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Conserved domains on  [gi|1586070552|gb|QBJ14027|]
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DNA translocase FtsK [Agrobacterium sp. 33MFTa1.1]

Protein Classification

DNA translocase FtsK( domain architecture ID 12144184)

DNA translocase FtsK is a motor that converts the chemical energy of binding and hydrolyzing ATP into movement of the double-stranded DNA substrate

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, ...
359-886 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: 863.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 359 ITAPSARPKPSERVAREAQASFIAADGFQLPTVHLLAEPKNivRDNTLSEEVLEQNARLLEGVLEDFGVKGEIIHVRPGP 438
Cdd:COG1674   108 LGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPP--KKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGP 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 439 VVTLYELEPAPGIKSSRVIGLADDIARSMSAIAARV-AVVPGRNAIGIELPNQTRETVFLRELIGSRDFENSKAKLAMAL 517
Cdd:COG1674   186 VVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIeAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIAL 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 518 GKTIGGEPVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPKMLELSIYDGIPHLLSPVVTDPKK 597
Cdd:COG1674   266 GKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKK 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 598 AVVALKWTVREMEERYKKMSKIGVRNIDGFNSRVQQALDKGEiltrtvqtgfdrqtgeaiyetEEFDLKPLPYIVVIIDE 677
Cdd:COG1674   346 AANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGE---------------------EEEGLEPLPYIVVIIDE 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 678 MADLMMVAGKDIEGAVQRLAQMARAAGIHVIMATQRPSVDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGMG 757
Cdd:COG1674   405 LADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRG 484
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 758 DMLYMA-GGGRIQRVHGPFVSDNEVEEIVSYLKTQGSPEYLEEITEEEDEDGAGASpaggasfSDSEDP-YDQAVAVVLR 835
Cdd:COG1674   485 DMLFLPpGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGD-------DDEDDElFDEAVELVVE 557
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1586070552 836 DGKASTSYVQRRLGIGYNRAASLIERMEQEGIIGPANHAGKREILVPTEAD 886
Cdd:COG1674   558 TQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEEL 608
FtsK_4TM pfam13491
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ...
22-184 7.68e-19

4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.


:

Pssm-ID: 463896  Cd Length: 171  Bit Score: 84.56  E-value: 7.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  22 FVRQIMALAGFALLATIALgiaALATWNVADPSLSY--ATGNQPTNLLGYGGAIFADIVMQFLGLSAIisLLPV--IAWA 97
Cdd:pfam13491   3 LLRELLGLALLLLGLFLLL---ALVSYSPADPSWSTsgSGAAPVHNWGGRFGAWLADLLLQLFGYSAW--LLPValLYWG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  98 IALIAGRKLQRIPARLVAWIAGAIVCAASLGCFPAPVTWPLPNGIGGVIGDMILRFPALFIGAypTGTVATILGVIFAAp 177
Cdd:pfam13491  78 WRLFRRRSLERRWLRLLGFLLLLLASSALFALRLPSLEFGLPGGAGGVIGRLLANALVTLLGF--TGATLLLLALLAIG- 154

                  ....*..
gi 1586070552 178 atwLMLF 184
Cdd:pfam13491 155 ---LSLV 158
 
Name Accession Description Interval E-value
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
359-886 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: 863.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 359 ITAPSARPKPSERVAREAQASFIAADGFQLPTVHLLAEPKNivRDNTLSEEVLEQNARLLEGVLEDFGVKGEIIHVRPGP 438
Cdd:COG1674   108 LGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPP--KKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGP 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 439 VVTLYELEPAPGIKSSRVIGLADDIARSMSAIAARV-AVVPGRNAIGIELPNQTRETVFLRELIGSRDFENSKAKLAMAL 517
Cdd:COG1674   186 VVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIeAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIAL 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 518 GKTIGGEPVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPKMLELSIYDGIPHLLSPVVTDPKK 597
Cdd:COG1674   266 GKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKK 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 598 AVVALKWTVREMEERYKKMSKIGVRNIDGFNSRVQQALDKGEiltrtvqtgfdrqtgeaiyetEEFDLKPLPYIVVIIDE 677
Cdd:COG1674   346 AANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGE---------------------EEEGLEPLPYIVVIIDE 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 678 MADLMMVAGKDIEGAVQRLAQMARAAGIHVIMATQRPSVDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGMG 757
Cdd:COG1674   405 LADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRG 484
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 758 DMLYMA-GGGRIQRVHGPFVSDNEVEEIVSYLKTQGSPEYLEEITEEEDEDGAGASpaggasfSDSEDP-YDQAVAVVLR 835
Cdd:COG1674   485 DMLFLPpGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGD-------DDEDDElFDEAVELVVE 557
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1586070552 836 DGKASTSYVQRRLGIGYNRAASLIERMEQEGIIGPANHAGKREILVPTEAD 886
Cdd:COG1674   558 TQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEEL 608
PRK10263 PRK10263
DNA translocase FtsK; Provisional
263-882 2.52e-178

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 551.61  E-value: 2.52e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  263 HPYDFNEYEFGTL--------NEPsrLKTAInrLDQRAEPSFEERTASRRQMSPPSIAPSHEDDGDGEPSFGTDEARLPS 334
Cdd:PRK10263   720 NPFSLDDFEFSPMkallddgpHEP--LFTPI--VEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQ 795
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  335 GILSDDDIDQKFTARQAPGRGQTKITAPSARP----KPSERVAREAQASFI----AADG---------FQLPTVHLLAEP 397
Cdd:PRK10263   796 QPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQpqyqQPQQPVAPQPQDTLLhpllMRNGdsrplhkptTPLPSLDLLTPP 875
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  398 KNIVRD-NTLSeevLEQNARLLEGVLEDFGVKGEIIHVRPGPVVTLYELEPAPGIKSSRVIGLADDIARSMSAIAARVA- 475
Cdd:PRK10263   876 PSEVEPvDTFA---LEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVe 952
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  476 VVPGRNAIGIELPNQTRETVFLRELIGSRDFENSKAKLAMALGKTIGGEPVIADLAKMPHLLVAGTTGSGKSVAINTMIL 555
Cdd:PRK10263   953 VIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMIL 1032
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  556 SLLYRMSPEQCRLIMIDPKMLELSIYDGIPHLLSPVVTDPKKAVVALKWTVREMEERYKKMSKIGVRNIDGFNSRVQQAL 635
Cdd:PRK10263  1033 SMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEAD 1112
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  636 DKGeiltRTVQTGFdRQTGEAIyETEEFDLKPLPYIVVIIDEMADLMMVAGKDIEGAVQRLAQMARAAGIHVIMATQRPS 715
Cdd:PRK10263  1113 RMM----RPIPDPY-WKPGDSM-DAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPS 1186
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  716 VDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGMGDMLYMAGGGRIQ-RVHGPFVSDNEVEEIVSYLKTQGSP 794
Cdd:PRK10263  1187 VDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPvRVHGAFVRDQEVHAVVQDWKARGRP 1266
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  795 EYLEEITeeededgagaspaggasfSDSE--------------DP-YDQAVAVVLRDGKASTSYVQRRLGIGYNRAASLI 859
Cdd:PRK10263  1267 QYVDGIT------------------SDSEseggaggfdgaeelDPlFDQAVQFVTEKRKASISGVQRQFRIGYNRAARII 1328
                          650       660
                   ....*....|....*....|...
gi 1586070552  860 ERMEQEGIIGPANHAGKREILVP 882
Cdd:PRK10263  1329 EQMEAQGIVSEQGHNGNREVLAP 1351
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
497-715 1.51e-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: 232.27  E-value: 1.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 497 LRELIGSRDFENSKAKLAMALGKTIGGEPVIADLAKMP-HLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPKM 575
Cdd:pfam01580   1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 576 LELSIYDGIPHLLS-PVVTDPKKAVVALKWTVREMEERYKKMSKIGVRNIDGFNSRVQQALDKGEILTRTVQTGFDrqtg 654
Cdd:pfam01580  81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVH---- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586070552 655 eaIYETEEFDLKPLPYIVVIIDEMADLMMVAGKD----IEGAVQRLAQMARAAGIHVIMATQRPS 715
Cdd:pfam01580 157 --VMCTAGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
Ftsk_gamma smart00843
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ...
821-882 3.14e-29

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: 110.58  E-value: 3.14e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586070552  821 DSEDP-YDQAVAVVLRDGKASTSYVQRRLGIGYNRAASLIERMEQEGIIGPANHAGKREILVP 882
Cdd:smart00843   1 EEEDElYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
513-746 1.49e-20

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: 97.75  E-value: 1.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  513 LAMALGKTIGGEPVIADL---AKMPHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPK---MLELsiYDGIPH 586
Cdd:TIGR03928  446 LAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPH 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  587 LLSpVVTD-----PKKAVVALKwtvREMEERYKKMSKIGVRNIDGFnsrvqQALDKGEILTrtvqtgfdrqtgeaiyete 661
Cdd:TIGR03928  524 LLG-TITNldgaqSMRALASIK---AELKKRQRLFGENNVNHINQY-----QKLYKQGKAK------------------- 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  662 efdlKPLPYIVVIIDEMADL------MMvagKDIEGAvqrlAQMARAAGIHVIMATQRPSvDVITGTIKANFPTRISFQV 735
Cdd:TIGR03928  576 ----EPMPHLFLISDEFAELkseqpeFM---KELVST----ARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKV 643
                          250
                   ....*....|.
gi 1586070552  736 TSKIDSRTILG 746
Cdd:TIGR03928  644 QDASDSNEILK 654
FtsK_4TM pfam13491
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ...
22-184 7.68e-19

4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.


Pssm-ID: 463896  Cd Length: 171  Bit Score: 84.56  E-value: 7.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  22 FVRQIMALAGFALLATIALgiaALATWNVADPSLSY--ATGNQPTNLLGYGGAIFADIVMQFLGLSAIisLLPV--IAWA 97
Cdd:pfam13491   3 LLRELLGLALLLLGLFLLL---ALVSYSPADPSWSTsgSGAAPVHNWGGRFGAWLADLLLQLFGYSAW--LLPValLYWG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  98 IALIAGRKLQRIPARLVAWIAGAIVCAASLGCFPAPVTWPLPNGIGGVIGDMILRFPALFIGAypTGTVATILGVIFAAp 177
Cdd:pfam13491  78 WRLFRRRSLERRWLRLLGFLLLLLASSALFALRLPSLEFGLPGGAGGVIGRLLANALVTLLGF--TGATLLLLALLAIG- 154

                  ....*..
gi 1586070552 178 atwLMLF 184
Cdd:pfam13491 155 ---LSLV 158
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
535-735 1.06e-05

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: 46.06  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 535 HLLVAGTTGSGKSVAINTMILSLLyrmsPEQCRLIMIDPKM---LELSIYDGIPHLLSPVVTdpkkavvalkwtvremee 611
Cdd:cd01127     1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKGelfLVIPDRDDSFAALRALFF------------------ 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 612 rykkmskigvrnidgfnsrvqqaldkgEILTRTVQTGFDRQTGeaiyeteefdlKPLPYIVVIIDEMADLMMvagkdIEG 691
Cdd:cd01127    59 ---------------------------NQLFRALTELASLSPG-----------RLPRRVWFILDEFANLGR-----IPN 95
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1586070552 692 AVQRLAQmARAAGIHVIMATQ------RPSVDVITGTIKANFPTRISFQV 735
Cdd:cd01127    96 LPNLLAT-GRKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
MFS_MMR_MDR_like cd17321
Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance ...
21-151 9.17e-03

Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of bacterial, fungal, and archaeal multidrug resistance (MDR) transporters including several proteins from Bacilli such as methylenomycin A resistance protein (also called MMR peptide), tetracycline resistance protein (TetB), and lincomycin resistance protein LmrB, as well as fungal proteins such as vacuolar basic amino acid transporters, which are involved in the transport into vacuoles of the basic amino acids histidine, lysine, and arginine in Saccharomyces cerevisiae, and aminotriazole/azole resistance proteins. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. For example, MMR confers resistance to the epoxide antibiotic methylenomycin while TetB resistance to tetracycline by an active tetracycline efflux. MMR-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340879 [Multi-domain]  Cd Length: 370  Bit Score: 39.46  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  21 FFVRQIMALAGFALLATIALGIAALATWNvadpslsyatgnqptnlLGYGGAIFadIVMQFL----GLSAIISLLPVIAW 96
Cdd:cd17321   153 FLINVPIGLVALLLARTFSGAVLAAFLLG-----------------AALGGLLF--LLPLYLqgvlGYSPLQAGLALLPL 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  97 AI-----ALIAGRKLQRIPARLVAwIAGAIVCAASLGCFpapVTWPLPNGIGGVIGDMIL 151
Cdd:cd17321   214 ALamlvaAPLAGRLADRFGPRLVL-VAGLLLTAVGLLLL---ALLGADSSVWLLLPGLVL 269
 
Name Accession Description Interval E-value
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
359-886 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: 863.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 359 ITAPSARPKPSERVAREAQASFIAADGFQLPTVHLLAEPKNivRDNTLSEEVLEQNARLLEGVLEDFGVKGEIIHVRPGP 438
Cdd:COG1674   108 LGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPP--KKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGP 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 439 VVTLYELEPAPGIKSSRVIGLADDIARSMSAIAARV-AVVPGRNAIGIELPNQTRETVFLRELIGSRDFENSKAKLAMAL 517
Cdd:COG1674   186 VVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIeAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIAL 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 518 GKTIGGEPVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPKMLELSIYDGIPHLLSPVVTDPKK 597
Cdd:COG1674   266 GKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKK 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 598 AVVALKWTVREMEERYKKMSKIGVRNIDGFNSRVQQALDKGEiltrtvqtgfdrqtgeaiyetEEFDLKPLPYIVVIIDE 677
Cdd:COG1674   346 AANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGE---------------------EEEGLEPLPYIVVIIDE 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 678 MADLMMVAGKDIEGAVQRLAQMARAAGIHVIMATQRPSVDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGMG 757
Cdd:COG1674   405 LADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRG 484
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 758 DMLYMA-GGGRIQRVHGPFVSDNEVEEIVSYLKTQGSPEYLEEITEEEDEDGAGASpaggasfSDSEDP-YDQAVAVVLR 835
Cdd:COG1674   485 DMLFLPpGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGD-------DDEDDElFDEAVELVVE 557
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1586070552 836 DGKASTSYVQRRLGIGYNRAASLIERMEQEGIIGPANHAGKREILVPTEAD 886
Cdd:COG1674   558 TQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEEL 608
PRK10263 PRK10263
DNA translocase FtsK; Provisional
263-882 2.52e-178

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 551.61  E-value: 2.52e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  263 HPYDFNEYEFGTL--------NEPsrLKTAInrLDQRAEPSFEERTASRRQMSPPSIAPSHEDDGDGEPSFGTDEARLPS 334
Cdd:PRK10263   720 NPFSLDDFEFSPMkallddgpHEP--LFTPI--VEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQ 795
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  335 GILSDDDIDQKFTARQAPGRGQTKITAPSARP----KPSERVAREAQASFI----AADG---------FQLPTVHLLAEP 397
Cdd:PRK10263   796 QPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQpqyqQPQQPVAPQPQDTLLhpllMRNGdsrplhkptTPLPSLDLLTPP 875
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  398 KNIVRD-NTLSeevLEQNARLLEGVLEDFGVKGEIIHVRPGPVVTLYELEPAPGIKSSRVIGLADDIARSMSAIAARVA- 475
Cdd:PRK10263   876 PSEVEPvDTFA---LEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVe 952
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  476 VVPGRNAIGIELPNQTRETVFLRELIGSRDFENSKAKLAMALGKTIGGEPVIADLAKMPHLLVAGTTGSGKSVAINTMIL 555
Cdd:PRK10263   953 VIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMIL 1032
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  556 SLLYRMSPEQCRLIMIDPKMLELSIYDGIPHLLSPVVTDPKKAVVALKWTVREMEERYKKMSKIGVRNIDGFNSRVQQAL 635
Cdd:PRK10263  1033 SMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEAD 1112
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  636 DKGeiltRTVQTGFdRQTGEAIyETEEFDLKPLPYIVVIIDEMADLMMVAGKDIEGAVQRLAQMARAAGIHVIMATQRPS 715
Cdd:PRK10263  1113 RMM----RPIPDPY-WKPGDSM-DAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPS 1186
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  716 VDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGMGDMLYMAGGGRIQ-RVHGPFVSDNEVEEIVSYLKTQGSP 794
Cdd:PRK10263  1187 VDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPvRVHGAFVRDQEVHAVVQDWKARGRP 1266
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  795 EYLEEITeeededgagaspaggasfSDSE--------------DP-YDQAVAVVLRDGKASTSYVQRRLGIGYNRAASLI 859
Cdd:PRK10263  1267 QYVDGIT------------------SDSEseggaggfdgaeelDPlFDQAVQFVTEKRKASISGVQRQFRIGYNRAARII 1328
                          650       660
                   ....*....|....*....|...
gi 1586070552  860 ERMEQEGIIGPANHAGKREILVP 882
Cdd:PRK10263  1329 EQMEAQGIVSEQGHNGNREVLAP 1351
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
497-715 1.51e-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: 232.27  E-value: 1.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 497 LRELIGSRDFENSKAKLAMALGKTIGGEPVIADLAKMP-HLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPKM 575
Cdd:pfam01580   1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 576 LELSIYDGIPHLLS-PVVTDPKKAVVALKWTVREMEERYKKMSKIGVRNIDGFNSRVQQALDKGEILTRTVQTGFDrqtg 654
Cdd:pfam01580  81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVH---- 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586070552 655 eaIYETEEFDLKPLPYIVVIIDEMADLMMVAGKD----IEGAVQRLAQMARAAGIHVIMATQRPS 715
Cdd:pfam01580 157 --VMCTAGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
FtsK_alpha pfam17854
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ...
388-489 5.37e-39

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: 139.98  E-value: 5.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 388 LPTVHLLAEPKNIVRdnTLSEEVLEQNARLLEGVLEDFGVKGEIIHVRPGPVVTLYELEPAPGIKSSRVIGLADDIARSM 467
Cdd:pfam17854   1 LPPLDLLEPPPTSSQ--KVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALAL 78
                          90       100
                  ....*....|....*....|...
gi 1586070552 468 SAIAARV-AVVPGRNAIGIELPN 489
Cdd:pfam17854  79 SAPSIRIvAPIPGKSTIGIEVPN 101
FtsK_gamma pfam09397
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ...
821-882 2.17e-29

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: 110.92  E-value: 2.17e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586070552 821 DSEDP-YDQAVAVVLRDGKASTSYVQRRLGIGYNRAASLIERMEQEGIIGPANHAGKREILVP 882
Cdd:pfam09397   1 EEEDElYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
Ftsk_gamma smart00843
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ...
821-882 3.14e-29

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: 110.58  E-value: 3.14e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586070552  821 DSEDP-YDQAVAVVLRDGKASTSYVQRRLGIGYNRAASLIERMEQEGIIGPANHAGKREILVP 882
Cdd:smart00843   1 EEEDElYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
513-746 1.49e-20

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: 97.75  E-value: 1.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  513 LAMALGKTIGGEPVIADL---AKMPHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPK---MLELsiYDGIPH 586
Cdd:TIGR03928  446 LAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPH 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  587 LLSpVVTD-----PKKAVVALKwtvREMEERYKKMSKIGVRNIDGFnsrvqQALDKGEILTrtvqtgfdrqtgeaiyete 661
Cdd:TIGR03928  524 LLG-TITNldgaqSMRALASIK---AELKKRQRLFGENNVNHINQY-----QKLYKQGKAK------------------- 575
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  662 efdlKPLPYIVVIIDEMADL------MMvagKDIEGAvqrlAQMARAAGIHVIMATQRPSvDVITGTIKANFPTRISFQV 735
Cdd:TIGR03928  576 ----EPMPHLFLISDEFAELkseqpeFM---KELVST----ARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKV 643
                          250
                   ....*....|.
gi 1586070552  736 TSKIDSRTILG 746
Cdd:TIGR03928  644 QDASDSNEILK 654
FtsK_4TM pfam13491
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ...
22-184 7.68e-19

4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.


Pssm-ID: 463896  Cd Length: 171  Bit Score: 84.56  E-value: 7.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  22 FVRQIMALAGFALLATIALgiaALATWNVADPSLSY--ATGNQPTNLLGYGGAIFADIVMQFLGLSAIisLLPV--IAWA 97
Cdd:pfam13491   3 LLRELLGLALLLLGLFLLL---ALVSYSPADPSWSTsgSGAAPVHNWGGRFGAWLADLLLQLFGYSAW--LLPValLYWG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  98 IALIAGRKLQRIPARLVAWIAGAIVCAASLGCFPAPVTWPLPNGIGGVIGDMILRFPALFIGAypTGTVATILGVIFAAp 177
Cdd:pfam13491  78 WRLFRRRSLERRWLRLLGFLLLLLASSALFALRLPSLEFGLPGGAGGVIGRLLANALVTLLGF--TGATLLLLALLAIG- 154

                  ....*..
gi 1586070552 178 atwLMLF 184
Cdd:pfam13491 155 ---LSLV 158
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
524-746 6.34e-14

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: 76.18  E-value: 6.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  524 EPVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPKMLELSIYDGIPHlLSPVVT--DPKKAVVA 601
Cdd:TIGR03928  801 EPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKL 879
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  602 LKWTVREMEERYKKMSKIGVRNIDGFNsrvqqaldkgeiltrtvqtgfdRQTGEaiyeteefdlkPLPYIVVIIDEMaDL 681
Cdd:TIGR03928  880 IRRIKKEIDRRKKLFSEYGVASISMYN----------------------KASGE-----------KLPQIVIIIDNY-DA 925
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586070552  682 MMVAG--KDIEGAVQRLAQMARAAGIHVIM-ATQRPSVDVitgTIKANFPTRISFQVTSKIDSRTILG 746
Cdd:TIGR03928  926 VKEEPfyEDFEELLIQLAREGASLGIYLVMtAGRQNAVRM---PLMNNIKTKIALYLIDKSEYRSIVG 990
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
457-777 1.88e-12

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: 71.16  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 457 IGLADDIARSMS---AIAARVAVVPGRNAIGielpnqtretvfLRELIGSRDFEN-----------SKAKLAMALGKTIG 522
Cdd:TIGR03924 351 IAEAEALARRLArwrAATAGTVDAPLTGARD------------LLELLGIGDPATldvdrlwrprpGRDRLRVPIGVGDD 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 523 GEPVIADLAK-----M-PHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPK----MLELsiyDGIPHlLSPVV 592
Cdd:TIGR03924 419 GEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---EGLPH-VSAVI 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 593 TD--PKKAVVA-LKWTVR-EMEERYKKMSKIG-VRNIDGFNSRvqqaldkgeiltrtvqtgfdRQTGEaiyeteefDLKP 667
Cdd:TIGR03924 495 TNlaDEAPLVDrMQDALAgEMNRRQELLRAAGnFANVAEYEKA--------------------RAAGA--------DLPP 546
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 668 LPYIVVIIDEMADLMMVAGKDIEGAVQrLAQMARAAGIHVIMATQRPSVDVITGtIKANFPTRISFQVTSKIDSRTILGE 747
Cdd:TIGR03924 547 LPALFVVVDEFSELLSQHPDFADLFVA-IGRLGRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGV 624
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1586070552 748 QGAEQL---LGMGdmlYM-AGGGRIQRVHGPFVS 777
Cdd:TIGR03924 625 PDAYHLpstPGAG---YLkVDTAEPVRFRAAYVS 655
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
435-612 6.41e-08

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: 56.15  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 435 RPGPVVTLYELEPApgIKSSRVIGLADDIARSMSAIAARVAVV-PGRNAIGIE-LPnqtrETVFLRELIGSRDFENskak 512
Cdd:TIGR03925 272 RPGRGLTPDGLHML--IALPRLDGIASVDDLGTRGLVAVIRDVwGGPPAPPVRlLP----ARLPLSALPAGGGAPR---- 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 513 LAMALGktIGG---EPVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMSPEQCRLIMIDPKmleLSIYDGIP--HL 587
Cdd:TIGR03925 342 LRVPLG--LGEsdlAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR---RTLLGAVPedYL 416
                         170       180
                  ....*....|....*....|....*
gi 1586070552 588 LSPVVTdPKKAVVALKWTVREMEER 612
Cdd:TIGR03925 417 AGYAAT-SAALTELIAALAALLERR 440
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
517-768 1.65e-07

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


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 54.95  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 517 LGKTIGGEPVIADLAKM---PHLLVAGTTGSGKSVAINTMILSLLYRmspeQCRLIMIDP--------KMLE---LSIYD 582
Cdd:COG3451   185 LLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDPggsyeilvRALGgtyIDLSP 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 583 GIPHLLSP--VVTDPKKAVVALKWtVREM----------EER----------YKKMSKIGVRNIDGFNSRVQQALDKGEI 640
Cdd:COG3451   261 GSPTGLNPfdLEDTEEKRDFLLEL-LELLlgregepltpEERaaidravralYRRADPEERTTLSDLYELLKEQPEAKDL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 641 LTRT---VQTG-----FDRQTGEAI-------YETEEF----DLKP--LPYI-----------------VVIIDEMADLM 682
Cdd:COG3451   340 AARLepyTKGGsygwlFDGPTNLDLsdarfvvFDLTELldnpELRPpvLLYLlhriwnrlrknndgrptLIVIDEAWLLL 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 683 mvagkDIEGAVQRLAQMARAA---GIHVIMATQRPSvDV----ITGTIKANFPTRIsFQVTSKIDSRTI-----LGEQGA 750
Cdd:COG3451   420 -----DNPAFAEFLEEWLKTLrkyNGAVIFATQSVE-DFlsspIAEAIIENSATKI-LLPQPKADIEDYaellgLSEREL 492
                         330       340
                  ....*....|....*....|..
gi 1586070552 751 EQLL----GMGDMLYMAGGGRI 768
Cdd:COG3451   493 ELIRsagrGKRDFLIKQGNGSV 514
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
514-760 5.89e-07

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: 52.69  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 514 AMALGKTIG-GEPVIADLAKM--PHLLVAGTTGSGKSVAintmILSLLYRMSPEQCRLIMIDPK------------MLEL 578
Cdd:COG0433    25 GILIGKLLSpGVPVYLDLDKLlnRHILILGATGSGKSNT----LQVLLEELSRAGVPVLVFDPHgeysglaepgaeRADV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 579 SIYDGIPHLLSPVV---------------------TDPKKAVVA------------------LKWTVREMEERYKKMSKI 619
Cdd:COG0433   101 GVFDPGAGRPLPINpwdlfataselgplllsrldlNDTQRGVLRealrladdkglllldlkdLIALLEEGEELGEEYGNV 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 620 GVRNIDGFNSRVQQALDKGEI-------LTRTVQT----------GFDRQTG------------EAIYETEEFDLKPLPy 670
Cdd:COG0433   181 SAASAGALLRRLESLESADGLfgepgldLEDLLRTdgrvtvidlsGLPEELQstfvlwllrelfEARPEVGDADDRKLP- 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 671 IVVIIDEmADLmmVAGKDIEGAVQRLAQMA---RAAGIHVIMATQRPSvDVITgTIKANFPTRISFQVTSKIDSRTI--- 744
Cdd:COG0433   260 LVLVIDE-AHL--LAPAAPSALLEILERIAregRKFGVGLILATQRPS-DIDE-DVLSQLGTQIILRLFNPRDQKAVkaa 334
                         330       340
                  ....*....|....*....|.
gi 1586070552 745 ---LGEQGAEQL--LGMGDML 760
Cdd:COG0433   335 aetLSEDLLERLpsLGTGEAL 355
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
535-735 1.06e-05

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: 46.06  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 535 HLLVAGTTGSGKSVAINTMILSLLyrmsPEQCRLIMIDPKM---LELSIYDGIPHLLSPVVTdpkkavvalkwtvremee 611
Cdd:cd01127     1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKGelfLVIPDRDDSFAALRALFF------------------ 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552 612 rykkmskigvrnidgfnsrvqqaldkgEILTRTVQTGFDRQTGeaiyeteefdlKPLPYIVVIIDEMADLMMvagkdIEG 691
Cdd:cd01127    59 ---------------------------NQLFRALTELASLSPG-----------RLPRRVWFILDEFANLGR-----IPN 95
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1586070552 692 AVQRLAQmARAAGIHVIMATQ------RPSVDVITGTIKANFPTRISFQV 735
Cdd:cd01127    96 LPNLLAT-GRKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
MFS_MMR_MDR_like cd17321
Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance ...
21-151 9.17e-03

Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of bacterial, fungal, and archaeal multidrug resistance (MDR) transporters including several proteins from Bacilli such as methylenomycin A resistance protein (also called MMR peptide), tetracycline resistance protein (TetB), and lincomycin resistance protein LmrB, as well as fungal proteins such as vacuolar basic amino acid transporters, which are involved in the transport into vacuoles of the basic amino acids histidine, lysine, and arginine in Saccharomyces cerevisiae, and aminotriazole/azole resistance proteins. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. For example, MMR confers resistance to the epoxide antibiotic methylenomycin while TetB resistance to tetracycline by an active tetracycline efflux. MMR-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340879 [Multi-domain]  Cd Length: 370  Bit Score: 39.46  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  21 FFVRQIMALAGFALLATIALGIAALATWNvadpslsyatgnqptnlLGYGGAIFadIVMQFL----GLSAIISLLPVIAW 96
Cdd:cd17321   153 FLINVPIGLVALLLARTFSGAVLAAFLLG-----------------AALGGLLF--LLPLYLqgvlGYSPLQAGLALLPL 213
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586070552  97 AI-----ALIAGRKLQRIPARLVAwIAGAIVCAASLGCFpapVTWPLPNGIGGVIGDMIL 151
Cdd:cd17321   214 ALamlvaAPLAGRLADRFGPRLVL-VAGLLLTAVGLLLL---ALLGADSSVWLLLPGLVL 269
 
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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