|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
181-811 |
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: 880.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 181 ILLGFFTAAFAGNVIWRRRTKKRKEKSIPKDAIVNPVFELEEDTEYAAEDDRENHGFFATTFGALLHLFYFLQARFFRLF 260
Cdd:COG1674 1 LLLLLLLLALLAGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 261 CFKSRFQSKGQGKSFDRIEPTFLGEKVKCEENQNKAYVSPVKNRKSLTASSNGGFVLPLVDYLSVPPPsvREAKLSPAVL 340
Cdd:COG1674 81 LLLLLLGLLGAALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPP--KKEKIDEEEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 341 RANSQELEGVLLDFGVKGQIIDACPGPVVTLYEFEPAAGIKSSRIIGLADDIARSMRAISARV-AVVPGRNVIGIELPNA 419
Cdd:COG1674 159 EENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIeAPIPGKSAVGIEVPNK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 420 KREMVYLREMLQAQEFIESKAKLGLALGKTIGGEAVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPEQCRLIM 499
Cdd:COG1674 239 KRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLIL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 500 VDPKMLELSVYDGIPHLLTPVVTDPKKAVIALKWAVREMEERYSKMSKLGVRNIDGFNARLKESEGQGEtmvrtiqvgfd 579
Cdd:COG1674 319 IDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGE----------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 580 hetgeplyetETLDFSPMPYIVVIIDEMADLMMVAGKDIEGAVQRLAQMARAAGIHVIMATQRPSVDVITGTIKANFPTR 659
Cdd:COG1674 388 ----------EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 660 ISFSVSSKIDSRTILGEQGAEQLLGQGDMLFM-MGGGRVQRVHGPFVADDEVEQVVAHLKAQARPDYLETITQEVEEDGA 738
Cdd:COG1674 458 IAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLpPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDE 537
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240268408 739 DvslASPSEDDP-YSQAVAIVLRDRKASTSYIQRRLGIGYNRAATLIERMEEEGIISPANHAGKREILVPAEEE 811
Cdd:COG1674 538 G---GDDDEDDElFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
317-807 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 561.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 317 LPLVDYLSvPPPSVREAkLSPAVLRANSQELEGVLLDFGVKGQIIDACPGPVVTLYEFEPAAGIKSSRIIGLADDIARSM 396
Cdd:PRK10263 866 LPSLDLLT-PPPSEVEP-VDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 397 RAISARVA-VVPGRNVIGIELPNAKREMVYLREMLQAQEFIESKAKLGLALGKTIGGEAVIADLAKMPHLLVAGTTGSGK 475
Cdd:PRK10263 944 STVAVRVVeVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGK 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 476 SVAINTMILSLLYRMTPEQCRLIMVDPKMLELSVYDGIPHLLTPVVTDPKKAVIALKWAVREMEERYSKMSKLGVRNIDG 555
Cdd:PRK10263 1024 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAG 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 556 FNARLKESegqgETMVRTI-----QVGFDHETGEPLYETEtldfspmPYIVVIIDEMADLMMVAGKDIEGAVQRLAQMAR 630
Cdd:PRK10263 1104 YNEKIAEA----DRMMRPIpdpywKPGDSMDAQHPVLKKE-------PYIVVLVDEFADLMMTVGKKVEELIARLAQKAR 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 631 AAGIHVIMATQRPSVDVITGTIKANFPTRISFSVSSKIDSRTILGEQGAEQLLGQGDMLFMMGGGRVQ-RVHGPFVADDE 709
Cdd:PRK10263 1173 AAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPvRVHGAFVRDQE 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 710 VEQVVAHLKAQARPDYLETITQEVEEDGADVSLASPSEDDP-YSQAVAIVLRDRKASTSYIQRRLGIGYNRAATLIERME 788
Cdd:PRK10263 1253 VHAVVQDWKARGRPQYVDGITSDSESEGGAGGFDGAEELDPlFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQME 1332
|
490
....*....|....*....
gi 240268408 789 EEGIISPANHAGKREILVP 807
Cdd:PRK10263 1333 AQGIVSEQGHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
426-644 |
1.59e-69 |
|
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: 228.42 E-value: 1.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 426 LREMLQAQEFIESKAKLGLALGKTIGGEAVIADLAKMP-HLLVAGTTGSGKSVAINTMILSLLYRMTPEQCRLIMVDPKM 504
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 505 LELSVYDGIPHLLT-PVVTDPKKAVIALKWAVREMEERYSKMSKLGVRNIDGFNARLKESEGQGETMVRTIQVGFDhetg 583
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVH---- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240268408 584 epLYETETLDFSPMPYIVVIIDEMADLMMVAGKD----IEGAVQRLAQMARAAGIHVIMATQRPS 644
Cdd:pfam01580 157 --VMCTAGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
746-807 |
7.13e-30 |
|
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: 112.51 E-value: 7.13e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240268408 746 SEDDPYSQAVAIVLRDRKASTSYIQRRLGIGYNRAATLIERMEEEGIISPANHAGKREILVP 807
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
416-675 |
4.25e-18 |
|
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: 89.66 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 416 LPNAKREMVYLREMLQAQEFIE-------SKAK----LGLALGKTIGGEAVIADL---AKMPHLLVAGTTGSGKSVAINT 481
Cdd:TIGR03928 409 LKNSIPESVTFLEMYGVKKVEElniqerwAKNEtyksLAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQT 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 482 MILSLLYRMTPEQCRLIMVDPK---MLELsvYDGIPHLLTpVVTD-----PKKAVIALKwavREMEERYSKMSKLGVRNI 553
Cdd:TIGR03928 489 YILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLLG-TITNldgaqSMRALASIK---AELKKRQRLFGENNVNHI 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 554 DGFNARLKEsegqgetmvrtiqvgfdhetGEPlyeTEtldfsPMPYIVVIIDEMADL------MMvagKDIEGAvqrlAQ 627
Cdd:TIGR03928 563 NQYQKLYKQ--------------------GKA---KE-----PMPHLFLISDEFAELkseqpeFM---KELVST----AR 607
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 240268408 628 MARAAGIHVIMATQRPSvDVITGTIKANFPTRISFSVSSKIDSRTILG 675
Cdd:TIGR03928 608 IGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILK 654
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
23-180 |
3.10e-16 |
|
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: 77.24 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 23 EMFLRQIgvfIGLGLLGFIIFCVFALATWNVEDPSLTHASTN--EVTNLMGWMGAIFSDFIMQFFGLASLAVLLPPLFWS 100
Cdd:pfam13491 1 ERLLREL---LGLALLLLGLFLLLALVSYSPADPSWSTSGSGaaPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 101 FLLLAQKNIYNLTLRFFLWLLSTICFLIAFALMSPvasFTYWPLPMGLGGVLGDKALSVASSVFP-----LFLSPLYTVF 175
Cdd:pfam13491 78 WRLFRRRSLERRWLRLLGFLLLLLASSALFALRLP---SLEFGLPGGAGGVIGRLLANALVTLLGftgatLLLLALLAIG 154
|
....*
gi 240268408 176 FSVVF 180
Cdd:pfam13491 155 LSLVT 159
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
464-664 |
2.27e-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: 44.90 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 464 HLLVAGTTGSGKSVAINTMILsllyRMTPEQCRLIMVDPKM---LELSVYDGIPHLLTPVVTDpkkaviALKWAVREMEE 540
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLL----DQAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 541 RYskMSKLGVRnidgfnarlkesegqgetmvrtiqvgfdhetgeplyetetldfspmpyIVVIIDEMADLMMvagkdIEG 620
Cdd:cd01127 71 LS--PGRLPRR------------------------------------------------VWFILDEFANLGR-----IPN 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 240268408 621 AVQRLAQmARAAGIHVIMATQ------RPSVDVITGTIKANFPTRISFSV 664
Cdd:cd01127 96 LPNLLAT-GRKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
181-811 |
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: 880.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 181 ILLGFFTAAFAGNVIWRRRTKKRKEKSIPKDAIVNPVFELEEDTEYAAEDDRENHGFFATTFGALLHLFYFLQARFFRLF 260
Cdd:COG1674 1 LLLLLLLLALLAGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 261 CFKSRFQSKGQGKSFDRIEPTFLGEKVKCEENQNKAYVSPVKNRKSLTASSNGGFVLPLVDYLSVPPPsvREAKLSPAVL 340
Cdd:COG1674 81 LLLLLLGLLGAALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPP--KKEKIDEEEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 341 RANSQELEGVLLDFGVKGQIIDACPGPVVTLYEFEPAAGIKSSRIIGLADDIARSMRAISARV-AVVPGRNVIGIELPNA 419
Cdd:COG1674 159 EENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIeAPIPGKSAVGIEVPNK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 420 KREMVYLREMLQAQEFIESKAKLGLALGKTIGGEAVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPEQCRLIM 499
Cdd:COG1674 239 KRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLIL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 500 VDPKMLELSVYDGIPHLLTPVVTDPKKAVIALKWAVREMEERYSKMSKLGVRNIDGFNARLKESEGQGEtmvrtiqvgfd 579
Cdd:COG1674 319 IDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGE----------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 580 hetgeplyetETLDFSPMPYIVVIIDEMADLMMVAGKDIEGAVQRLAQMARAAGIHVIMATQRPSVDVITGTIKANFPTR 659
Cdd:COG1674 388 ----------EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 660 ISFSVSSKIDSRTILGEQGAEQLLGQGDMLFM-MGGGRVQRVHGPFVADDEVEQVVAHLKAQARPDYLETITQEVEEDGA 738
Cdd:COG1674 458 IAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLpPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDE 537
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240268408 739 DvslASPSEDDP-YSQAVAIVLRDRKASTSYIQRRLGIGYNRAATLIERMEEEGIISPANHAGKREILVPAEEE 811
Cdd:COG1674 538 G---GDDDEDDElFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
317-807 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 561.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 317 LPLVDYLSvPPPSVREAkLSPAVLRANSQELEGVLLDFGVKGQIIDACPGPVVTLYEFEPAAGIKSSRIIGLADDIARSM 396
Cdd:PRK10263 866 LPSLDLLT-PPPSEVEP-VDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 397 RAISARVA-VVPGRNVIGIELPNAKREMVYLREMLQAQEFIESKAKLGLALGKTIGGEAVIADLAKMPHLLVAGTTGSGK 475
Cdd:PRK10263 944 STVAVRVVeVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGK 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 476 SVAINTMILSLLYRMTPEQCRLIMVDPKMLELSVYDGIPHLLTPVVTDPKKAVIALKWAVREMEERYSKMSKLGVRNIDG 555
Cdd:PRK10263 1024 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAG 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 556 FNARLKESegqgETMVRTI-----QVGFDHETGEPLYETEtldfspmPYIVVIIDEMADLMMVAGKDIEGAVQRLAQMAR 630
Cdd:PRK10263 1104 YNEKIAEA----DRMMRPIpdpywKPGDSMDAQHPVLKKE-------PYIVVLVDEFADLMMTVGKKVEELIARLAQKAR 1172
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 631 AAGIHVIMATQRPSVDVITGTIKANFPTRISFSVSSKIDSRTILGEQGAEQLLGQGDMLFMMGGGRVQ-RVHGPFVADDE 709
Cdd:PRK10263 1173 AAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPvRVHGAFVRDQE 1252
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 710 VEQVVAHLKAQARPDYLETITQEVEEDGADVSLASPSEDDP-YSQAVAIVLRDRKASTSYIQRRLGIGYNRAATLIERME 788
Cdd:PRK10263 1253 VHAVVQDWKARGRPQYVDGITSDSESEGGAGGFDGAEELDPlFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQME 1332
|
490
....*....|....*....
gi 240268408 789 EEGIISPANHAGKREILVP 807
Cdd:PRK10263 1333 AQGIVSEQGHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
426-644 |
1.59e-69 |
|
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: 228.42 E-value: 1.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 426 LREMLQAQEFIESKAKLGLALGKTIGGEAVIADLAKMP-HLLVAGTTGSGKSVAINTMILSLLYRMTPEQCRLIMVDPKM 504
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 505 LELSVYDGIPHLLT-PVVTDPKKAVIALKWAVREMEERYSKMSKLGVRNIDGFNARLKESEGQGETMVRTIQVGFDhetg 583
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVH---- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240268408 584 epLYETETLDFSPMPYIVVIIDEMADLMMVAGKD----IEGAVQRLAQMARAAGIHVIMATQRPS 644
Cdd:pfam01580 157 --VMCTAGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
317-418 |
8.95e-36 |
|
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: 130.35 E-value: 8.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 317 LPLVDYLSVPPPSvrEAKLSPAVLRANSQELEGVLLDFGVKGQIIDACPGPVVTLYEFEPAAGIKSSRIIGLADDIARSM 396
Cdd:pfam17854 1 LPPLDLLEPPPTS--SQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALAL 78
|
90 100
....*....|....*....|...
gi 240268408 397 RAISARV-AVVPGRNVIGIELPN 418
Cdd:pfam17854 79 SAPSIRIvAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
746-807 |
5.94e-30 |
|
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: 112.46 E-value: 5.94e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240268408 746 SEDDP-YSQAVAIVLRDRKASTSYIQRRLGIGYNRAATLIERMEEEGIISPANHAGKREILVP 807
Cdd:pfam09397 1 EEEDElYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
746-807 |
7.13e-30 |
|
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: 112.51 E-value: 7.13e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240268408 746 SEDDPYSQAVAIVLRDRKASTSYIQRRLGIGYNRAATLIERMEEEGIISPANHAGKREILVP 807
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
416-675 |
4.25e-18 |
|
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: 89.66 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 416 LPNAKREMVYLREMLQAQEFIE-------SKAK----LGLALGKTIGGEAVIADL---AKMPHLLVAGTTGSGKSVAINT 481
Cdd:TIGR03928 409 LKNSIPESVTFLEMYGVKKVEElniqerwAKNEtyksLAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQT 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 482 MILSLLYRMTPEQCRLIMVDPK---MLELsvYDGIPHLLTpVVTD-----PKKAVIALKwavREMEERYSKMSKLGVRNI 553
Cdd:TIGR03928 489 YILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLLG-TITNldgaqSMRALASIK---AELKKRQRLFGENNVNHI 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 554 DGFNARLKEsegqgetmvrtiqvgfdhetGEPlyeTEtldfsPMPYIVVIIDEMADL------MMvagKDIEGAvqrlAQ 627
Cdd:TIGR03928 563 NQYQKLYKQ--------------------GKA---KE-----PMPHLFLISDEFAELkseqpeFM---KELVST----AR 607
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 240268408 628 MARAAGIHVIMATQRPSvDVITGTIKANFPTRISFSVSSKIDSRTILG 675
Cdd:TIGR03928 608 IGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILK 654
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
23-180 |
3.10e-16 |
|
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: 77.24 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 23 EMFLRQIgvfIGLGLLGFIIFCVFALATWNVEDPSLTHASTN--EVTNLMGWMGAIFSDFIMQFFGLASLAVLLPPLFWS 100
Cdd:pfam13491 1 ERLLREL---LGLALLLLGLFLLLALVSYSPADPSWSTSGSGaaPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 101 FLLLAQKNIYNLTLRFFLWLLSTICFLIAFALMSPvasFTYWPLPMGLGGVLGDKALSVASSVFP-----LFLSPLYTVF 175
Cdd:pfam13491 78 WRLFRRRSLERRWLRLLGFLLLLLASSALFALRLP---SLEFGLPGGAGGVIGRLLANALVTLLGftgatLLLLALLAIG 154
|
....*
gi 240268408 176 FSVVF 180
Cdd:pfam13491 155 LSLVT 159
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
458-675 |
1.19e-11 |
|
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: 68.86 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 458 DLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPEQCRLIMVDPKMLELSVYDGIPHLLTPVVTDP----KKAVIALKw 533
Cdd:TIGR03928 806 DLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEeekiEKLIRRIK- 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 534 avREMEERYSKMSKLGVRNIDGFNARLKEsegqgetmvrtiqvgfdhetgeplyetetldfsPMPYIVVIIDEMaDLMMV 613
Cdd:TIGR03928 885 --KEIDRRKKLFSEYGVASISMYNKASGE---------------------------------KLPQIVIIIDNY-DAVKE 928
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240268408 614 AG--KDIEGAVQRLAQMARAAGIHVIM-ATQRPSVDVitgTIKANFPTRISFSVSSKIDSRTILG 675
Cdd:TIGR03928 929 EPfyEDFEELLIQLAREGASLGIYLVMtAGRQNAVRM---PLMNNIKTKIALYLIDKSEYRSIVG 990
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
463-682 |
2.79e-10 |
|
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: 63.84 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 463 PHLLVAGTTGSGKSVAINTMILSLLYRMTPEQCRLIMVDPK----MLELsvyDGIPHlLTPVVT---DPKKAVIALKWAV 535
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---EGLPH-VSAVITnlaDEAPLVDRMQDAL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 536 R-EMEERYSKMSKLG-VRNIDGFN-ARlkesegqgetmvrtiqvgfdhETGEPLyetetldfSPMPYIVVIIDE------ 606
Cdd:TIGR03924 512 AgEMNRRQELLRAAGnFANVAEYEkAR---------------------AAGADL--------PPLPALFVVVDEfsells 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 607 ----MADLMMvagkdiegAVQRLaqmARAAGIHVIMATQRPSVDVITGtIKANFPTRISFSVSSKIDSRTILGEQGAEQL 682
Cdd:TIGR03924 563 qhpdFADLFV--------AIGRL---GRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHL 630
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
384-503 |
3.92e-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: 56.92 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 384 RIIGLADDIARSMRAISARVAVV-PGRNVIGIE-LPnakrEMVYLREMLQAQEFieskAKLGLALGktIGG---EAVIAD 458
Cdd:TIGR03925 290 RLDGIASVDDLGTRGLVAVIRDVwGGPPAPPVRlLP----ARLPLSALPAGGGA----PRLRVPLG--LGEsdlAPVYVD 359
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 240268408 459 LAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPEQCRLIMVDPK 503
Cdd:TIGR03925 360 FAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR 404
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
443-502 |
2.95e-06 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 50.72 E-value: 2.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240268408 443 GLALGKTIGGEAVIADLAKM---PHLLVAGTTGSGKSVAINTMILSLLYRmtpeQCRLIMVDP 502
Cdd:COG3451 182 GIYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
464-664 |
2.27e-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: 44.90 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 464 HLLVAGTTGSGKSVAINTMILsllyRMTPEQCRLIMVDPKM---LELSVYDGIPHLLTPVVTDpkkaviALKWAVREMEE 540
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLL----DQAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 541 RYskMSKLGVRnidgfnarlkesegqgetmvrtiqvgfdhetgeplyetetldfspmpyIVVIIDEMADLMMvagkdIEG 620
Cdd:cd01127 71 LS--PGRLPRR------------------------------------------------VWFILDEFANLGR-----IPN 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 240268408 621 AVQRLAQmARAAGIHVIMATQ------RPSVDVITGTIKANFPTRISFSV 664
Cdd:cd01127 96 LPNLLAT-GRKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
443-694 |
6.26e-05 |
|
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: 46.14 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 443 GLALGKTIGGEA-VIADLAKM--PHLLVAGTTGSGKSVAINTMILSL----------------------------LYRMT 491
Cdd:COG0433 25 GILIGKLLSPGVpVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELsragvpvlvfdphgeysglaepgaeradVGVFD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 492 PEQCRLIMVDPKMLELSVYDGIPHLLTPVV-TDPKKAVI--ALKWA----------------VREMEERYSKMSKLGVRN 552
Cdd:COG0433 105 PGAGRPLPINPWDLFATASELGPLLLSRLDlNDTQRGVLreALRLAddkglllldlkdlialLEEGEELGEEYGNVSAAS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 553 IDGFNARLKESE-------GQGETMVRTIQV----------GFDHETG------------EPLYETETLDFSPMPyIVVI 603
Cdd:COG0433 185 AGALLRRLESLEsadglfgEPGLDLEDLLRTdgrvtvidlsGLPEELQstfvlwllrelfEARPEVGDADDRKLP-LVLV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240268408 604 IDEmADLmmVAGKDIEGAVQRLAQMA---RAAGIHVIMATQRPSvDVITgTIKANFPTRISFSVSSKIDSRTI------L 674
Cdd:COG0433 264 IDE-AHL--LAPAAPSALLEILERIAregRKFGVGLILATQRPS-DIDE-DVLSQLGTQIILRLFNPRDQKAVkaaaetL 338
|
330 340
....*....|....*....|..
gi 240268408 675 GEQGAEQL--LGQGDMLFMMGG 694
Cdd:COG0433 339 SEDLLERLpsLGTGEALVLGEG 360
|
|
| |
