|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
109-720 |
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: 776.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 109 VLGILSFFAGHVSVMGQDIFLPGIVGDLLGKHLLGRLAGSAGGLVLLVALLLFSLMLVTGLPLSGLPGLvrkDSSPEKVR 188
Cdd:COG1674 5 LLLLALLAGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLL---LLLGLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 189 EKVKEKLAPREAWEEETPRRQATEGRGEAAPPRVVARKPVPEEAAPPRTAGKAFVLPSLDLLEPARGVEEGVDEETLREN 268
Cdd:COG1674 82 LLLLLGLLGAALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 269 AQALLSKLAEHGIEGQITEIRTGPLVTMYEFRPAPGIKANRVSAMADDLALAMRCESVRVVPNIPGKGVMGFEIPNARRA 348
Cdd:COG1674 162 ARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 349 PIVLRELLGCPAYASAVPALSLAMGKDIFGDPVVRDLGKMPHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDP 428
Cdd:COG1674 242 TVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 429 KMLELSLYDGIPHLYHPVVTQPRDAAQVLKWAVGEMRGRYQLMMENGVRHIDAFNQFVEKRLrsggrsKAEGEGDDLVKL 508
Cdd:COG1674 322 KMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAK------AKGEEEEGLEPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 509 PYIVIVIDELADLMMTSAsrREVEDSITQLTQMARAAGIHLIFATQRPSVDVLTGVIKANFPSRVSFKVISQFDSRTILD 588
Cdd:COG1674 396 PYIVVIIDELADLMMVAG--KEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 589 QSGAETLLGFGDMLFLQPGVGGIVRVHCPYVGEGEIQRVVEHLKAQGPPVYDSAITAPPSTEDPDPS---RDEMFDAAVE 665
Cdd:COG1674 474 QGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGDddeDDELFDEAVE 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1084737110 666 EVVRAGRASVSFLQRRLKIGFNRAARIVEEMERQGIVGPAEGGKQREVYVTRKEE 720
Cdd:COG1674 554 LVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
244-713 |
1.22e-154 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 483.05 E-value: 1.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 244 LPSLDLLEPARGVEEGVDEETLRENAQALLSKLAEHGIEGQITEIRTGPLVTMYEFRPAPGIKANRVSAMADDLALAMRC 323
Cdd:PRK10263 866 LPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 324 ESVRVVPNIPGKGVMGFEIPNARRAPIVLRELLGCPAYASAVPALSLAMGKDIFGDPVVRDLGKMPHLLIAGATGSGKSV 403
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 404 ALHTMILSILFRATPDEVRLILVDPKMLELSLYDGIPHLYHPVVTQPRDAAQVLKWAVGEMRGRYQLMMENGVRHIDAFN 483
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 484 QFVEKRLRSG----------GRSkAEGEGDDLVKLPYIVIVIDELADLMMTSAsrREVEDSITQLTQMARAAGIHLIFAT 553
Cdd:PRK10263 1106 EKIAEADRMMrpipdpywkpGDS-MDAQHPVLKKEPYIVVLVDEFADLMMTVG--KKVEELIARLAQKARAAGIHLVLAT 1182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 554 QRPSVDVLTGVIKANFPSRVSFKVISQFDSRTILDQSGAETLLGFGDMLFLQPGVGGIVRVHCPYVGEGEIQRVVEHLKA 633
Cdd:PRK10263 1183 QRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKA 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 634 QGPPVYDSAITAPPSTE------DPDPSRDEMFDAAVEEVVRAGRASVSFLQRRLKIGFNRAARIVEEMERQGIVGPAEG 707
Cdd:PRK10263 1263 RGRPQYVDGITSDSESEggaggfDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGH 1342
|
....*.
gi 1084737110 708 GKQREV 713
Cdd:PRK10263 1343 NGNREV 1348
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
352-557 |
1.02e-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: 211.08 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 352 LRELLGCPAYASAVPALSLAMGKDIFGDPVVRDLGKMP-HLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPKM 430
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 431 LELSLYDGIPHLYH-PVVTQPRDAAQVLKWAVGEMRGRYQLMMENGVRHIDAFNQ---------FVEKRLRSGGRSKAEG 500
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGeiaedpldgFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084737110 501 EGDDLVKLPYIVIVIDELADLMMTSA--SRREVEDSITQLTQMARAAGIHLIFATQRPS 557
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPkdSEMRVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
7-174 |
3.05e-29 |
|
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: 114.22 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 7 AKIRRETVAVLFLAAGVVLSVALVSFHQMDPSLSTAGSPEPEVRNWAGWGGAILSDLLLQLFGVGAVGFPVLCLLLAYWT 86
Cdd:pfam13491 1 ERLLRELLGLALLLLGLFLLLALVSYSPADPSWSTSGSGAAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 87 YRGEGILGKWGRAAGGLLAVCSVLGILSFFAGHVSvMGQDIFLPGIVGDLLGKHLLgRLAGSAGGLVLLVALLLFSLMLV 166
Cdd:pfam13491 81 FRRRSLERRWLRLLGFLLLLLASSALFALRLPSLE-FGLPGGAGGVIGRLLANALV-TLLGFTGATLLLLALLAIGLSLV 158
|
....*...
gi 1084737110 167 TGLPLSGL 174
Cdd:pfam13491 159 TGFSWLAL 166
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
655-716 |
1.12e-27 |
|
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: 105.96 E-value: 1.12e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084737110 655 SRDEMFDAAVEEVVRAGRASVSFLQRRLKIGFNRAARIVEEMERQGIVGPAEGGKQREVYVT 716
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
389-592 |
4.45e-22 |
|
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: 101.99 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 389 PHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPK---MLElsLYDGIPHLYhPVVTQpRDAAQVLKWAV---G 462
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNLPHLL-GTITN-LDGAQSMRALAsikA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 463 EMRGRYQLMMENGVRHIdafNQFVEKrlrsggrSKaegEGDDLVKLPYIVIVIDELADLmmtsasRREVEDSITQLTQMA 542
Cdd:TIGR03928 546 ELKKRQRLFGENNVNHI---NQYQKL-------YK---QGKAKEPMPHLFLISDEFAEL------KSEQPEFMKELVSTA 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1084737110 543 ---RAAGIHLIFATQRPSvDVLTGVIKANFPSRVSFKVISQFDSRTILDQSGA 592
Cdd:TIGR03928 607 rigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDA 658
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1-88 |
2.24e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 51.24 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 1 MTLADLAKIRRETVAVLFLAA--GVVLSVALVSFHQMDPSLSTAGSPEPeVRNWAGWGGAILSDLLLQLFGVGAVGFPVL 78
Cdd:PRK10263 11 VTLTKLSSGRRLLEALLILIVlfAVWLMAALLSFNPSDPSWSQTAWHEP-IHNLGGMPGAWLADTLFFIFGVMAYTIPVI 89
|
90
....*....|
gi 1084737110 79 CLLLAYWTYR 88
Cdd:PRK10263 90 IVGGCWFAWR 99
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
390-575 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 390 HLLIAGATGSGKSVALHTMILSILFRATpdevRLILVDPKmlelslydgiPHLYhpVVTQPRD------AAQVLKWavge 463
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPK----------GELF--LVIPDRDdsfaalRALFFNQ---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 464 mrgryqlmmengvrhidAFNQFVEKRLRSGGRSKaegegddlvklPYIVIVIDELADLMMtsasrrevEDSITQLTQMAR 543
Cdd:cd01127 61 -----------------LFRALTELASLSPGRLP-----------RRVWFILDEFANLGR--------IPNLPNLLATGR 104
|
170 180 190
....*....|....*....|....*....|....*...
gi 1084737110 544 AAGIHLIFATQ------RPSVDVLTGVIKANFPSRVSF 575
Cdd:cd01127 105 KRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYL 142
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
109-720 |
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: 776.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 109 VLGILSFFAGHVSVMGQDIFLPGIVGDLLGKHLLGRLAGSAGGLVLLVALLLFSLMLVTGLPLSGLPGLvrkDSSPEKVR 188
Cdd:COG1674 5 LLLLALLAGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLL---LLLGLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 189 EKVKEKLAPREAWEEETPRRQATEGRGEAAPPRVVARKPVPEEAAPPRTAGKAFVLPSLDLLEPARGVEEGVDEETLREN 268
Cdd:COG1674 82 LLLLLGLLGAALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 269 AQALLSKLAEHGIEGQITEIRTGPLVTMYEFRPAPGIKANRVSAMADDLALAMRCESVRVVPNIPGKGVMGFEIPNARRA 348
Cdd:COG1674 162 ARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 349 PIVLRELLGCPAYASAVPALSLAMGKDIFGDPVVRDLGKMPHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDP 428
Cdd:COG1674 242 TVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 429 KMLELSLYDGIPHLYHPVVTQPRDAAQVLKWAVGEMRGRYQLMMENGVRHIDAFNQFVEKRLrsggrsKAEGEGDDLVKL 508
Cdd:COG1674 322 KMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAK------AKGEEEEGLEPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 509 PYIVIVIDELADLMMTSAsrREVEDSITQLTQMARAAGIHLIFATQRPSVDVLTGVIKANFPSRVSFKVISQFDSRTILD 588
Cdd:COG1674 396 PYIVVIIDELADLMMVAG--KEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 589 QSGAETLLGFGDMLFLQPGVGGIVRVHCPYVGEGEIQRVVEHLKAQGPPVYDSAITAPPSTEDPDPS---RDEMFDAAVE 665
Cdd:COG1674 474 QGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEGGDddeDDELFDEAVE 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1084737110 666 EVVRAGRASVSFLQRRLKIGFNRAARIVEEMERQGIVGPAEGGKQREVYVTRKEE 720
Cdd:COG1674 554 LVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
244-713 |
1.22e-154 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 483.05 E-value: 1.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 244 LPSLDLLEPARGVEEGVDEETLRENAQALLSKLAEHGIEGQITEIRTGPLVTMYEFRPAPGIKANRVSAMADDLALAMRC 323
Cdd:PRK10263 866 LPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLST 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 324 ESVRVVPNIPGKGVMGFEIPNARRAPIVLRELLGCPAYASAVPALSLAMGKDIFGDPVVRDLGKMPHLLIAGATGSGKSV 403
Cdd:PRK10263 946 VAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSV 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 404 ALHTMILSILFRATPDEVRLILVDPKMLELSLYDGIPHLYHPVVTQPRDAAQVLKWAVGEMRGRYQLMMENGVRHIDAFN 483
Cdd:PRK10263 1026 GVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYN 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 484 QFVEKRLRSG----------GRSkAEGEGDDLVKLPYIVIVIDELADLMMTSAsrREVEDSITQLTQMARAAGIHLIFAT 553
Cdd:PRK10263 1106 EKIAEADRMMrpipdpywkpGDS-MDAQHPVLKKEPYIVVLVDEFADLMMTVG--KKVEELIARLAQKARAAGIHLVLAT 1182
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 554 QRPSVDVLTGVIKANFPSRVSFKVISQFDSRTILDQSGAETLLGFGDMLFLQPGVGGIVRVHCPYVGEGEIQRVVEHLKA 633
Cdd:PRK10263 1183 QRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKA 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 634 QGPPVYDSAITAPPSTE------DPDPSRDEMFDAAVEEVVRAGRASVSFLQRRLKIGFNRAARIVEEMERQGIVGPAEG 707
Cdd:PRK10263 1263 RGRPQYVDGITSDSESEggaggfDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGH 1342
|
....*.
gi 1084737110 708 GKQREV 713
Cdd:PRK10263 1343 NGNREV 1348
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
352-557 |
1.02e-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: 211.08 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 352 LRELLGCPAYASAVPALSLAMGKDIFGDPVVRDLGKMP-HLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPKM 430
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 431 LELSLYDGIPHLYH-PVVTQPRDAAQVLKWAVGEMRGRYQLMMENGVRHIDAFNQ---------FVEKRLRSGGRSKAEG 500
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGeiaedpldgFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084737110 501 EGDDLVKLPYIVIVIDELADLMMTSA--SRREVEDSITQLTQMARAAGIHLIFATQRPS 557
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPkdSEMRVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
244-344 |
7.16e-38 |
|
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: 136.13 E-value: 7.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 244 LPSLDLLEPARGVEEGVDEETLRENAQALLSKLAEHGIEGQITEIRTGPLVTMYEFRPAPGIKANRVSAMADDLALAMRC 323
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 1084737110 324 ESVRVVPNIPGKGVMGFEIPN 344
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
655-716 |
2.49e-29 |
|
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 462786 [Multi-domain] Cd Length: 63 Bit Score: 110.54 E-value: 2.49e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084737110 655 SRDEMFDAAVEEVVRAGRASVSFLQRRLKIGFNRAARIVEEMERQGIVGPAEGGKQREVYVT 716
Cdd:pfam09397 2 EEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
7-174 |
3.05e-29 |
|
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: 114.22 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 7 AKIRRETVAVLFLAAGVVLSVALVSFHQMDPSLSTAGSPEPEVRNWAGWGGAILSDLLLQLFGVGAVGFPVLCLLLAYWT 86
Cdd:pfam13491 1 ERLLRELLGLALLLLGLFLLLALVSYSPADPSWSTSGSGAAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 87 YRGEGILGKWGRAAGGLLAVCSVLGILSFFAGHVSvMGQDIFLPGIVGDLLGKHLLgRLAGSAGGLVLLVALLLFSLMLV 166
Cdd:pfam13491 81 FRRRSLERRWLRLLGFLLLLLASSALFALRLPSLE-FGLPGGAGGVIGRLLANALV-TLLGFTGATLLLLALLAIGLSLV 158
|
....*...
gi 1084737110 167 TGLPLSGL 174
Cdd:pfam13491 159 TGFSWLAL 166
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
655-716 |
1.12e-27 |
|
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: 105.96 E-value: 1.12e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084737110 655 SRDEMFDAAVEEVVRAGRASVSFLQRRLKIGFNRAARIVEEMERQGIVGPAEGGKQREVYVT 716
Cdd:smart00843 2 EEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
389-592 |
4.45e-22 |
|
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: 101.99 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 389 PHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPK---MLElsLYDGIPHLYhPVVTQpRDAAQVLKWAV---G 462
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMAN--LFKNLPHLL-GTITN-LDGAQSMRALAsikA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 463 EMRGRYQLMMENGVRHIdafNQFVEKrlrsggrSKaegEGDDLVKLPYIVIVIDELADLmmtsasRREVEDSITQLTQMA 542
Cdd:TIGR03928 546 ELKKRQRLFGENNVNHI---NQYQKL-------YK---QGKAKEPMPHLFLISDEFAEL------KSEQPEFMKELVSTA 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1084737110 543 ---RAAGIHLIFATQRPSvDVLTGVIKANFPSRVSFKVISQFDSRTILDQSGA 592
Cdd:TIGR03928 607 rigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDA 658
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
378-619 |
1.77e-16 |
|
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: 83.48 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 378 GDPVVRDL-----GKM-PHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPKmlELSLYDGIPHLYH------- 444
Cdd:TIGR03924 419 GEPVELDLkesaeGGMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFK--GGATFLGLEGLPHvsavitn 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 445 -----PVVTQPRDAAQvlkwavGEMRGRYQLMMENG-VRHIDAFNQfvekrlrsggrskAEGEGDDLVKLPYIVIVIDEL 518
Cdd:TIGR03924 497 ladeaPLVDRMQDALA------GEMNRRQELLRAAGnFANVAEYEK-------------ARAAGADLPPLPALFVVVDEF 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 519 ADLMmtsASRREVEDSITQLTQMARAAGIHLIFATQRPSVDVLTGvIKANFPSRVSFKVISQFDSRTILDQSGAETL--- 595
Cdd:TIGR03924 558 SELL---SQHPDFADLFVAIGRLGRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHLpst 633
|
250 260
....*....|....*....|....
gi 1084737110 596 LGFGdmlFLQPGVGGIVRVHCPYV 619
Cdd:TIGR03924 634 PGAG---YLKVDTAEPVRFRAAYV 654
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
380-587 |
6.99e-16 |
|
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: 82.34 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 380 PVVRDLGKMPHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPKMLELSLYDGIPHLYHPV-VTQPRDAAQVLK 458
Cdd:TIGR03928 802 PLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFtLDEEEKIEKLIR 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 459 WAVGEMRGRYQLMMENGVRHIDAFNQFVEKrlrsggrskaegegddlvKLPYIVIVIDELaDLMMTSASRREVEDSITQL 538
Cdd:TIGR03928 882 RIKKEIDRRKKLFSEYGVASISMYNKASGE------------------KLPQIVIIIDNY-DAVKEEPFYEDFEELLIQL 942
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1084737110 539 TQMARAAGIHLIF-ATQRPSVDVltgVIKANFPSRVSFKVISQFDSRTIL 587
Cdd:TIGR03928 943 AREGASLGIYLVMtAGRQNAVRM---PLMNNIKTKIALYLIDKSEYRSIV 989
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
311-552 |
1.11e-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: 61.55 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 311 SAMADDLALAMRCESVRVVPniPGKGVmgfeiPNARRAPIVL--RELLGCPAyasaVPALSLAMGKDIFG-DPVVRDLGK 387
Cdd:TIGR03925 294 IASVDDLGTRGLVAVIRDVW--GGPPA-----PPVRLLPARLplSALPAGGG----APRLRVPLGLGESDlAPVYVDFAE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 388 MPHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPKmleLSLYDGIPHlyhpvvtqprdaaqvlkwavgEMRGR 467
Cdd:TIGR03925 363 SPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR---RTLLGAVPE---------------------DYLAG 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 468 YQLMMENGVRHIDAFNQFVEKRLRSGGRSKAEGEGDDLVKLPYIVIVIDELaDLMMTSASrreveDSITQLTQM---ARA 544
Cdd:TIGR03925 419 YAATSAALTELIAALAALLERRLPGPDVTPQQLRARSWWSGPEIYVVVDDY-DLVATGSG-----NPLAPLVELlphARD 492
|
....*...
gi 1084737110 545 AGIHLIFA 552
Cdd:TIGR03925 493 IGLHVVVA 500
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
379-584 |
5.12e-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: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 379 DPVVRDL-GKMPHLLIAGATGSGKSVALHTMILSILFRATPDEVRLILVDPKMLELSLYDGIPHlyhpV--VTQPRDAAQ 455
Cdd:TIGR03925 69 DPLVVDLsGAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH----VggVAGRLDPER 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 456 VLKwAVGEMRG----RYQLMMENGVRHIDAFnqfveKRLRSGGRSKAEGEGDdlvklpyIVIVIDELADLmmtsasRRE- 530
Cdd:TIGR03925 145 VRR-TVAEVEGllrrRERLFRTHGIDSMAQY-----RARRAAGRLPEDPFGD-------VFLVIDGWGTL------RQDf 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 531 --VEDSITQLTQMARAAGIHLIFATQRPSvDVLTGViKANFPSRVSFK----VISQFDSR 584
Cdd:TIGR03925 206 edLEDKVTDLAARGLAYGVHVVLTASRWS-EIRPAL-RDLIGTRIELRlgdpMDSEIDRR 263
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
338-567 |
1.60e-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: 51.91 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 338 MGFEIPNARRAPI-------VLRELLGCPAYASAVPALSLAMGKDIFG-DPVVRDLGKMPHLLIAGATGSGKSVALHTMI 409
Cdd:TIGR03928 1038 MNEAWTGERPKPIpmvpeelSLEEFRERYEVRKILEEGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLL 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 410 LSIlfrATPDEVRLILVDPKMLELSLYDGIPHLYHpVVTQPRDAAQVLKWAVGEMRGRYQLMMEngvrhidafnqfvekr 489
Cdd:TIGR03928 1118 KTL---AKQEKEKIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILAELKEEIELREAAYKE---------------- 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 490 lrsggrskAEGEGDDLVKLPYIVIVIDELADLM-MTSAsrrEVEDSITQLTQMARAAGIHLIFATQRPSV----DVLTGV 564
Cdd:TIGR03928 1178 --------ALQNETGEPAFKPILLIIDDLEDFIqRTDL---EIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKE 1246
|
...
gi 1084737110 565 IKA 567
Cdd:TIGR03928 1247 IKQ 1249
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1-88 |
2.24e-06 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 51.24 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 1 MTLADLAKIRRETVAVLFLAA--GVVLSVALVSFHQMDPSLSTAGSPEPeVRNWAGWGGAILSDLLLQLFGVGAVGFPVL 78
Cdd:PRK10263 11 VTLTKLSSGRRLLEALLILIVlfAVWLMAALLSFNPSDPSWSQTAWHEP-IHNLGGMPGAWLADTLFFIFGVMAYTIPVI 89
|
90
....*....|
gi 1084737110 79 CLLLAYWTYR 88
Cdd:PRK10263 90 IVGGCWFAWR 99
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
390-575 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 390 HLLIAGATGSGKSVALHTMILSILFRATpdevRLILVDPKmlelslydgiPHLYhpVVTQPRD------AAQVLKWavge 463
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPK----------GELF--LVIPDRDdsfaalRALFFNQ---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 464 mrgryqlmmengvrhidAFNQFVEKRLRSGGRSKaegegddlvklPYIVIVIDELADLMMtsasrrevEDSITQLTQMAR 543
Cdd:cd01127 61 -----------------LFRALTELASLSPGRLP-----------RRVWFILDEFANLGR--------IPNLPNLLATGR 104
|
170 180 190
....*....|....*....|....*....|....*...
gi 1084737110 544 AAGIHLIFATQ------RPSVDVLTGVIKANFPSRVSF 575
Cdd:cd01127 105 KRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYL 142
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
369-615 |
1.35e-04 |
|
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: 44.98 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 369 SLAMGKDIFGD-PVVRDLGKM--PHLLIAGATGSGKSVALHTMILSI------------------LFRA----------T 417
Cdd:COG0433 25 GILIGKLLSPGvPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELsragvpvlvfdphgeysgLAEPgaeradvgvfD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 418 PDEVRLILVDPKMLELSLYDGIPHL---YHPVVTQPRDAAQVLKWAVGEMRGRYQL-----MMENG-------------- 475
Cdd:COG0433 105 PGAGRPLPINPWDLFATASELGPLLlsrLDLNDTQRGVLREALRLADDKGLLLLDLkdliaLLEEGeelgeeygnvsaas 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 476 ----VRHIDAFNQF----------VEKRLRSGGR--------------------------SKAEGEGDDLVKLPYIVIVI 515
Cdd:COG0433 185 agalLRRLESLESAdglfgepgldLEDLLRTDGRvtvidlsglpeelqstfvlwllrelfEARPEVGDADDRKLPLVLVI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084737110 516 DELADLMmtSASRREVEDSITQLTQMARAAGIHLIFATQRPSvDVLTGVIkANFPSRVSFKVISQFDSRTI------LDQ 589
Cdd:COG0433 265 DEAHLLA--PAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDEDVL-SQLGTQIILRLFNPRDQKAVkaaaetLSE 340
|
330 340
....*....|....*....|....*...
gi 1084737110 590 SGAETL--LGFGDMLFLQPGVGGIVRVH 615
Cdd:COG0433 341 DLLERLpsLGTGEALVLGEGIPLPVLVK 368
|
|
| |
