|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
299-786 |
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: 750.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 299 EFEKDETDVQIDFKPKQRLAYKLPSIDLFAPIKAKSQSNEKRIVRQNIKVLEDTFASFGIKVVVERAEIGPSVTKYEVKP 378
Cdd:COG1674 115 AAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 379 AVGVRVNRISNLADDLALALAAKDVRIEAPIPGKSLVGIEVPNSEVATVPFRELWEQSKTDPDKL-LEIPLGKAVNGSVR 457
Cdd:COG1674 195 APGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSpLPIALGKDISGEPV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 458 SFNLARMPHLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKMVELSVYNDIPHLLIPVVTNPRKAARALQKVV 537
Cdd:COG1674 275 VADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 538 DEMEKRYELFSQIGVRNLEGYNAKVEEFNSRSEEKQI--PLPLIVVIVDELADLMMVASKEVEDAIIRLGQKARAAGIHM 615
Cdd:COG1674 355 REMERRYKLFAKAGVRNIAGYNEKVREAKAKGEEEEGlePLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 616 ILATQRPSVDVISGLIKANVPSRIAFAVSSGTDSRTILDENGAEKLLGRGDMLFKPIDENHPVRLQGSFISDDDVEAIVG 695
Cdd:COG1674 435 ILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVD 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 696 FIKDQADADYDESFDPGEVAEgdgDAGFGDAGGDPLFNEARALVVETQKASASMIQRRLSVGFNRATRLMEELEAAGVIG 775
Cdd:COG1674 515 FLKSQGEPEYIEEILEEEEEE---DEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVG 591
|
490
....*....|.
gi 459386991 776 PAEGTKPRKVL 786
Cdd:COG1674 592 PAEGSKPREVL 602
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
310-786 |
1.04e-143 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 456.47 E-value: 1.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 310 DFKPKQRLAYKLPSIDLFAPIKAKSQSNEKRIVRQNIKVLEDTFASFGIKVVVERAEIGPSVTKYEVKPAVGVRVNRISN 389
Cdd:PRK10263 855 DSRPLHKPTTPLPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISN 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 390 LADDLALALAAKDVRIEAPIPGKSLVGIEVPNSEVATVPFRELWEQSK-TDPDKLLEIPLGKAVNGSVRSFNLARMPHLL 468
Cdd:PRK10263 935 LSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKfRDNPSPLTVVLGKDIAGEPVVADLAKMPHLL 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 469 VAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKMVELSVYNDIPHLLIPVVTNPRKAARALQKVVDEMEKRYELFS 548
Cdd:PRK10263 1015 VAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMS 1094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 549 QIGVRNLEGYNAKVEEFN-------------SRSEEKQIP----LPLIVVIVDELADLMMVASKEVEDAIIRLGQKARAA 611
Cdd:PRK10263 1095 ALGVRNLAGYNEKIAEADrmmrpipdpywkpGDSMDAQHPvlkkEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAA 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 612 GIHMILATQRPSVDVISGLIKANVPSRIAFAVSSGTDSRTILDENGAEKLLGRGDMLFKPIDENHPVRLQGSFISDDDVE 691
Cdd:PRK10263 1175 GIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVH 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 692 AIVGFIKDQADADYDESFDPGEVAEGDGDAGFGDAGGDPLFNEARALVVETQKASASMIQRRLSVGFNRATRLMEELEAA 771
Cdd:PRK10263 1255 AVVQDWKARGRPQYVDGITSDSESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQ 1334
|
490
....*....|....*
gi 459386991 772 GVIGPAEGTKPRKVL 786
Cdd:PRK10263 1335 GIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
430-623 |
4.97e-64 |
|
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: 213.39 E-value: 4.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 430 RELWEQSKTDPDK-LLEIPLGKAVNGSVRSFNLARMP-HLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKMV 507
Cdd:pfam01580 2 LEVLESKPFDTDYsRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 508 ELSVYNDIPHLL-IPVVTNPRKAARALQKVVDEMEKRYELFSQIGVRNLEGYNAKVEEFNSRSEEKQIP----------- 575
Cdd:pfam01580 82 ELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLviygvhvmcta 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 459386991 576 ------LPLIVVIVDELADLMMVASKE----VEDAIIRLGQKARAAGIHMILATQRPS 623
Cdd:pfam01580 162 grwleiLPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
436-653 |
9.67e-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: 117.40 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 436 SKTDPDKLLEIPLGKAVNGSVRSFNL---ARMPHLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPK---MVEL 509
Cdd:TIGR03928 438 AKNETYKSLAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 510 svYNDIPHLLiPVVTN--PRKAARALQKVVDEMEKRYELFSQIGVRNLEGY-----NAKVEEfnsrseekqiPLPLIVVI 582
Cdd:TIGR03928 518 --FKNLPHLL-GTITNldGAQSMRALASIKAELKKRQRLFGENNVNHINQYqklykQGKAKE----------PMPHLFLI 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 459386991 583 VDELADLmmvaSKEVEDAIIRLGQKA---RAAGIHMILATQRPSvDVISGLIKANVPSRIAFAVSSGTDSRTIL 653
Cdd:TIGR03928 585 SDEFAEL----KSEQPEFMKELVSTArigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
730-786 |
1.90e-26 |
|
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: 102.49 E-value: 1.90e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 459386991 730 PLFNEARALVVETQKASASMIQRRLSVGFNRATRLMEELEAAGVIGPAEGTKPRKVL 786
Cdd:smart00843 5 ELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVL 61
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
466-643 |
2.62e-06 |
|
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: 47.60 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 466 HLLVAGSTGSGKSVAVNGIISSILMKAGpdqvKFMMIDPKMvelSVYndiphLLIPVVTNPRKAARALqkvvdemekrye 545
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKG---ELF-----LVIPDRDDSFAALRAL------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 546 LFSQIGVRNLEGYNAKVEEFNSRseekqiplplIVVIVDELAdlMMVASKEVEDAIirlgQKARAAGIHMILATQ----- 620
Cdd:cd01127 57 FFNQLFRALTELASLSPGRLPRR----------VWFILDEFA--NLGRIPNLPNLL----ATGRKRGISVVLILQslaql 120
|
170 180
....*....|....*....|....
gi 459386991 621 -RPSVDVISGLIKANVPSRIAFAV 643
Cdd:cd01127 121 eAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
46-185 |
1.70e-04 |
|
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: 42.96 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 46 GVFGvtSY--NIFRLLFGSLAYLLLVGAFI---YLLIPKVLREREGTISGFWLIVIGLLIefqayldwtyqgsdLFGHTL 120
Cdd:pfam13491 48 GRFG--AWlaDLLLQLFGYSAWLLPVALLYwgwRLFRRRSLERRWLRLLGFLLLLLASSA--------------LFALRL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 459386991 121 kLALSDLAKFQvtaflGGGMIGSIFYLPVSFLFANVGSFFIGLLVIAFGIFFVSPWSVYDVADGL 185
Cdd:pfam13491 112 -PSLEFGLPGG-----AGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAERL 170
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
299-786 |
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: 750.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 299 EFEKDETDVQIDFKPKQRLAYKLPSIDLFAPIKAKSQSNEKRIVRQNIKVLEDTFASFGIKVVVERAEIGPSVTKYEVKP 378
Cdd:COG1674 115 AAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 379 AVGVRVNRISNLADDLALALAAKDVRIEAPIPGKSLVGIEVPNSEVATVPFRELWEQSKTDPDKL-LEIPLGKAVNGSVR 457
Cdd:COG1674 195 APGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSpLPIALGKDISGEPV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 458 SFNLARMPHLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKMVELSVYNDIPHLLIPVVTNPRKAARALQKVV 537
Cdd:COG1674 275 VADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 538 DEMEKRYELFSQIGVRNLEGYNAKVEEFNSRSEEKQI--PLPLIVVIVDELADLMMVASKEVEDAIIRLGQKARAAGIHM 615
Cdd:COG1674 355 REMERRYKLFAKAGVRNIAGYNEKVREAKAKGEEEEGlePLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 616 ILATQRPSVDVISGLIKANVPSRIAFAVSSGTDSRTILDENGAEKLLGRGDMLFKPIDENHPVRLQGSFISDDDVEAIVG 695
Cdd:COG1674 435 ILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVD 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 696 FIKDQADADYDESFDPGEVAEgdgDAGFGDAGGDPLFNEARALVVETQKASASMIQRRLSVGFNRATRLMEELEAAGVIG 775
Cdd:COG1674 515 FLKSQGEPEYIEEILEEEEEE---DEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVG 591
|
490
....*....|.
gi 459386991 776 PAEGTKPRKVL 786
Cdd:COG1674 592 PAEGSKPREVL 602
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
310-786 |
1.04e-143 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 456.47 E-value: 1.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 310 DFKPKQRLAYKLPSIDLFAPIKAKSQSNEKRIVRQNIKVLEDTFASFGIKVVVERAEIGPSVTKYEVKPAVGVRVNRISN 389
Cdd:PRK10263 855 DSRPLHKPTTPLPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISN 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 390 LADDLALALAAKDVRIEAPIPGKSLVGIEVPNSEVATVPFRELWEQSK-TDPDKLLEIPLGKAVNGSVRSFNLARMPHLL 468
Cdd:PRK10263 935 LSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKfRDNPSPLTVVLGKDIAGEPVVADLAKMPHLL 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 469 VAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKMVELSVYNDIPHLLIPVVTNPRKAARALQKVVDEMEKRYELFS 548
Cdd:PRK10263 1015 VAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMS 1094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 549 QIGVRNLEGYNAKVEEFN-------------SRSEEKQIP----LPLIVVIVDELADLMMVASKEVEDAIIRLGQKARAA 611
Cdd:PRK10263 1095 ALGVRNLAGYNEKIAEADrmmrpipdpywkpGDSMDAQHPvlkkEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAA 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 612 GIHMILATQRPSVDVISGLIKANVPSRIAFAVSSGTDSRTILDENGAEKLLGRGDMLFKPIDENHPVRLQGSFISDDDVE 691
Cdd:PRK10263 1175 GIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVH 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 692 AIVGFIKDQADADYDESFDPGEVAEGDGDAGFGDAGGDPLFNEARALVVETQKASASMIQRRLSVGFNRATRLMEELEAA 771
Cdd:PRK10263 1255 AVVQDWKARGRPQYVDGITSDSESEGGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQ 1334
|
490
....*....|....*
gi 459386991 772 GVIGPAEGTKPRKVL 786
Cdd:PRK10263 1335 GIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
430-623 |
4.97e-64 |
|
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: 213.39 E-value: 4.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 430 RELWEQSKTDPDK-LLEIPLGKAVNGSVRSFNLARMP-HLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKMV 507
Cdd:pfam01580 2 LEVLESKPFDTDYsRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 508 ELSVYNDIPHLL-IPVVTNPRKAARALQKVVDEMEKRYELFSQIGVRNLEGYNAKVEEFNSRSEEKQIP----------- 575
Cdd:pfam01580 82 ELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLviygvhvmcta 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 459386991 576 ------LPLIVVIVDELADLMMVASKE----VEDAIIRLGQKARAAGIHMILATQRPS 623
Cdd:pfam01580 162 grwleiLPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
321-421 |
3.03e-29 |
|
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: 111.86 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 321 LPSIDLFAPIKAKSQSNEKRIVRQNIKVLEDTFASFGIKVVVERAEIGPSVTKYEVKPAVGVRVNRISNLADDLALALAA 400
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 459386991 401 KDVRIEAPIPGKSLVGIEVPN 421
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
730-786 |
1.65e-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: 108.23 E-value: 1.65e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 459386991 730 PLFNEARALVVETQKASASMIQRRLSVGFNRATRLMEELEAAGVIGPAEGTKPRKVL 786
Cdd:pfam09397 5 ELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVL 61
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
436-653 |
9.67e-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: 117.40 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 436 SKTDPDKLLEIPLGKAVNGSVRSFNL---ARMPHLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPK---MVEL 509
Cdd:TIGR03928 438 AKNETYKSLAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 510 svYNDIPHLLiPVVTN--PRKAARALQKVVDEMEKRYELFSQIGVRNLEGY-----NAKVEEfnsrseekqiPLPLIVVI 582
Cdd:TIGR03928 518 --FKNLPHLL-GTITNldGAQSMRALASIKAELKKRQRLFGENNVNHINQYqklykQGKAKE----------PMPHLFLI 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 459386991 583 VDELADLmmvaSKEVEDAIIRLGQKA---RAAGIHMILATQRPSvDVISGLIKANVPSRIAFAVSSGTDSRTIL 653
Cdd:TIGR03928 585 SDEFAEL----KSEQPEFMKELVSTArigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
730-786 |
1.90e-26 |
|
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: 102.49 E-value: 1.90e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 459386991 730 PLFNEARALVVETQKASASMIQRRLSVGFNRATRLMEELEAAGVIGPAEGTKPRKVL 786
Cdd:smart00843 5 ELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVL 61
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
413-688 |
1.77e-18 |
|
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: 90.03 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 413 SLVGIevpnSEVATVPFRELWeQSKTDPDkLLEIPLGKAVNGSVRSFNL---AR--M-PHLLVAGSTGSGKSVAVNGIIS 486
Cdd:TIGR03924 384 ELLGI----GDPATLDVDRLW-RPRPGRD-RLRVPIGVGDDGEPVELDLkesAEggMgPHGLCIGATGSGKSELLRTLVL 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 487 SILMKAGPDQVKFMMIDPK-------MVELsvyndiPHLlIPVVTNPRKAARALQKVVD----EMEKRYELFSQIGvrNL 555
Cdd:TIGR03924 458 GLAATHSPEQLNLVLVDFKggatflgLEGL------PHV-SAVITNLADEAPLVDRMQDalagEMNRRQELLRAAG--NF 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 556 egynAKVEEFNSRSEEKQI--PLPLIVVIVDELADLMmvASK----EVEDAIIRLGqkaRAAGIHMILATQRPSVDVISG 629
Cdd:TIGR03924 529 ----ANVAEYEKARAAGADlpPLPALFVVVDEFSELL--SQHpdfaDLFVAIGRLG---RSLGVHLLLASQRLDEGRLRG 599
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 459386991 630 LiKANVPSRIAFAVSSGTDSRTILDENGAEKLLGRGDMLFKPIDENHPVRLQGSFISDD 688
Cdd:TIGR03924 600 L-ESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
418-665 |
7.15e-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: 85.42 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 418 EVPNSEVATVPFRELWeqskTDPDKLLEIPLGKAVNGSVRS-----FNLARMPHLLVAGSTGSGKSVAVNGIISSILMKA 492
Cdd:TIGR03928 763 KIYLDDLHAVEFDKLW----SKPKEPLQATIGLLDDPELQSqepltLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQH 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 493 GPDQVKFMMIDPKMVELSVYNDIPHLL-IPVVTNPRKAARALQKVVDEMEKRYELFSQIGVRNLEGYNAKVEEfnsrsee 571
Cdd:TIGR03928 839 SPEQLHFYLFDFGTNGLLPLKKLPHVAdYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASGE------- 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 572 kqiPLPLIVVIVDELADLMMVASKEV-EDAIIRLGQKARAAGIHMIL-ATQRPSVDVIsglIKANVPSRIAFAVSSGTDS 649
Cdd:TIGR03928 912 ---KLPQIVIIIDNYDAVKEEPFYEDfEELLIQLAREGASLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEY 985
|
250
....*....|....*...
gi 459386991 650 RTILDEN--GAEKLLGRG 665
Cdd:TIGR03928 986 RSIVGRTkfTIEEIPGRG 1003
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
466-665 |
6.48e-09 |
|
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: 59.24 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 466 HLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKMVELSVYNDIPHlLIPVVT--NPRKAARALQKVVDEMEKR 543
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGrlDPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 544 YELFSQIGVRNLEGYNAKVEEFNSRSEekqiPLPLIVVIVDELADLMMvASKEVEDAIIRLGQKARAAGIHMILATQRPS 623
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRARRAAGRLPED----PFGDVFLVIDGWGTLRQ-DFEDLEDKVTDLAARGLAYGVHVVLTASRWS 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 459386991 624 vdVISGLIKANVPSRIAFAVSSGTDSrtILDENGAEKLL----GRG 665
Cdd:TIGR03925 235 --EIRPALRDLIGTRIELRLGDPMDS--EIDRRAAARVPagrpGRG 276
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
444-618 |
5.87e-07 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 53.07 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 444 LEIPLGKA-VNGSVRSFNLARMPHLLVAGSTGSGKSVAVNGIISSILMKAGPDQVKFMMIDPKmveLSVYNDIP--HLLi 520
Cdd:TIGR03925 342 LRVPLGLGeSDLAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR---RTLLGAVPedYLA- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 521 PVVTNPRKAARALQKVVDEMEKRyelfsqigvrnLEGYNAKVEEFNSRSEEKQiplPLIVVIVDELaDLMMVASKEVEDA 600
Cdd:TIGR03925 418 GYAATSAALTELIAALAALLERR-----------LPGPDVTPQQLRARSWWSG---PEIYVVVDDY-DLVATGSGNPLAP 482
|
170
....*....|....*...
gi 459386991 601 IIRLGQKARAAGIHMILA 618
Cdd:TIGR03925 483 LVELLPHARDIGLHVVVA 500
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
426-633 |
1.06e-06 |
|
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: 52.68 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 426 TVPFRELWEQSKTDpdKLLE---IPLG-KAVNGSVRSFNLARMPHLLVAGSTGSGKSVAVNGIISSILMKagpDQVKFMM 501
Cdd:TIGR03928 1056 ELSLEEFRERYEVR--KILEegsIPIGlDEETVEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGL 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 502 IDPKMVELSVYNDIPHLLIpVVTNPRKAARALQKVVDEMEKRYELFSQIgvrnlegynakveefnSRSEEKQIPLPLIVV 581
Cdd:TIGR03928 1131 IDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILAELKEEIELREAAYKEA----------------LQNETGEPAFKPILL 1193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 459386991 582 IVDELADLMMVASKEVEDAIIRLGQKARAAGIHMILATQRPSV----DVISGLIKA 633
Cdd:TIGR03928 1194 IIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ 1249
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
466-643 |
2.62e-06 |
|
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: 47.60 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 466 HLLVAGSTGSGKSVAVNGIISSILMKAGpdqvKFMMIDPKMvelSVYndiphLLIPVVTNPRKAARALqkvvdemekrye 545
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKG---ELF-----LVIPDRDDSFAALRAL------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 546 LFSQIGVRNLEGYNAKVEEFNSRseekqiplplIVVIVDELAdlMMVASKEVEDAIirlgQKARAAGIHMILATQ----- 620
Cdd:cd01127 57 FFNQLFRALTELASLSPGRLPRR----------VWFILDEFA--NLGRIPNLPNLL----ATGRKRGISVVLILQslaql 120
|
170 180
....*....|....*....|....
gi 459386991 621 -RPSVDVISGLIKANVPSRIAFAV 643
Cdd:cd01127 121 eAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
420-505 |
6.70e-06 |
|
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: 49.22 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 420 PNSEVATVPFRELWEQSKTDPdkllEIPLGKAVNGSVR-SFNLARM--PHLLVAGSTGSGKSVAVNGIISSiLMKAGpdq 496
Cdd:COG0433 4 PGSPVYLADDEELEELLGDGG----GILIGKLLSPGVPvYLDLDKLlnRHILILGATGSGKSNTLQVLLEE-LSRAG--- 75
|
....*....
gi 459386991 497 VKFMMIDPK 505
Cdd:COG0433 76 VPVLVFDPH 84
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
46-185 |
1.70e-04 |
|
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: 42.96 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459386991 46 GVFGvtSY--NIFRLLFGSLAYLLLVGAFI---YLLIPKVLREREGTISGFWLIVIGLLIefqayldwtyqgsdLFGHTL 120
Cdd:pfam13491 48 GRFG--AWlaDLLLQLFGYSAWLLPVALLYwgwRLFRRRSLERRWLRLLGFLLLLLASSA--------------LFALRL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 459386991 121 kLALSDLAKFQvtaflGGGMIGSIFYLPVSFLFANVGSFFIGLLVIAFGIFFVSPWSVYDVADGL 185
Cdd:pfam13491 112 -PSLEFGLPGG-----AGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAERL 170
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
465-504 |
7.57e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 39.55 E-value: 7.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 459386991 465 PHLLVAGSTGSGKSVAVNGIISSiLMKAGPDQVkfmMIDP 504
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQ-LLRYGARIV---IFDP 240
|
|
| |
