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Conserved domains on  [gi|1172645140|gb|ARD68017|]
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DNA translocase FtsK [Eubacterium limosum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 294-765 0e+00

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: 825.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 294 EADEVYHFPETTLLN-PPASGSKNRKDAVVKKAKIIEETLSNFGVHAKIVGVDVGPSITRFELQPDPGVKVNKIVNLADD 372
Cdd:COG1674   130 EALALAVLPPLDLLDpPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADD 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 373 LALNLATSDIRIEAPIPGKAAVGIEVPNEESVIVGLREIIETPAFENFKGPLPFALGKTLSGQNIIGDISKMPHVLIAGA 452
Cdd:COG1674   210 IALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 453 TGSGKSVCINSIIISLLYKASPEDLRFIMIDPKMVELNQYNAIPHLLIPVVTDPKKASYALNWGIKEMTDRYQLFKENGV 532
Cdd:COG1674   290 TGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGV 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 533 RDIDGYNELMA--------GQGGEKLPRIVIVVDELADLMMTSPKECENAICRIAQLARACGIHLIIATQRPSVDVITGL 604
Cdd:COG1674   370 RNIAGYNEKVReakakgeeEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGL 449

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 605 IKANIPSRIAFSVASNTDSRTILDMAGAEKLLGKGDMLYYPVGKSKPLRVQCTFVSDAEINRVINAVKPKKQPTYNDEIE 684
Cdd:COG1674   450 IKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEIL 529

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 685 EAINepQEEEEAKEDDLDPLFDQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIISGPNGSKPRTLLMTQEE 764
Cdd:COG1674   530 EEEE--EEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEE 607


                  .
gi 1172645140 765 Y 765
Cdd:COG1674   608 L 608
SQR_QFR_TM super family cl00881
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 7-94 2.88e-03

Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, transmembrane subunits; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol, while QFR catalyzes the reverse reaction. SQR, also called succinate dehydrogenase or Complex II, is part of the citric acid cycle and the aerobic respiratory chain, while QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQRs may reduce either high or low potential quinones while QFRs oxidize only low potential quinols. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit(s) containing the electron donor/acceptor (quinol or quinone). The reversible reduction of quinone is an essential feature of respiration, allowing the transfer of electrons between respiratory complexes. SQRs and QFRs can be classified into five types (A-E) according to the number of their hydrophobic subunits and heme groups. This classification is consistent with the characteristics and phylogeny of the catalytic and iron-sulfur subunits. Type E proteins, e.g. non-classical archael SQRs, contain atypical transmembrane subunits and are not included in this hierarchy. The heme and quinone binding sites reside in the transmembrane subunits. Although succinate oxidation and fumarate reduction are carried out by separate enzymes in most organisms, some bifunctional enzymes that exhibit both SQR and QFR activities exist.


The actual alignment was detected with superfamily member pfam01127:

Pssm-ID: 469971  Cd Length: 122  Bit Score: 38.52  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140   7 QRITGAVLAVLGLYVGYAFLTATPGILD---------KIVGKVIFTYMFGntTIMIALYMIAWGI-MLFFDKHKG-NIQT 75
Cdd:pfam01127  26 HRITGVALAVLGLIFLLLWLLLLLSLLGpesyatvvaWLASPVKLILLLL--LLLALFYHAANGIrHLIWDVGFGlELKT 103

                          90
                  ....*....|....*....
gi 1172645140  76 LVMVFLLLVNLMVVFSLNI 94
Cdd:pfam01127 104 VRKSGAAVLALSVVLVIVL 122
 
Name Accession Description Interval E-value
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 294-765 0e+00

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: 825.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 294 EADEVYHFPETTLLN-PPASGSKNRKDAVVKKAKIIEETLSNFGVHAKIVGVDVGPSITRFELQPDPGVKVNKIVNLADD 372
Cdd:COG1674   130 EALALAVLPPLDLLDpPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADD 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 373 LALNLATSDIRIEAPIPGKAAVGIEVPNEESVIVGLREIIETPAFENFKGPLPFALGKTLSGQNIIGDISKMPHVLIAGA 452
Cdd:COG1674   210 IALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 453 TGSGKSVCINSIIISLLYKASPEDLRFIMIDPKMVELNQYNAIPHLLIPVVTDPKKASYALNWGIKEMTDRYQLFKENGV 532
Cdd:COG1674   290 TGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGV 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 533 RDIDGYNELMA--------GQGGEKLPRIVIVVDELADLMMTSPKECENAICRIAQLARACGIHLIIATQRPSVDVITGL 604
Cdd:COG1674   370 RNIAGYNEKVReakakgeeEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGL 449

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 605 IKANIPSRIAFSVASNTDSRTILDMAGAEKLLGKGDMLYYPVGKSKPLRVQCTFVSDAEINRVINAVKPKKQPTYNDEIE 684
Cdd:COG1674   450 IKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEIL 529

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 685 EAINepQEEEEAKEDDLDPLFDQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIISGPNGSKPRTLLMTQEE 764
Cdd:COG1674   530 EEEE--EEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEE 607


                  .
gi 1172645140 765 Y 765
Cdd:COG1674   608 L 608
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 254-754 4.61e-155

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 486.13  E-value: 4.61e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  254 PEEQQESLfllPEKKQKQNKIVDELLDLSDDG---ENPVNPqmeadevyhFPETTLLNPPASGSKNRKD-AVVKKAKIIE 329
Cdd:PRK10263   828 PQYQQPQQ---PVAPQPQDTLLHPLLMRNGDSrplHKPTTP---------LPSLDLLTPPPSEVEPVDTfALEQMARLVE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  330 ETLSNFGVHAKIVGVDVGPSITRFELQPDPGVKVNKIVNLADDLALNLATSDIRIEAPIPGKAAVGIEVPNEESVIVGLR 409
Cdd:PRK10263   896 ARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLR 975

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  410 EIIETPAFENFKGPLPFALGKTLSGQNIIGDISKMPHVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPKMVEL 489
Cdd:PRK10263   976 EVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLEL 1055

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  490 NQYNAIPHLLIPVVTDPKKASYALNWGIKEMTDRYQLFKENGVRDIDGYNELMAGQGG---------------------- 547
Cdd:PRK10263  1056 SVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEADRmmrpipdpywkpgdsmdaqhpv 1135

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  548 -EKLPRIVIVVDELADLMMTSPKECENAICRIAQLARACGIHLIIATQRPSVDVITGLIKANIPSRIAFSVASNTDSRTI 626
Cdd:PRK10263  1136 lKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTI 1215

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  627 LDMAGAEKLLGKGDMLYYPVGKSKPLRVQCTFVSDAEINRVINAVKPKKQPTYNDEI-EEAINEPQEEEEAKEDDLDPLF 705
Cdd:PRK10263  1216 LDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGItSDSESEGGAGGFDGAEELDPLF 1295

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1172645140  706 DQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIIS--GPNGSK 754
Cdd:PRK10263  1296 DQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSeqGHNGNR 1346
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 408-597 1.23e-70

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: 230.73  E-value: 1.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 408 LREIIETPAFENFKGPLPFALGKTLSGQNIIGDISKMP-HVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPKM 486
Cdd:pfam01580   1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 487 VELNQYNAIPHLL-IPVVTDPKKASYALNWGIKEMTDRYQLFKENGVRDIDGYNELMA---------------------- 543
Cdd:pfam01580  81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflviygvhvmct 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1172645140 544 -GQGGEKLPRIVIVVDELADLMMTSPKEC----ENAICRIAQLARACGIHLIIATQRPS 597
Cdd:pfam01580 161 aGRWLEILPYLVVIVDERAELRLAAPKDSemrvEDAIVRLAQKGRAAGIHLLLATQRPS 219
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 445-627 1.53e-27

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: 120.09  E-value: 1.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  445 PHVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPK---MVelNQYNAIPHLLiPVVT--DPKKASYALNwGIK- 518
Cdd:TIGR03928  470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFKNLPHLL-GTITnlDGAQSMRALA-SIKa 545

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  519 EMTDRYQLFKENGVRDIDGYNELM-AGQGGEKLPRIVIVVDELADLMMTSP---KECENAicriAQLARACGIHLIIATQ 594
Cdd:TIGR03928  546 ELKKRQRLFGENNVNHINQYQKLYkQGKAKEPMPHLFLISDEFAELKSEQPefmKELVST----ARIGRSLGVHLILATQ 621

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1172645140  595 RPSvDVITGLIKANIPSRIAFSVASNTDSRTIL 627
Cdd:TIGR03928  622 KPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
Ftsk_gamma smart00843
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ...
 699-761 1.89e-24

This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.


Pssm-ID: 197911 [Multi-domain]  Cd Length: 63  Bit Score: 96.71  E-value: 1.89e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172645140  699 DDLDPLFDQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIISGPNGSKPRTLLMT 761
Cdd:smart00843   1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 446-617 1.20e-07

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: 51.45  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 446 HVLIAGATGSGKSVCINSIIISLLykasPEDLRFIMIDPKMvELNqynaiphLLIPV--VTDPKKASYALNWgikemtdr 523
Cdd:cd01127     1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKG-ELF-------LVIPDrdDSFAALRALFFNQ-------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 524 yqLFKENgvrdidgyNELMAGQGGEKLPRIVIVVDELADLmmtspkecenaiCRIAQLARAC------GIHLIIATQ--- 594
Cdd:cd01127    61 --LFRAL--------TELASLSPGRLPRRVWFILDEFANL------------GRIPNLPNLLatgrkrGISVVLILQsla 118

                         170       180
                  ....*....|....*....|....*.
gi 1172645140 595 ---RPSVDVITGLIKANIPSRIAFSV 617
Cdd:cd01127   119 qleAVYGKDGAQTILGNCNTKLYLGT 144
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 7-94 2.88e-03

Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a transmembrane protein from both the Succinate dehydrogenase and Fumarate reductase complexes.


Pssm-ID: 426067  Cd Length: 122  Bit Score: 38.52  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140   7 QRITGAVLAVLGLYVGYAFLTATPGILD---------KIVGKVIFTYMFGntTIMIALYMIAWGI-MLFFDKHKG-NIQT 75
Cdd:pfam01127  26 HRITGVALAVLGLIFLLLWLLLLLSLLGpesyatvvaWLASPVKLILLLL--LLLALFYHAANGIrHLIWDVGFGlELKT 103

                          90
                  ....*....|....*....
gi 1172645140  76 LVMVFLLLVNLMVVFSLNI 94
Cdd:pfam01127 104 VRKSGAAVLALSVVLVIVL 122
 
Name Accession Description Interval E-value
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 294-765 0e+00

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: 825.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 294 EADEVYHFPETTLLN-PPASGSKNRKDAVVKKAKIIEETLSNFGVHAKIVGVDVGPSITRFELQPDPGVKVNKIVNLADD 372
Cdd:COG1674   130 EALALAVLPPLDLLDpPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADD 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 373 LALNLATSDIRIEAPIPGKAAVGIEVPNEESVIVGLREIIETPAFENFKGPLPFALGKTLSGQNIIGDISKMPHVLIAGA 452
Cdd:COG1674   210 IALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 453 TGSGKSVCINSIIISLLYKASPEDLRFIMIDPKMVELNQYNAIPHLLIPVVTDPKKASYALNWGIKEMTDRYQLFKENGV 532
Cdd:COG1674   290 TGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGV 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 533 RDIDGYNELMA--------GQGGEKLPRIVIVVDELADLMMTSPKECENAICRIAQLARACGIHLIIATQRPSVDVITGL 604
Cdd:COG1674   370 RNIAGYNEKVReakakgeeEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGL 449

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 605 IKANIPSRIAFSVASNTDSRTILDMAGAEKLLGKGDMLYYPVGKSKPLRVQCTFVSDAEINRVINAVKPKKQPTYNDEIE 684
Cdd:COG1674   450 IKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEIL 529

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 685 EAINepQEEEEAKEDDLDPLFDQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIISGPNGSKPRTLLMTQEE 764
Cdd:COG1674   530 EEEE--EEDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEE 607


                  .
gi 1172645140 765 Y 765
Cdd:COG1674   608 L 608
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 254-754 4.61e-155

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 486.13  E-value: 4.61e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  254 PEEQQESLfllPEKKQKQNKIVDELLDLSDDG---ENPVNPqmeadevyhFPETTLLNPPASGSKNRKD-AVVKKAKIIE 329
Cdd:PRK10263   828 PQYQQPQQ---PVAPQPQDTLLHPLLMRNGDSrplHKPTTP---------LPSLDLLTPPPSEVEPVDTfALEQMARLVE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  330 ETLSNFGVHAKIVGVDVGPSITRFELQPDPGVKVNKIVNLADDLALNLATSDIRIEAPIPGKAAVGIEVPNEESVIVGLR 409
Cdd:PRK10263   896 ARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLR 975

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  410 EIIETPAFENFKGPLPFALGKTLSGQNIIGDISKMPHVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPKMVEL 489
Cdd:PRK10263   976 EVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLEL 1055

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  490 NQYNAIPHLLIPVVTDPKKASYALNWGIKEMTDRYQLFKENGVRDIDGYNELMAGQGG---------------------- 547
Cdd:PRK10263  1056 SVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEADRmmrpipdpywkpgdsmdaqhpv 1135

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  548 -EKLPRIVIVVDELADLMMTSPKECENAICRIAQLARACGIHLIIATQRPSVDVITGLIKANIPSRIAFSVASNTDSRTI 626
Cdd:PRK10263  1136 lKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTI 1215

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  627 LDMAGAEKLLGKGDMLYYPVGKSKPLRVQCTFVSDAEINRVINAVKPKKQPTYNDEI-EEAINEPQEEEEAKEDDLDPLF 705
Cdd:PRK10263  1216 LDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGItSDSESEGGAGGFDGAEELDPLF 1295

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1172645140  706 DQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIIS--GPNGSK 754
Cdd:PRK10263  1296 DQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSeqGHNGNR 1346
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 408-597 1.23e-70

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: 230.73  E-value: 1.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 408 LREIIETPAFENFKGPLPFALGKTLSGQNIIGDISKMP-HVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPKM 486
Cdd:pfam01580   1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 487 VELNQYNAIPHLL-IPVVTDPKKASYALNWGIKEMTDRYQLFKENGVRDIDGYNELMA---------------------- 543
Cdd:pfam01580  81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflviygvhvmct 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1172645140 544 -GQGGEKLPRIVIVVDELADLMMTSPKEC----ENAICRIAQLARACGIHLIIATQRPS 597
Cdd:pfam01580 161 aGRWLEILPYLVVIVDERAELRLAAPKDSemrvEDAIVRLAQKGRAAGIHLLLATQRPS 219
FtsK_alpha pfam17854
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ...
 301-400 3.53e-41

FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.


Pssm-ID: 436096 [Multi-domain]  Cd Length: 101  Bit Score: 145.76  E-value: 3.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 301 FPETTLLNPP-ASGSKNRKDAVVKKAKIIEETLSNFGVHAKIVGVDVGPSITRFELQPDPGVKVNKIVNLADDLALNLAT 379
Cdd:pfam17854   1 LPPLDLLEPPpTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80

                          90       100
                  ....*....|....*....|.
gi 1172645140 380 SDIRIEAPIPGKAAVGIEVPN 400
Cdd:pfam17854  81 PSIRIVAPIPGKSTIGIEVPN 101
FtsK_gamma pfam09397
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ...
 699-761 2.79e-28

Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.


Pssm-ID: 462786 [Multi-domain]  Cd Length: 63  Bit Score: 107.84  E-value: 2.79e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172645140 699 DDLDPLFDQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIISGPNGSKPRTLLMT 761
Cdd:pfam09397   1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 445-627 1.53e-27

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: 120.09  E-value: 1.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  445 PHVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPK---MVelNQYNAIPHLLiPVVT--DPKKASYALNwGIK- 518
Cdd:TIGR03928  470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFKNLPHLL-GTITnlDGAQSMRALA-SIKa 545

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  519 EMTDRYQLFKENGVRDIDGYNELM-AGQGGEKLPRIVIVVDELADLMMTSP---KECENAicriAQLARACGIHLIIATQ 594
Cdd:TIGR03928  546 ELKKRQRLFGENNVNHINQYQKLYkQGKAKEPMPHLFLISDEFAELKSEQPefmKELVST----ARIGRSLGVHLILATQ 621

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1172645140  595 RPSvDVITGLIKANIPSRIAFSVASNTDSRTIL 627
Cdd:TIGR03928  622 KPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
Ftsk_gamma smart00843
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ...
 699-761 1.89e-24

This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.


Pssm-ID: 197911 [Multi-domain]  Cd Length: 63  Bit Score: 96.71  E-value: 1.89e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172645140  699 DDLDPLFDQAVETAFTYNQVSTSMLQRKLKVGYARAGRLIDSLEQKGIISGPNGSKPRTLLMT 761
Cdd:smart00843   1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
 445-660 4.28e-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: 4.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 445 PHVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPK-------MVELNQYNA-IPHL-----LIPVVTDpkkasy 511
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatflgLEGLPHVSAvITNLadeapLVDRMQD------ 509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 512 ALnWGikEMTDRYQLFKENG-VRDIDGYNEL-MAGQGGEKLPRIVIVVDELADLMMTSPKECE--NAICRiaqLARACGI 587
Cdd:TIGR03924 510 AL-AG--EMNRRQELLRAAGnFANVAEYEKArAAGADLPPLPALFVVVDEFSELLSQHPDFADlfVAIGR---LGRSLGV 583

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172645140 588 HLIIATQRPSVDVITGLiKANIPSRIAFSVASNTDSRTILDMAGAEKLLGKGDMLYYPVGKSKPLRVQCTFVS 660
Cdd:TIGR03924 584 HLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYVS 655
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 440-627 3.58e-17

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: 86.58  E-value: 3.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  440 DISKMPHVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPKMVELNQYNAIPHLL-IPVVTDPKKASYALNWGIK 518
Cdd:TIGR03928  806 DLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVAdYFTLDEEEKIEKLIRRIKK 885

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  519 EMTDRYQLFKENGVRDIDGYNELmagqGGEKLPRIVIVVDELaDLMMTSP--KECENAICRIAQLARACGIHLII-ATQR 595
Cdd:TIGR03928  886 EIDRRKKLFSEYGVASISMYNKA----SGEKLPQIVIIIDNY-DAVKEEPfyEDFEELLIQLAREGASLGIYLVMtAGRQ 960

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1172645140  596 PSVDVItglIKANIPSRIAFSVASNTDSRTIL 627
Cdd:TIGR03928  961 NAVRMP---LMNNIKTKIALYLIDKSEYRSIV 989
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 446-623 4.11e-10

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: 63.09  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 446 HVLIAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPKMVELNQYNAIPHlLIPVVT--DPKKASYALNWGIKEMTDR 523
Cdd:TIGR03925  81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGrlDPERVRRTVAEVEGLLRRR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 524 YQLFKENGVRDIDGYNELMAGQGGEKLPR--IVIVVDELADLmMTSPKECENAICRIAQLARACGIHLIIATQRPSvdVI 601
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRARRAAGRLPEDPFgdVFLVIDGWGTL-RQDFEDLEDKVTDLAARGLAYGVHVVLTASRWS--EI 236

                         170       180
                  ....*....|....*....|..
gi 1172645140 602 TGLIKANIPSRIAFSVASNTDS 623
Cdd:TIGR03925 237 RPALRDLIGTRIELRLGDPMDS 258
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 425-672 3.16e-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: 59.62  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 425 PFALGKTLS-GQNIIGDISKM--PHVLIAGATGSGKSVCINSIIISLLYKASPedlrFIMIDPK------------MVEL 489
Cdd:COG0433    25 GILIGKLLSpGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDPHgeysglaepgaeRADV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 490 NQYNAIPHLLIPV---------------------------------------------------------------VTDP 506
Cdd:COG0433   101 GVFDPGAGRPLPInpwdlfataselgplllsrldlndtqrgvlrealrladdkglllldlkdlialleegeelgeeYGNV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 507 KKASY-ALNWGIKEMTDRYQLFKENGVR--------------DIDGYNE------------------LMAGQGGEKLPRI 553
Cdd:COG0433   181 SAASAgALLRRLESLESADGLFGEPGLDledllrtdgrvtviDLSGLPEelqstfvlwllrelfearPEVGDADDRKLPL 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 554 VIVVDELADLMMTSPKECENAICRIAQLARACGIHLIIATQRPSvDVITGlIKANIPSRIAFSVASNTDSRTILDMAGAE 633
Cdd:COG0433   261 VLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLFNPRDQKAVKAAAETL 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1172645140 634 KL--------LGKGDMLYYPVGKSKPLRVQCTFVSDAEINRVINAVK 672
Cdd:COG0433   339 SEdllerlpsLGTGEALVLGEGIPLPVLVKIRLPESRPGGESPDLVR 385
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 446-617 1.20e-07

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: 51.45  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 446 HVLIAGATGSGKSVCINSIIISLLykasPEDLRFIMIDPKMvELNqynaiphLLIPV--VTDPKKASYALNWgikemtdr 523
Cdd:cd01127     1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKG-ELF-------LVIPDrdDSFAALRALFFNQ-------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 524 yqLFKENgvrdidgyNELMAGQGGEKLPRIVIVVDELADLmmtspkecenaiCRIAQLARAC------GIHLIIATQ--- 594
Cdd:cd01127    61 --LFRAL--------TELASLSPGRLPRRVWFILDEFANL------------GRIPNLPNLLatgrkrGISVVLILQsla 118

                         170       180
                  ....*....|....*....|....*.
gi 1172645140 595 ---RPSVDVITGLIKANIPSRIAFSV 617
Cdd:cd01127   119 qleAVYGKDGAQTILGNCNTKLYLGT 144
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 370-592 1.02e-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: 45.75  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 370 ADDLALNLATSDIRIEAPIPGKAAVGIeVPNeesvIVGLREIIETPAFENfkGPLPFALGKT-LSGQNIigDISKMPHVL 448
Cdd:TIGR03925 297 VDDLGTRGLVAVIRDVWGGPPAPPVRL-LPA----RLPLSALPAGGGAPR--LRVPLGLGESdLAPVYV--DFAESPHLL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 449 IAGATGSGKSVCINSIIISLLYKASPEDLRFIMIDPKmvelnqynaipHLLIPVVTDPKKASYALNWGI--KEMTDRYQL 526
Cdd:TIGR03925 368 IFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR-----------RTLLGAVPEDYLAGYAATSAAltELIAALAAL 436

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1172645140 527 FKEngvR----DIDGyNELMAGQGGEKlPRIVIVVDELaDLMMTSPkecENAICRIAQL---ARACGIHLIIA 592
Cdd:TIGR03925 437 LER---RlpgpDVTP-QQLRARSWWSG-PEIYVVVDDY-DLVATGS---GNPLAPLVELlphARDIGLHVVVA 500
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 423-484 1.02e-04

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


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 45.71  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172645140 423 PLPFALGKTLSGQNIIGDISKM---PHVLIAGATGSGKSVCINSIIISLLYKaspeDLRFIMIDP 484
Cdd:COG3451   180 PWGIYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 421-654 1.04e-04

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: 46.13  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  421 KGPLPFALG-KTLSGQNIigDISKMPHVLIAGATGSGKSVCINSIIISLLYKaspEDLRFIMIDPKMVELNQYNAIPHLl 499
Cdd:TIGR03928 1074 EGSIPIGLDeETVEPVYI--DLTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGLIDSIDRGLLAYRDLKEV- 1147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  500 ipvvtdpkkASYALNW-GIKEMTDryQLFKENGVRDIDGYNELMAGQGGEKLPRIVIVVDELADLMMTSPKECENAICRI 578
Cdd:TIGR03928 1148 ---------ATYIEEKeDLKEILA--ELKEEIELREAAYKEALQNETGEPAFKPILLIIDDLEDFIQRTDLEIQDILALI 1216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  579 AQLARACGIHLIIATQRPSV----DVITGLIKAnipSRIAFSVASNTDSRTI-LDMAGAEKLLGKGDMLYYPVGKSKPLR 653
Cdd:TIGR03928 1217 MKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQSFFkLPFTRSEKELEPGEGYFVVNGKYQKIK 1293


                   .
gi 1172645140  654 V 654
Cdd:TIGR03928 1294 I 1294
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
 446-485 1.30e-03

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: 41.89  E-value: 1.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1172645140 446 HVLIAGATGSGKSVcinSIIISLLYKASPEDlRFIMIDPK 485
Cdd:COG3505     1 HVLVIGPTGSGKTV---GLVIPNLTQLARGE-SVVVTDPK 36
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 7-94 2.88e-03

Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a transmembrane protein from both the Succinate dehydrogenase and Fumarate reductase complexes.


Pssm-ID: 426067  Cd Length: 122  Bit Score: 38.52  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140   7 QRITGAVLAVLGLYVGYAFLTATPGILD---------KIVGKVIFTYMFGntTIMIALYMIAWGI-MLFFDKHKG-NIQT 75
Cdd:pfam01127  26 HRITGVALAVLGLIFLLLWLLLLLSLLGpesyatvvaWLASPVKLILLLL--LLLALFYHAANGIrHLIWDVGFGlELKT 103

                          90
                  ....*....|....*....
gi 1172645140  76 LVMVFLLLVNLMVVFSLNI 94
Cdd:pfam01127 104 VRKSGAAVLALSVVLVIVL 122
AAA_10 pfam12846
AAA-like domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 432-529 5.55e-03

AAA-like domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins, including VirB4 components of the Type IV secretory pathway and conjugal transfer protein TrbE. This entry includes the arcaheal Vir4/HerA homolog CedB, a membrane-bound protein that is highly induced upon UV treatment and essential for DNA transfer between Sulfolobus cells.


Pssm-ID: 315512 [Multi-domain]  Cd Length: 362  Bit Score: 39.69  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140 432 LSGQNIIGDISKMPHVLIAGATGSGKSVCINSIIisllYKASPEDLRFIMIDPKMVELNQYNAIPHLL--IPVVT-DPKK 508
Cdd:pfam12846   9 LANQGVKGSKTNAPHSAIIGDLGGGKSVLNKTLF----YYIVLLGGKALYIDPKKERGQWKETLPEIAheINFVTlDSET 84

                          90       100
                  ....*....|....*....|.
gi 1172645140 509 AsyalNWGikeMTDRYQLFKE 529
Cdd:pfam12846  85 E----NHG---LLDPIVLLPR 98
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 443-615 9.87e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 37.35  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  443 KMPHVLIAGATGSGKSVCINSIIisllYKASPEDLRFIMIDPkmvelnqynaiphllipvvTDPKKASYALNWGIKEMTD 522
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA----RELGPPGGGVIYIDG-------------------EDILEEVLDQLLLIIVGGK 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172645140  523 RYQLFKENGVRDIdgyNELMagqggEKLPRIVIVVDELADLMMTSPKECENAICR---IAQLARACGIHLIIATQRPSvD 599
Cdd:smart00382  58 KASGSGELRLRLA---LALA-----RKLKPDVLILDEITSLLDAEQEALLLLLEElrlLLLLKSEKNLTVILTTNDEK-D 128

                          170
                   ....*....|....*.
gi 1172645140  600 VITGLIKANIPSRIAF 615
Cdd:smart00382 129 LGPALLRRRFDRRIVL 144
 
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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