cds1 homolog, or serine/threonine-protein kinase Chk2, plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438718 [Multi-domain]  Cd Length: 112  Bit Score: 39.53  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062   86 PSGQKFSII--VEESYesysdfnkyilnhsriTIGSAEGNSIIYNNRNL--------VSRKHTVIERD---ANGNYFVID 152
Cdd:cd22666      6 PLGSGFSSLdlVKDEY----------------TFGRDKSCDYCFDSPALkktsyyrtYSKKHFRIFREkgsKNTYPVFLE 69
                           90       100
                   ....*....|....*....|....*....
gi 2207671062  153 QKSSNSTFVNGRRIlGSHK---LSYGDVI 178
Cdd:cd22666     70 DHSSNGTFVNGEKI-GKGKkrpLNNNDEI 97
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
111-180 2.98e-03

first 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 first one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 39.57  E-value: 2.98e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2207671062  111 NHSRI-TIGSAEGNSIIYNNRNlVSRKHTVI---ERDANGNYFVIDQKSSNSTFVNGRRILGSHK--LSYGDVIYI 180
Cdd:cd22689     42 SIKKVwTFGRHPACDYHLGNSR-LSNKHFQIllgESDPSDGNVLLNDISSNGTWLNGQRLEKNSNqlLSQGDEITI 116
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
133-187 3.19e-03

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


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 38.52  E-value: 3.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2207671062  133 VSRKHTVIERdANGNYFVIDQKSSNSTFVNGRRIlGSHKLSYGDVIYIIGLKIVY 187
Cdd:cd22684     40 VSRRHAEFRR-AEGGFVVRDVGSLNGTYVNRERI-DSAVLRNGDEVQIGKFRLVF 92
FHA_VPS64-like cd22695
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ...
86-178 9.03e-03

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: 38.05  E-value: 9.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207671062   86 PSGQKFSIIVEESYESYSDFNKYILNHSRITigSAEGNsiiYNNRnLVSRKHTVIERD-ANGNYFVIDQKSSNSTFVNGR 164
Cdd:cd22695     24 PDGLKLGRPVTNSVNKNNSGSKRDLFSQQVR--PDNGN---FDSR-VLSRNHACLSCDpTTGKVYIRDLKSSNGTFVNGQ 97
                           90
                   ....*....|....*
gi 2207671062  165 RILG-SHKLSYGDVI 178
Cdd:cd22695     98 KIRQnDVELKVGDEV 112
 
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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