|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
344-854 |
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: 777.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 344 AAIEKEAQEVTQTIARSLEEDAPRAYVYPSLDLLTQPSGDSARAAHEELEGTLDRLSSVLNSFGIDGHVTGAVQGPSVTR 423
Cdd:COG1674 110 LLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 424 YEVALEQGVRLNKLTNLSDDVALALGVSSVRI-APVPGKiSVVGIEVPNKVVIPVPIREVLDSPAFRRHKSSVAFSVGKD 502
Cdd:COG1674 190 YEIEPAPGVKVSKITNLADDIALALAAKSVRIeAPIPGK-SAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKD 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 503 IGGNYIVGDCSKLPHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKMVELGGYNGIPHLLIPVVTDPKKAAG 582
Cdd:COG1674 269 ISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAAN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 583 ALQWAVTEMMKRYRLFAEAGVRELSSYNQWAK-------GQEGVDTMPKVVIVIDELADLMLVAAKEVEESICRVAQMGR 655
Cdd:COG1674 349 ALKWAVREMERRYKLFAKAGVRNIAGYNEKVReakakgeEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKAR 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 656 AAGMHLVIATQRPSADVITGLMKANIPSRIAFAVASSLESRIILDNTGAEKLVGKGDMLWFPLGSGKPLRVQGCFISDEE 735
Cdd:COG1674 429 AAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 736 VAAVVDSVKQNAAAEYDDEVMAQIEQhvtesekkgksaggafPAGEAGEEEQDELFPAGVDVILDLGQASVSLLQRRLKL 815
Cdd:COG1674 509 VERVVDFLKSQGEPEYIEEILEEEEE----------------EDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRI 572
|
490 500 510
....*....|....*....|....*....|....*....
gi 524045443 816 GYARAARLMDQMEEKGIVGPSEGSKPRQILITKDQWVQM 854
Cdd:COG1674 573 GYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
255-845 |
1.61e-138 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 445.68 E-value: 1.61e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 255 LPAAKQRTGTPPQEKGKKPAPAAPAAAQVLREEEEKPPlfQPESHVKRPDEVLEELTQEAEAPAwklaEDAPVWQPPGEP 334
Cdd:PRK10263 750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAP--QPQYQQPQQPVAPQPQYQQPQQPV----APQPQYQQPQQP 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 335 --KPPTRAQRQAAIEKEAQE-------VTQTIARSLEEDAPRayvYPSLDLLTQPSGDSARAAHEELEGTLDRLSSVLNS 405
Cdd:PRK10263 824 vaPQPQYQQPQQPVAPQPQDtllhpllMRNGDSRPLHKPTTP---LPSLDLLTPPPSEVEPVDTFALEQMARLVEARLAD 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 406 FGIDGHVTGAVQGPSVTRYEVALEQGVRLNKLTNLSDDVALALGVSSVRIAPV-PGKiSVVGIEVPNKVVIPVPIREVLD 484
Cdd:PRK10263 901 FRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEViPGK-PYVGLELPNKKRQTVYLREVLD 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 485 SPAFRRHKSSVAFSVGKDIGGNYIVGDCSKLPHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKMVELGGYN 564
Cdd:PRK10263 980 NAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYE 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 565 GIPHLLIPVVTDPKKAAGALQWAVTEMMKRYRLFAEAGVRELSSYNQ----------------WAKG-----QEGV-DTM 622
Cdd:PRK10263 1060 GIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEkiaeadrmmrpipdpyWKPGdsmdaQHPVlKKE 1139
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 623 PKVVIVIDELADLMLVAAKEVEESICRVAQMGRAAGMHLVIATQRPSADVITGLMKANIPSRIAFAVASSLESRIILDNT 702
Cdd:PRK10263 1140 PYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQA 1219
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 703 GAEKLVGKGDMLWFPLGSGKPLRVQGCFISDEEVAAVVDSVKQNAAAEYDDEVmaqieqhVTESEKKGksAGGAFPAGea 782
Cdd:PRK10263 1220 GAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGI-------TSDSESEG--GAGGFDGA-- 1288
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524045443 783 geEEQDELFPAGVDVILDLGQASVSLLQRRLKLGYARAARLMDQMEEKGIVGPSEGSKPRQIL 845
Cdd:PRK10263 1289 --EELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
479-669 |
4.83e-63 |
|
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: 211.85 E-value: 4.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 479 IREVLDSPAFRRHKSSVAFSVGKDIGGNYIVGDCSKLP-HMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKM 557
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 558 VELGGYNGIPHLL-IPVVTDPKKAAGALQWAVTEMMKRYRLFAEAGVRELSSYNQWAK------------GQEGVDTM-- 622
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflVIYGVHVMct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524045443 623 --------PKVVIVIDELADLMLVAAKE----VEESICRVAQMGRAAGMHLVIATQRPS 669
Cdd:pfam01580 161 agrwleilPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
785-847 |
4.19e-28 |
|
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: 107.50 E-value: 4.19e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524045443 785 EEQDELFPAGVDVILDLGQASVSLLQRRLKLGYARAARLMDQMEEKGIVGPSEGSKPRQILIT 847
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
516-708 |
5.40e-24 |
|
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: 108.92 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 516 PHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKmvelGG-----YNGIPHLLiPVVT--DPKKAAGALQWAV 588
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYK----GGgmanlFKNLPHLL-GTITnlDGAQSMRALASIK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 589 TEMMKRYRLFAEAGVRELSSYNQWAKGQEGVDTMPKVVIVIDELADLmlvaAKEVEESI---CRVAQMGRAAGMHLVIAT 665
Cdd:TIGR03928 545 AELKKRQRLFGENNVNHINQYQKLYKQGKAKEPMPHLFLISDEFAEL----KSEQPEFMkelVSTARIGRSLGVHLILAT 620
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 524045443 666 QRPSAdVITGLMKANIPSRIAFAVASSLESRIILDNTGAEKLV 708
Cdd:TIGR03928 621 QKPSG-VVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEIT 662
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
517-689 |
1.77e-07 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 51.07 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 517 HMLIAGTTGSGKSVCINSLLISMLYKSTpeelRLIMVDPKM---VELGGYNGIPHLLIPVVTDpkkaagALQWAVTEMMK 593
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 594 RYRlfaeaGVRElssynqwakgqegvdtmPKVVIVIDELADLMLVaakeveESICRVAQMGRAAGMHLVIATQ------R 667
Cdd:cd01127 71 LSP-----GRLP-----------------RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaqleA 122
|
170 180
....*....|....*....|..
gi 524045443 668 PSADVITGLMKANIPSRIAFAV 689
Cdd:cd01127 123 VYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
344-854 |
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: 777.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 344 AAIEKEAQEVTQTIARSLEEDAPRAYVYPSLDLLTQPSGDSARAAHEELEGTLDRLSSVLNSFGIDGHVTGAVQGPSVTR 423
Cdd:COG1674 110 LLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 424 YEVALEQGVRLNKLTNLSDDVALALGVSSVRI-APVPGKiSVVGIEVPNKVVIPVPIREVLDSPAFRRHKSSVAFSVGKD 502
Cdd:COG1674 190 YEIEPAPGVKVSKITNLADDIALALAAKSVRIeAPIPGK-SAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKD 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 503 IGGNYIVGDCSKLPHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKMVELGGYNGIPHLLIPVVTDPKKAAG 582
Cdd:COG1674 269 ISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAAN 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 583 ALQWAVTEMMKRYRLFAEAGVRELSSYNQWAK-------GQEGVDTMPKVVIVIDELADLMLVAAKEVEESICRVAQMGR 655
Cdd:COG1674 349 ALKWAVREMERRYKLFAKAGVRNIAGYNEKVReakakgeEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKAR 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 656 AAGMHLVIATQRPSADVITGLMKANIPSRIAFAVASSLESRIILDNTGAEKLVGKGDMLWFPLGSGKPLRVQGCFISDEE 735
Cdd:COG1674 429 AAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 736 VAAVVDSVKQNAAAEYDDEVMAQIEQhvtesekkgksaggafPAGEAGEEEQDELFPAGVDVILDLGQASVSLLQRRLKL 815
Cdd:COG1674 509 VERVVDFLKSQGEPEYIEEILEEEEE----------------EDEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRI 572
|
490 500 510
....*....|....*....|....*....|....*....
gi 524045443 816 GYARAARLMDQMEEKGIVGPSEGSKPRQILITKDQWVQM 854
Cdd:COG1674 573 GYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
255-845 |
1.61e-138 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 445.68 E-value: 1.61e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 255 LPAAKQRTGTPPQEKGKKPAPAAPAAAQVLREEEEKPPlfQPESHVKRPDEVLEELTQEAEAPAwklaEDAPVWQPPGEP 334
Cdd:PRK10263 750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAP--QPQYQQPQQPVAPQPQYQQPQQPV----APQPQYQQPQQP 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 335 --KPPTRAQRQAAIEKEAQE-------VTQTIARSLEEDAPRayvYPSLDLLTQPSGDSARAAHEELEGTLDRLSSVLNS 405
Cdd:PRK10263 824 vaPQPQYQQPQQPVAPQPQDtllhpllMRNGDSRPLHKPTTP---LPSLDLLTPPPSEVEPVDTFALEQMARLVEARLAD 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 406 FGIDGHVTGAVQGPSVTRYEVALEQGVRLNKLTNLSDDVALALGVSSVRIAPV-PGKiSVVGIEVPNKVVIPVPIREVLD 484
Cdd:PRK10263 901 FRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEViPGK-PYVGLELPNKKRQTVYLREVLD 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 485 SPAFRRHKSSVAFSVGKDIGGNYIVGDCSKLPHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKMVELGGYN 564
Cdd:PRK10263 980 NAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYE 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 565 GIPHLLIPVVTDPKKAAGALQWAVTEMMKRYRLFAEAGVRELSSYNQ----------------WAKG-----QEGV-DTM 622
Cdd:PRK10263 1060 GIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEkiaeadrmmrpipdpyWKPGdsmdaQHPVlKKE 1139
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 623 PKVVIVIDELADLMLVAAKEVEESICRVAQMGRAAGMHLVIATQRPSADVITGLMKANIPSRIAFAVASSLESRIILDNT 702
Cdd:PRK10263 1140 PYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQA 1219
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 703 GAEKLVGKGDMLWFPLGSGKPLRVQGCFISDEEVAAVVDSVKQNAAAEYDDEVmaqieqhVTESEKKGksAGGAFPAGea 782
Cdd:PRK10263 1220 GAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGI-------TSDSESEG--GAGGFDGA-- 1288
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524045443 783 geEEQDELFPAGVDVILDLGQASVSLLQRRLKLGYARAARLMDQMEEKGIVGPSEGSKPRQIL 845
Cdd:PRK10263 1289 --EELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
479-669 |
4.83e-63 |
|
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: 211.85 E-value: 4.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 479 IREVLDSPAFRRHKSSVAFSVGKDIGGNYIVGDCSKLP-HMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKM 557
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 558 VELGGYNGIPHLL-IPVVTDPKKAAGALQWAVTEMMKRYRLFAEAGVRELSSYNQWAK------------GQEGVDTM-- 622
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAedpldgfgdvflVIYGVHVMct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 524045443 623 --------PKVVIVIDELADLMLVAAKE----VEESICRVAQMGRAAGMHLVIATQRPS 669
Cdd:pfam01580 161 agrwleilPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
372-471 |
5.44e-33 |
|
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: 122.64 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 372 PSLDLLTQPSGDSARAAHEELEGTLDRLSSVLNSFGIDGHVTGAVQGPSVTRYEVALEQGVRLNKLTNLSDDVALALGVS 451
Cdd:pfam17854 2 PPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSAP 81
|
90 100
....*....|....*....|.
gi 524045443 452 SVRI-APVPGKiSVVGIEVPN 471
Cdd:pfam17854 82 SIRIvAPIPGK-STIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
785-847 |
3.00e-32 |
|
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: 119.01 E-value: 3.00e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524045443 785 EEQDELFPAGVDVILDLGQASVSLLQRRLKLGYARAARLMDQMEEKGIVGPSEGSKPRQILIT 847
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
785-847 |
4.19e-28 |
|
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: 107.50 E-value: 4.19e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524045443 785 EEQDELFPAGVDVILDLGQASVSLLQRRLKLGYARAARLMDQMEEKGIVGPSEGSKPRQILIT 847
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
516-708 |
5.40e-24 |
|
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: 108.92 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 516 PHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKmvelGG-----YNGIPHLLiPVVT--DPKKAAGALQWAV 588
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYK----GGgmanlFKNLPHLL-GTITnlDGAQSMRALASIK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 589 TEMMKRYRLFAEAGVRELSSYNQWAKGQEGVDTMPKVVIVIDELADLmlvaAKEVEESI---CRVAQMGRAAGMHLVIAT 665
Cdd:TIGR03928 545 AELKKRQRLFGENNVNHINQYQKLYKQGKAKEPMPHLFLISDEFAEL----KSEQPEFMkelVSTARIGRSLGVHLILAT 620
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 524045443 666 QRPSAdVITGLMKANIPSRIAFAVASSLESRIILDNTGAEKLV 708
Cdd:TIGR03928 621 QKPSG-VVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEIT 662
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
516-732 |
1.08e-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: 91.19 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 516 PHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKmvelGG-----YNGIPHlLIPVVTDPKKAAG-------A 583
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFK----GGatflgLEGLPH-VSAVITNLADEAPlvdrmqdA 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 584 LQwavTEMMKRYRLFAEAG-VRELSSYNQ-WAKGQEgVDTMPKVVIVIDELADLMlvAAK----EVEESICRVaqmGRAA 657
Cdd:TIGR03924 511 LA---GEMNRRQELLRAAGnFANVAEYEKaRAAGAD-LPPLPALFVVVDEFSELL--SQHpdfaDLFVAIGRL---GRSL 581
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524045443 658 GMHLVIATQRPSADVITGLMKaNIPSRIAFAVASSLESRIILDNTGAEKLVGKGDMLWFPLGSGKPLRVQGCFIS 732
Cdd:TIGR03924 582 GVHLLLASQRLDEGRLRGLES-HLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYVS 655
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
511-711 |
3.22e-12 |
|
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: 70.79 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 511 DCSKLPHMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKMVELGGYNGIPHLL-IPVVTDPKKAAGALQWAVT 589
Cdd:TIGR03928 806 DLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVAdYFTLDEEEKIEKLIRRIKK 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 590 EMMKRYRLFAEAGVRELSSYNQWAKgqegvDTMPKVVIVIDELADLMLVAAKEVEES-ICRVAQMGRAAGMHLVIATQRP 668
Cdd:TIGR03928 886 EIDRRKKLFSEYGVASISMYNKASG-----EKLPQIVIIIDNYDAVKEEPFYEDFEElLIQLAREGASLGIYLVMTAGRQ 960
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 524045443 669 SAdvITGLMKANIPSRIAFAVASSLESRIILDNT--GAEKLVGKG 711
Cdd:TIGR03928 961 NA--VRMPLMNNIKTKIALYLIDKSEYRSIVGRTkfTIEEIPGRG 1003
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
517-697 |
4.14e-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: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 517 HMLIAGTTGSGKSVCINSLLISMLYKSTPEELRLIMVDPKMVELGGYNGIPHlLIPVVT--DPKKAAGALQWAVTEMMKR 594
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGrlDPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 595 YRLFAEAGVRELSSYNQ-WAKGQEGVDTMPKVVIVIDELADLMlVAAKEVEESICRVAQMGRAAGMHLVIATQRpSADVI 673
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRArRAAGRLPEDPFGDVFLVIDGWGTLR-QDFEDLEDKVTDLAARGLAYGVHVVLTASR-WSEIR 237
|
170 180
....*....|....*....|....
gi 524045443 674 TGLmKANIPSRIAFAVASSLESRI 697
Cdd:TIGR03925 238 PAL-RDLIGTRIELRLGDPMDSEI 260
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
517-689 |
1.77e-07 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 51.07 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 517 HMLIAGTTGSGKSVCINSLLISMLYKSTpeelRLIMVDPKM---VELGGYNGIPHLLIPVVTDpkkaagALQWAVTEMMK 593
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 594 RYRlfaeaGVRElssynqwakgqegvdtmPKVVIVIDELADLMLVaakeveESICRVAQMGRAAGMHLVIATQ------R 667
Cdd:cd01127 71 LSP-----GRLP-----------------RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaqleA 122
|
170 180
....*....|....*....|..
gi 524045443 668 PSADVITGLMKANIPSRIAFAV 689
Cdd:cd01127 123 VYGKDGAQTILGNCNTKLYLGT 144
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
517-669 |
2.19e-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: 47.68 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 517 HMLIAGTTGSGKSVCINSLLISMLYKSTPeelrLIMVDPK-----MVELGGYNGIPHLLIPVVTDP-------------- 577
Cdd:COG0433 49 HILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDPHgeysgLAEPGAERADVGVFDPGAGRPlpinpwdlfatase 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 578 ---------------------------------------------------------KKAAGALQWAVTEMMKRYRLFAE 600
Cdd:COG0433 125 lgplllsrldlndtqrgvlrealrladdkglllldlkdlialleegeelgeeygnvsAASAGALLRRLESLESADGLFGE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 601 AGV---------------------------------RELSSYNQWAKGQEGVDtmPKVVIVIDELADLMLVAAKEVEESI 647
Cdd:COG0433 205 PGLdledllrtdgrvtvidlsglpeelqstfvlwllRELFEARPEVGDADDRK--LPLVLVIDEAHLLAPAAPSALLEIL 282
|
250 260
....*....|....*....|..
gi 524045443 648 CRVAQMGRAAGMHLVIATQRPS 669
Cdd:COG0433 283 ERIAREGRKFGVGLILATQRPS 304
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
507-712 |
6.89e-05 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 46.90 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 507 YIVGDCSKLPHMLIAGTTGSGKSVCINSLLISMLYKstpEELRLIMVDPKMVELGGYNGIPHllipVVTDPKKAAGALQW 586
Cdd:TIGR03928 1088 PVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGLIDSIDRGLLAYRDLKE----VATYIEEKEDLKEI 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524045443 587 aVTEMMkryrlfAEAGVRELSsYNQWAKGQEGVDTMPKVVIVIDELADLMLVAAKEVEESICRVAQMGRAAGMHLVIATQ 666
Cdd:TIGR03928 1161 -LAELK------EEIELREAA-YKEALQNETGEPAFKPILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGT 1232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 524045443 667 RP----SADVITGLMKAnipSRIAFAVASSLESRII-LDNTGAEKLVGKGD 712
Cdd:TIGR03928 1233 HSelskSYDGVPKEIKQ---LRTGILGMRKSDQSFFkLPFTRSEKELEPGE 1280
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
516-562 |
1.24e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 45.71 E-value: 1.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 524045443 516 PHMLIAGTTGSGKSVCINSLLISMLYKSTpeelRLIMVDP-----KMVE-LGG 562
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRYGA----RIVIFDPggsyeILVRaLGG 253
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
517-556 |
6.35e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 39.97 E-value: 6.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 524045443 517 HMLIAGTTGSGKSVcinSLLISMLYKSTPEElRLIMVDPK 556
Cdd:COG3505 1 HVLVIGPTGSGKTV---GLVIPNLTQLARGE-SVVVTDPK 36
|
|
| |
