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Conserved domains on  [gi|1239658286|gb|ASW53127|]
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cell division protein FtsK [Plantactinospora sp. KBS50]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
T7SS_EccC_a super family cl37347
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
177-526 4.82e-21

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]


The actual alignment was detected with superfamily member TIGR03924:

Pssm-ID: 274858 [Multi-domain]  Cd Length: 658  Bit Score: 98.51  E-value: 4.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 177 RRPAIDLPGFQRVLAEAEERIERVQAGEA--DPSVLLLCVAAMPQGTGRtewsrltAIAHAGPAAGVFLLLAGYPPPQHP 254
Cdd:TIGR03924 246 RLVYTSLAELEAALAELLADRGRFSPDDAasLPHLVVVVDGGDLPGWED-------LIGESGLDGVTVIDLGGSLPGLPD 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 255 GLDAVPRLErtthltatgDGSFQVSDPPGPYRFSDDGTGLAVpmrldsgppdELVEAVCRRLAK----AARVQAST---- 326
Cdd:TIGR03924 319 RRGLRLVVE---------ADRLDARTADGVEEFGVAPDQLSI----------AEAEALARRLARwraaTAGTVDAPltga 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 327 ----------DFTALMPAEMWQESS-VEGLRTVVGRDGRAECV------LALDDATPHWLVGGRTGSGKTVFLLDVLYGL 389
Cdd:TIGR03924 380 rdllellgigDPATLDVDRLWRPRPgRDRLRVPIGVGDDGEPVeldlkeSAEGGMGPHGLCIGATGSGKSELLRTLVLGL 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 390 ASRYSPDELGLYLLDFKEGVSFAEFTPtavdpswIPHarTVGIESDREYGLA----VLRTLSREMTRRASELKRAGvtKL 465
Cdd:TIGR03924 460 AATHSPEQLNLVLVDFKGGATFLGLEG-------LPH--VSAVITNLADEAPlvdrMQDALAGEMNRRQELLRAAG--NF 528
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239658286 466 ADLR-------TGRPDVAMPRLVAVIDEFHVLFegndAVARQAVALLEELARKGRSYGIHLVLASQTI 526
Cdd:TIGR03924 529 ANVAeyekaraAGADLPPLPALFVVVDEFSELL----SQHPDFADLFVAIGRLGRSLGVHLLLASQRL 592
 
Name Accession Description Interval E-value
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
177-526 4.82e-21

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: 98.51  E-value: 4.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 177 RRPAIDLPGFQRVLAEAEERIERVQAGEA--DPSVLLLCVAAMPQGTGRtewsrltAIAHAGPAAGVFLLLAGYPPPQHP 254
Cdd:TIGR03924 246 RLVYTSLAELEAALAELLADRGRFSPDDAasLPHLVVVVDGGDLPGWED-------LIGESGLDGVTVIDLGGSLPGLPD 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 255 GLDAVPRLErtthltatgDGSFQVSDPPGPYRFSDDGTGLAVpmrldsgppdELVEAVCRRLAK----AARVQAST---- 326
Cdd:TIGR03924 319 RRGLRLVVE---------ADRLDARTADGVEEFGVAPDQLSI----------AEAEALARRLARwraaTAGTVDAPltga 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 327 ----------DFTALMPAEMWQESS-VEGLRTVVGRDGRAECV------LALDDATPHWLVGGRTGSGKTVFLLDVLYGL 389
Cdd:TIGR03924 380 rdllellgigDPATLDVDRLWRPRPgRDRLRVPIGVGDDGEPVeldlkeSAEGGMGPHGLCIGATGSGKSELLRTLVLGL 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 390 ASRYSPDELGLYLLDFKEGVSFAEFTPtavdpswIPHarTVGIESDREYGLA----VLRTLSREMTRRASELKRAGvtKL 465
Cdd:TIGR03924 460 AATHSPEQLNLVLVDFKGGATFLGLEG-------LPH--VSAVITNLADEAPlvdrMQDALAGEMNRRQELLRAAG--NF 528
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239658286 466 ADLR-------TGRPDVAMPRLVAVIDEFHVLFegndAVARQAVALLEELARKGRSYGIHLVLASQTI 526
Cdd:TIGR03924 529 ANVAeyekaraAGADLPPLPALFVVVDEFSELL----SQHPDFADLFVAIGRLGRSLGVHLLLASQRL 592
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
330-527 2.04e-18

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: 84.74  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 330 ALMPAEMWQESSVegLRTVVGRDGRAECVLA-LDDATPHWLVGGRTGSGKTVFLLDVLYGLASRYSPDELGLYLLDFKeG 408
Cdd:pfam01580   4 VLESKPFDTDYSR--LPIALGKDISGNPEVFdLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPK-M 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 409 VSFAEFTPtavdpswIPHARTVGIESDREYGLAVLRTLSREMTRRASELKRAGVTKLADLRTGRPDVAM----------- 477
Cdd:pfam01580  81 GELSAYED-------IPHLLSVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLdgfgdvflviy 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239658286 478 ---------------PRLVAVIDEFH--VLFEGNDAVARQaVALLEELARKGRSYGIHLVLASQTIS 527
Cdd:pfam01580 154 gvhvmctagrwleilPYLVVIVDERAelRLAAPKDSEMRV-EDAIVRLAQKGRAAGIHLLLATQRPS 219
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
366-566 4.73e-14

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: 76.12  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 366 PHWLVGGRTGSGKTVF----LLDVLYglasRYSPDELGLYLLDFK-------EGvsfaeftptavdpswIPHARTvGIES 434
Cdd:COG1674   282 PHLLIAGATGSGKSVCinamILSLLY----KATPDEVRLILIDPKmvelsvyNG---------------IPHLLT-PVVT 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 435 DREYGLAVLRTLSREMTRRASELKRAGVTKLAD-----------LRTGRPDVAMPRLVAVIDEFHVLF-----EGNDAVA 498
Cdd:COG1674   342 DPKKAANALKWAVREMERRYKLFAKAGVRNIAGynekvreakakGEEEEGLEPLPYIVVIIDELADLMmvagkEVEEAIA 421
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239658286 499 RqavalleeLARKGRSYGIHLVLASQT-----ISGVealfaktesIFGQFPLRIALAGGGG-----ILDQLndGADNL 566
Cdd:COG1674   422 R--------LAQKARAAGIHLILATQRpsvdvITGL---------IKANIPSRIAFAVSSKidsrtILDQG--GAEKL 480
PRK10263 PRK10263
DNA translocase FtsK; Provisional
345-566 2.49e-12

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 71.27  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  345 LRTVVGRDGRAECVLALDDATPHWLVGGRTGSGKTVFLLDVLYGLASRYSPdelglylldfkEGVSFAEFTPTAVDPS-- 422
Cdd:PRK10263   990 LTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQP-----------EDVRFIMIDPKMLELSvy 1058
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  423 -WIPHARTvGIESDREYGLAVLRTLSREMTRRASELKRAGVTKLADL--------RTGRP------------DV------ 475
Cdd:PRK10263  1059 eGIPHLLT-EVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYnekiaeadRMMRPipdpywkpgdsmDAqhpvlk 1137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  476 AMPRLVAVIDEFHVLFEgndAVARQAVALLEELARKGRSYGIHLVLASQTISgVEALfakTESIFGQFPLRIALAGGGG- 554
Cdd:PRK10263  1138 KEPYIVVLVDEFADLMM---TVGKKVEELIARLAQKARAAGIHLVLATQRPS-VDVI---TGLIKANIPTRIAFTVSSKi 1210
                          250
                   ....*....|....*.
gi 1239658286  555 ----ILDQlnDGADNL 566
Cdd:PRK10263  1211 dsrtILDQ--AGAESL 1224
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
367-551 1.84e-11

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: 62.62  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 367 HWLVGGRTGSGKTVFLLDVLYGLASRYSPdelgLYLLDFKegvsfaeftptavDPSWIphartvgIESDREYGLAVLRTL 446
Cdd:cd01127     1 NTLVLGTTGSGKTTSIVIPLLDQAARGGS----VIITDPK-------------GELFL-------VIPDRDDSFAALRAL 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 447 SREMTRRAselkragVTKLADLRTGRPDvamPRLVAVIDEFHVLfegndavarQAVALLEELARKGRSYGIHLVLASQTI 526
Cdd:cd01127    57 FFNQLFRA-------LTELASLSPGRLP---RRVWFILDEFANL---------GRIPNLPNLLATGRKRGISVVLILQSL 117
                         170       180
                  ....*....|....*....|....*..
gi 1239658286 527 SGVEALFAK--TESIFGQFPLRIALAG 551
Cdd:cd01127   118 AQLEAVYGKdgAQTILGNCNTKLYLGT 144
 
Name Accession Description Interval E-value
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
177-526 4.82e-21

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: 98.51  E-value: 4.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 177 RRPAIDLPGFQRVLAEAEERIERVQAGEA--DPSVLLLCVAAMPQGTGRtewsrltAIAHAGPAAGVFLLLAGYPPPQHP 254
Cdd:TIGR03924 246 RLVYTSLAELEAALAELLADRGRFSPDDAasLPHLVVVVDGGDLPGWED-------LIGESGLDGVTVIDLGGSLPGLPD 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 255 GLDAVPRLErtthltatgDGSFQVSDPPGPYRFSDDGTGLAVpmrldsgppdELVEAVCRRLAK----AARVQAST---- 326
Cdd:TIGR03924 319 RRGLRLVVE---------ADRLDARTADGVEEFGVAPDQLSI----------AEAEALARRLARwraaTAGTVDAPltga 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 327 ----------DFTALMPAEMWQESS-VEGLRTVVGRDGRAECV------LALDDATPHWLVGGRTGSGKTVFLLDVLYGL 389
Cdd:TIGR03924 380 rdllellgigDPATLDVDRLWRPRPgRDRLRVPIGVGDDGEPVeldlkeSAEGGMGPHGLCIGATGSGKSELLRTLVLGL 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 390 ASRYSPDELGLYLLDFKEGVSFAEFTPtavdpswIPHarTVGIESDREYGLA----VLRTLSREMTRRASELKRAGvtKL 465
Cdd:TIGR03924 460 AATHSPEQLNLVLVDFKGGATFLGLEG-------LPH--VSAVITNLADEAPlvdrMQDALAGEMNRRQELLRAAG--NF 528
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239658286 466 ADLR-------TGRPDVAMPRLVAVIDEFHVLFegndAVARQAVALLEELARKGRSYGIHLVLASQTI 526
Cdd:TIGR03924 529 ANVAeyekaraAGADLPPLPALFVVVDEFSELL----SQHPDFADLFVAIGRLGRSLGVHLLLASQRL 592
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
330-527 2.04e-18

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: 84.74  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 330 ALMPAEMWQESSVegLRTVVGRDGRAECVLA-LDDATPHWLVGGRTGSGKTVFLLDVLYGLASRYSPDELGLYLLDFKeG 408
Cdd:pfam01580   4 VLESKPFDTDYSR--LPIALGKDISGNPEVFdLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPK-M 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 409 VSFAEFTPtavdpswIPHARTVGIESDREYGLAVLRTLSREMTRRASELKRAGVTKLADLRTGRPDVAM----------- 477
Cdd:pfam01580  81 GELSAYED-------IPHLLSVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLdgfgdvflviy 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239658286 478 ---------------PRLVAVIDEFH--VLFEGNDAVARQaVALLEELARKGRSYGIHLVLASQTIS 527
Cdd:pfam01580 154 gvhvmctagrwleilPYLVVIVDERAelRLAAPKDSEMRV-EDAIVRLAQKGRAAGIHLLLATQRPS 219
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
366-566 4.73e-14

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: 76.12  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 366 PHWLVGGRTGSGKTVF----LLDVLYglasRYSPDELGLYLLDFK-------EGvsfaeftptavdpswIPHARTvGIES 434
Cdd:COG1674   282 PHLLIAGATGSGKSVCinamILSLLY----KATPDEVRLILIDPKmvelsvyNG---------------IPHLLT-PVVT 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 435 DREYGLAVLRTLSREMTRRASELKRAGVTKLAD-----------LRTGRPDVAMPRLVAVIDEFHVLF-----EGNDAVA 498
Cdd:COG1674   342 DPKKAANALKWAVREMERRYKLFAKAGVRNIAGynekvreakakGEEEEGLEPLPYIVVIIDELADLMmvagkEVEEAIA 421
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239658286 499 RqavalleeLARKGRSYGIHLVLASQT-----ISGVealfaktesIFGQFPLRIALAGGGG-----ILDQLndGADNL 566
Cdd:COG1674   422 R--------LAQKARAAGIHLILATQRpsvdvITGL---------IKANIPSRIAFAVSSKidsrtILDQG--GAEKL 480
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
367-549 3.37e-13

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: 73.87  E-value: 3.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  367 HWLVGGRTGSGKTVFLLDVLYGLASRYSPDELGLYLLDFKEGvSFAEFTPtavdpswIPH-ARTVGIESDREYGLAVlRT 445
Cdd:TIGR03928  812 HLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTN-GLLPLKK-------LPHvADYFTLDEEEKIEKLI-RR 882
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  446 LSREMTRRASELKRAGVTKLADLR--TGRPdvaMPRLVAVIDEFHVLfeGNDAVARQAVALLEELARKGRSYGIHLVLas 523
Cdd:TIGR03928  883 IKKEIDRRKKLFSEYGVASISMYNkaSGEK---LPQIVIIIDNYDAV--KEEPFYEDFEELLIQLAREGASLGIYLVM-- 955
                          170       180
                   ....*....|....*....|....*.
gi 1239658286  524 qTISGVEALFAKtesIFGQFPLRIAL 549
Cdd:TIGR03928  956 -TAGRQNAVRMP---LMNNIKTKIAL 977
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
366-529 4.90e-13

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: 73.48  E-value: 4.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  366 PHWLVGGRTGSGKTVFLLDVLYGLASRYSPDELGLYLLDFKEG---VSFAEftptavdpswIPHAR-TV----GIESDRe 437
Cdd:TIGR03928  470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGgmaNLFKN----------LPHLLgTItnldGAQSMR- 538
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  438 yGLAVLRTlsrEMTRRASELKRAGVTKLAD----LRTGRPDVAMPRLVAVIDEFHVL------FegndavarqavalLEE 507
Cdd:TIGR03928  539 -ALASIKA---ELKKRQRLFGENNVNHINQyqklYKQGKAKEPMPHLFLISDEFAELkseqpeF-------------MKE 601
                          170       180
                   ....*....|....*....|....*
gi 1239658286  508 L---ARKGRSYGIHLVLASQTISGV 529
Cdd:TIGR03928  602 LvstARIGRSLGVHLILATQKPSGV 626
PRK10263 PRK10263
DNA translocase FtsK; Provisional
345-566 2.49e-12

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 71.27  E-value: 2.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  345 LRTVVGRDGRAECVLALDDATPHWLVGGRTGSGKTVFLLDVLYGLASRYSPdelglylldfkEGVSFAEFTPTAVDPS-- 422
Cdd:PRK10263   990 LTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQP-----------EDVRFIMIDPKMLELSvy 1058
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  423 -WIPHARTvGIESDREYGLAVLRTLSREMTRRASELKRAGVTKLADL--------RTGRP------------DV------ 475
Cdd:PRK10263  1059 eGIPHLLT-EVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYnekiaeadRMMRPipdpywkpgdsmDAqhpvlk 1137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286  476 AMPRLVAVIDEFHVLFEgndAVARQAVALLEELARKGRSYGIHLVLASQTISgVEALfakTESIFGQFPLRIALAGGGG- 554
Cdd:PRK10263  1138 KEPYIVVLVDEFADLMM---TVGKKVEELIARLAQKARAAGIHLVLATQRPS-VDVI---TGLIKANIPTRIAFTVSSKi 1210
                          250
                   ....*....|....*.
gi 1239658286  555 ----ILDQlnDGADNL 566
Cdd:PRK10263  1211 dsrtILDQ--AGAESL 1224
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
367-551 1.84e-11

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: 62.62  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 367 HWLVGGRTGSGKTVFLLDVLYGLASRYSPdelgLYLLDFKegvsfaeftptavDPSWIphartvgIESDREYGLAVLRTL 446
Cdd:cd01127     1 NTLVLGTTGSGKTTSIVIPLLDQAARGGS----VIITDPK-------------GELFL-------VIPDRDDSFAALRAL 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 447 SREMTRRAselkragVTKLADLRTGRPDvamPRLVAVIDEFHVLfegndavarQAVALLEELARKGRSYGIHLVLASQTI 526
Cdd:cd01127    57 FFNQLFRA-------LTELASLSPGRLP---RRVWFILDEFANL---------GRIPNLPNLLATGRKRGISVVLILQSL 117
                         170       180
                  ....*....|....*....|....*..
gi 1239658286 527 SGVEALFAK--TESIFGQFPLRIALAG 551
Cdd:cd01127   118 AQLEAVYGKdgAQTILGNCNTKLYLGT 144
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
469-549 5.63e-08

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: 55.77  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 469 RTGRPDVAMPRLVAVIDEFHVLFEGNDAVARQAvalLEELARKGRSYGIHLVLASQTISGVEalfaktESIFGQFPLRIA 548
Cdd:COG0433   249 EVGDADDRKLPLVLVIDEAHLLAPAAPSALLEI---LERIAREGRKFGVGLILATQRPSDID------EDVLSQLGTQII 319

                  .
gi 1239658286 549 L 549
Cdd:COG0433   320 L 320
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
354-522 1.58e-07

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: 55.00  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 354 RAECVLALDDATPHWLVGGRTGSGKTVFLLDVLYGLASRYSPDELGLYLLDFKEGvsfaeftpTAVDPSWIPHARTVGIE 433
Cdd:TIGR03925  68 QDPLVVDLSGAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGG--------GLASLADLPHVGGVAGR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 434 SDREYGLAVLRTLSREMTRRASELKRAGVTKLADLRTGR-----PDVAMPRLVAVIDEFHVLFEGNDAVArqavALLEEL 508
Cdd:TIGR03925 140 LDPERVRRTVAEVEGLLRRRERLFRTHGIDSMAQYRARRaagrlPEDPFGDVFLVIDGWGTLRQDFEDLE----DKVTDL 215
                         170
                  ....*....|....
gi 1239658286 509 ARKGRSYGIHLVLA 522
Cdd:TIGR03925 216 AARGLAYGVHVVLT 229
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
441-552 1.11e-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: 48.83  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 441 AVLRTLSREMTRRASelkragvtkladlRTGRPDvamPRLVAVIDEFHVLfegndavarQAVALLEELARKGRSYGIHLV 520
Cdd:COG3505   226 LLLSQLIRALLRRAE-------------RSGRLP---RPVLLLLDEFANL---------GRLPSLETLLATGRGYGIRLV 280
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1239658286 521 LASQTISGVEALF--AKTESIFGQFPLRIALAGG 552
Cdd:COG3505   281 LILQSLAQLEAIYgeEGAETILGNCGTKIFLGVN 314
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
331-533 2.80e-05

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: 47.68  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 331 LMPAEMWQESSVEGLRTVVGRDGRAECVLALD-DATPHWLVGGRTGSGKTVFLLDVLYGLASRYSPDELGLYLLDFKEGV 409
Cdd:TIGR03925 328 LPLSALPAGGGAPRLRVPLGLGESDLAPVYVDfAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRTL 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 410 SfaeftpTAVDPSWIphartVGIESDREYGLAVLRTLSREMTRRaseLKRAGVTKlADLR-----TGrpdvamPRLVAVI 484
Cdd:TIGR03925 408 L------GAVPEDYL-----AGYAATSAALTELIAALAALLERR---LPGPDVTP-QQLRarswwSG------PEIYVVV 466
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1239658286 485 DEFHVLFEGNDavarQAVALLEELARKGRSYGIHLVLASQTISGVEALF 533
Cdd:TIGR03925 467 DDYDLVATGSG----NPLAPLVELLPHARDIGLHVVVARRSGGAARALM 511
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
389-549 4.41e-05

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


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 47.25  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 389 LASRYSPDELGLYLLDFKEGVSFAEF--TPTAVDpswIPHARTVGIEsdreyglavLRTLSREmtrraSELKRAGVT--- 463
Cdd:COG3451   330 LKEQPEAKDLAARLEPYTKGGSYGWLfdGPTNLD---LSDARFVVFD---------LTELLDN-----PELRPPVLLyll 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 464 -----KLADLRTGRPdvamprLVAVIDEFHVLFeGNDAVArqavALLEELARKGRSYGIHLVLASQTISGVEALfAKTES 538
Cdd:COG3451   393 hriwnRLRKNNDGRP------TLIVIDEAWLLL-DNPAFA----EFLEEWLKTLRKYNGAVIFATQSVEDFLSS-PIAEA 460
                         170
                  ....*....|.
gi 1239658286 539 IFGQFPLRIAL 549
Cdd:COG3451   461 IIENSATKILL 471
TraG-D_C pfam12696
TraM recognition site of TraD and TraG; This family includes both TraG and TraD as well as ...
479-552 6.87e-05

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: 43.41  E-value: 6.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239658286 479 RLVAVIDEFhvlfeGNdaVARqaVALLEELARKGRSYGIHLVLASQTISGVEALF--AKTESIFGQFPLRIALAGG 552
Cdd:pfam12696   1 PVLFVLDEF-----AN--LGK--IPDLEKLISTGRSRGISLMLILQSIAQLEELYgkDGAETILGNCNTKVFLGGG 67
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
369-531 1.80e-03

KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 40.69  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 369 LVGGRTGSGKTVFLLDVLYGLASRYspDELGLYlldfkegVSFAEfTPTAVdpswIPHARTVGIESDR--EYGLAVLRTL 446
Cdd:pfam06745  23 LITGGPGTGKTIFGLQFLYNGALKY--GEPGVF-------VTLEE-PPEDL----RENARSFGWDLEKleEEGKLAIIDA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239658286 447 SREMTRRASELKRAGVTKLAD-LRTGRPDVAMPRLvaVIDEFHVLF-EGNDAVARQavaLLEELARKGRSYGIHLVLASQ 524
Cdd:pfam06745  89 STSGIGIAEVEDRFDLEELIErLREAIREIGAKRV--VIDSITTLFyLLKPAVARE---ILRRLKRVLKGLGVTAIFTSE 163

                  ....*..
gi 1239658286 525 TISGVEA 531
Cdd:pfam06745 164 KPSGEGG 170
 
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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