|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
191-822 |
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: 892.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 191 FGIGFSLFFHVSWMAVAERIGEAIELSIEWVILRYQDREDRRQGMAATVKREEVVVKEREKHVERHPELLQKLAAKAVKA 270
Cdd:COG1674 1 LLLLLLLLALLAGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 271 VKGEDKGSGKIEPGGEPMTAAPTPAPIIRVEPPMVSIPRSERAEKEKQAPLFGELEntdMPPLALLDEAPPAQETVAVET 350
Cdd:COG1674 81 LLLLLLGLLGAALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAV---LPPLDLLDPPPPKKEKIDEEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 351 LEFTSRLIEKKLSDFGVEAKVVAAYPGPVVTRYEIEPATGVKGSQIVNLARDLARSLSLTSIRVVETIPGKNYMALELPN 430
Cdd:COG1674 158 LEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 431 AKRQIVRLSEIVGSKVYADNVSALTVALGKDIAGKPVVADLAKMPHLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMI 510
Cdd:COG1674 238 KKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 511 LIDPKMLEMSVYEGIPHLLAPVVTDMRQAGHALNWAVNEMERRYKLMSKLGVRNLAGYNAKIAEAAKREEhipnpfsitp 590
Cdd:COG1674 318 LIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGE---------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 591 dSPEPLEKLPTIVIIIDELADLMMVVGKKVEELIARIAQKARAAGLHLILATQRPSVDVITGLIKANIPTRIAFQVSSKI 670
Cdd:COG1674 388 -EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 671 DSRTILDQMGAETLLGMGDMLYMPPGTGLPIRVHGAFVSDDEVHRVVAHLKLQGEPNYIDGILEGGTLEDGSgggegaaa 750
Cdd:COG1674 467 DSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEG-------- 538
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1419377277 751 gEGGGEADPMYDQAVQVVLKNRRASISLVQRHLRIGYNRAARLLEQMEQSGVVSAMQSNGNRDILVPAASAE 822
Cdd:COG1674 539 -GDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELE 609
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
328-817 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 709.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 328 TDMPPLALLDEAPPAQETVAVETLEFTSRLIEKKLSDFGVEAKVVAAYPGPVVTRYEIEPATGVKGSQIVNLARDLARSL 407
Cdd:PRK10263 864 TPLPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 408 SLTSIRVVETIPGKNYMALELPNAKRQIVRLSEIVGSKVYADNVSALTVALGKDIAGKPVVADLAKMPHLLVAGTTGSGK 487
Cdd:PRK10263 944 STVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGK 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 488 SVGINATILSLLYKSDPQDVRMILIDPKMLEMSVYEGIPHLLAPVVTDMRQAGHALNWAVNEMERRYKLMSKLGVRNLAG 567
Cdd:PRK10263 1024 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAG 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 568 YNAKIAEAAKREEHIPNPFSITPDSPEP----LEKLPTIVIIIDELADLMMVVGKKVEELIARIAQKARAAGLHLILATQ 643
Cdd:PRK10263 1104 YNEKIAEADRMMRPIPDPYWKPGDSMDAqhpvLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQ 1183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 644 RPSVDVITGLIKANIPTRIAFQVSSKIDSRTILDQMGAETLLGMGDMLYMPPGTGLPIRVHGAFVSDDEVHRVVAHLKLQ 723
Cdd:PRK10263 1184 RPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKAR 1263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 724 GEPNYIDGILE------GGTLEDGSgggegaaageggGEADPMYDQAVQVVLKNRRASISLVQRHLRIGYNRAARLLEQM 797
Cdd:PRK10263 1264 GRPQYVDGITSdsesegGAGGFDGA------------EELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQM 1331
|
490 500
....*....|....*....|
gi 1419377277 798 EQSGVVSAMQSNGNRDILVP 817
Cdd:PRK10263 1332 EAQGIVSEQGHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
438-646 |
2.95e-73 |
|
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: 238.43 E-value: 2.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 438 LSEIVGSKVYADNVSALTVALGKDIAGKPVVADLAKMP-HLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMILIDPKM 516
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 517 LEMSVYEGIPHLLA-PVVTDMRQAGHALNWAVNEMERRYKLMSKLGVRNLAGYNAKIAEAAKREEHIPNPFS----ITPD 591
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIygvhVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1419377277 592 SPEPLEKLPTIVIIIDELADLMMVVGKK----VEELIARIAQKARAAGLHLILATQRPS 646
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
28-211 |
1.28e-49 |
|
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: 172.39 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 28 RLLSEARWFALAALCLYFILIMASYHKVDPGWSHA-SLVPKVSNLGGRAGAWISDLMLYIFGFSAWWWCLYLVRYVWRGY 106
Cdd:pfam13491 2 RLLRELLGLALLLLGLFLLLALVSYSPADPSWSTSgSGAAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 107 RRLTrtflLEQPAdedpehshegmIRLIGFVLLLIGSMGLEYLRMRSLHVELPRTPGGVLGQLLGNAAQVGLGSTGGTLM 186
Cdd:pfam13491 82 RRRS----LERRW-----------LRLLGFLLLLLASSALFALRLPSLEFGLPGGAGGVIGRLLANALVTLLGFTGATLL 146
|
170 180
....*....|....*....|....*
gi 1419377277 187 LLLLFGIGFSLFFHVSWMAVAERIG 211
Cdd:pfam13491 147 LLALLAIGLSLVTGFSWLALAERLG 171
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
758-817 |
4.16e-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: 107.11 E-value: 4.16e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 758 DPMYDQAVQVVLKNRRASISLVQRHLRIGYNRAARLLEQMEQSGVVSAMQSNGNRDILVP 817
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
475-676 |
4.85e-25 |
|
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: 112.00 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 475 PHLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMILIDPKMLEMS-VYEGIPHLLApVVT--DMRQAGHALNWAVNEME 551
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLG-TITnlDGAQSMRALASIKAELK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 552 RRYKLMSKLGVRNLAGYNakiaEAAKREEHipnpfsitpdspepLEKLPTIVIIIDELADLmmvvgkKVE------ELI- 624
Cdd:TIGR03928 549 KRQRLFGENNVNHINQYQ----KLYKQGKA--------------KEPMPHLFLISDEFAEL------KSEqpefmkELVs 604
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1419377277 625 -ARIaqkARAAGLHLILATQRPSvDVITGLIKANIPTRIAFQVSSKIDSRTIL 676
Cdd:TIGR03928 605 tARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
28-232 |
1.18e-17 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 88.22 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 28 RLLSEARWFALAALCLYFILIMASYHKVDPGWSHASLVPKVSNLGGRAGAWISDLMLYIFGFSAWWWCLYLVRYVWRGYR 107
Cdd:PRK10263 20 RRLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIVGGCWFAWR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 108 rltrtfllEQPADEDPEHSHEGMiRLIGFVLLLIGSMGLEYLRMRSLHVelpRTPGGVLGQLLGNAAQVGLGSTGGTLML 187
Cdd:PRK10263 100 --------HQSSDEYIDYFAVSL-RIIGVLALILTSCGLAAINADDIWY---FASGGVIGSLLSTTLQPLLHSSGGTIAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419377277 188 LLLFGIGFSLFFHVSWMAVAERIGeaielsiEWV--ILRYQDREDRR 232
Cdd:PRK10263 168 LCVWAAGLTLFTGWSWVTIAEKLG-------GWIlnILTFASNRTRR 207
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
476-666 |
5.51e-09 |
|
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: 55.30 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 476 HLLVAGTTGSGKSVGINATILSllykSDPQDVRMILIDPKM---LEMSVYEGIPHLLAPVVTDMrqaghaLNWAVNEMER 552
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLD----QAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFNQ------LFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 553 RYKlmsklgvrnlagynakiaeaAKREEHipnpfsitpdspepleklptIVIIIDELADLMMVVGkkveelIARIAQKAR 632
Cdd:cd01127 71 LSP--------------------GRLPRR--------------------VWFILDEFANLGRIPN------LPNLLATGR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1419377277 633 AAGLHLILATQ------RPSVDVITGLIKANIPTRIAFQV 666
Cdd:cd01127 105 KRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
191-822 |
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: 892.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 191 FGIGFSLFFHVSWMAVAERIGEAIELSIEWVILRYQDREDRRQGMAATVKREEVVVKEREKHVERHPELLQKLAAKAVKA 270
Cdd:COG1674 1 LLLLLLLLALLAGLLLLLLLLLLLLLLLLLLLLLLALLLGLLLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 271 VKGEDKGSGKIEPGGEPMTAAPTPAPIIRVEPPMVSIPRSERAEKEKQAPLFGELEntdMPPLALLDEAPPAQETVAVET 350
Cdd:COG1674 81 LLLLLLGLLGAALLALLALALALLLGALGLLALAAAALGALALLLLAAAEALALAV---LPPLDLLDPPPPKKEKIDEEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 351 LEFTSRLIEKKLSDFGVEAKVVAAYPGPVVTRYEIEPATGVKGSQIVNLARDLARSLSLTSIRVVETIPGKNYMALELPN 430
Cdd:COG1674 158 LEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 431 AKRQIVRLSEIVGSKVYADNVSALTVALGKDIAGKPVVADLAKMPHLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMI 510
Cdd:COG1674 238 KKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 511 LIDPKMLEMSVYEGIPHLLAPVVTDMRQAGHALNWAVNEMERRYKLMSKLGVRNLAGYNAKIAEAAKREEhipnpfsitp 590
Cdd:COG1674 318 LIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYNEKVREAKAKGE---------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 591 dSPEPLEKLPTIVIIIDELADLMMVVGKKVEELIARIAQKARAAGLHLILATQRPSVDVITGLIKANIPTRIAFQVSSKI 670
Cdd:COG1674 388 -EEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 671 DSRTILDQMGAETLLGMGDMLYMPPGTGLPIRVHGAFVSDDEVHRVVAHLKLQGEPNYIDGILEGGTLEDGSgggegaaa 750
Cdd:COG1674 467 DSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDEG-------- 538
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1419377277 751 gEGGGEADPMYDQAVQVVLKNRRASISLVQRHLRIGYNRAARLLEQMEQSGVVSAMQSNGNRDILVPAASAE 822
Cdd:COG1674 539 -GDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELE 609
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
328-817 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 709.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 328 TDMPPLALLDEAPPAQETVAVETLEFTSRLIEKKLSDFGVEAKVVAAYPGPVVTRYEIEPATGVKGSQIVNLARDLARSL 407
Cdd:PRK10263 864 TPLPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 408 SLTSIRVVETIPGKNYMALELPNAKRQIVRLSEIVGSKVYADNVSALTVALGKDIAGKPVVADLAKMPHLLVAGTTGSGK 487
Cdd:PRK10263 944 STVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGK 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 488 SVGINATILSLLYKSDPQDVRMILIDPKMLEMSVYEGIPHLLAPVVTDMRQAGHALNWAVNEMERRYKLMSKLGVRNLAG 567
Cdd:PRK10263 1024 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAG 1103
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 568 YNAKIAEAAKREEHIPNPFSITPDSPEP----LEKLPTIVIIIDELADLMMVVGKKVEELIARIAQKARAAGLHLILATQ 643
Cdd:PRK10263 1104 YNEKIAEADRMMRPIPDPYWKPGDSMDAqhpvLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQ 1183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 644 RPSVDVITGLIKANIPTRIAFQVSSKIDSRTILDQMGAETLLGMGDMLYMPPGTGLPIRVHGAFVSDDEVHRVVAHLKLQ 723
Cdd:PRK10263 1184 RPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKAR 1263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 724 GEPNYIDGILE------GGTLEDGSgggegaaageggGEADPMYDQAVQVVLKNRRASISLVQRHLRIGYNRAARLLEQM 797
Cdd:PRK10263 1264 GRPQYVDGITSdsesegGAGGFDGA------------EELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQM 1331
|
490 500
....*....|....*....|
gi 1419377277 798 EQSGVVSAMQSNGNRDILVP 817
Cdd:PRK10263 1332 EAQGIVSEQGHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
438-646 |
2.95e-73 |
|
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: 238.43 E-value: 2.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 438 LSEIVGSKVYADNVSALTVALGKDIAGKPVVADLAKMP-HLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMILIDPKM 516
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 517 LEMSVYEGIPHLLA-PVVTDMRQAGHALNWAVNEMERRYKLMSKLGVRNLAGYNAKIAEAAKREEHIPNPFS----ITPD 591
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIygvhVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1419377277 592 SPEPLEKLPTIVIIIDELADLMMVVGKK----VEELIARIAQKARAAGLHLILATQRPS 646
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
28-211 |
1.28e-49 |
|
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: 172.39 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 28 RLLSEARWFALAALCLYFILIMASYHKVDPGWSHA-SLVPKVSNLGGRAGAWISDLMLYIFGFSAWWWCLYLVRYVWRGY 106
Cdd:pfam13491 2 RLLRELLGLALLLLGLFLLLALVSYSPADPSWSTSgSGAAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 107 RRLTrtflLEQPAdedpehshegmIRLIGFVLLLIGSMGLEYLRMRSLHVELPRTPGGVLGQLLGNAAQVGLGSTGGTLM 186
Cdd:pfam13491 82 RRRS----LERRW-----------LRLLGFLLLLLASSALFALRLPSLEFGLPGGAGGVIGRLLANALVTLLGFTGATLL 146
|
170 180
....*....|....*....|....*
gi 1419377277 187 LLLLFGIGFSLFFHVSWMAVAERIG 211
Cdd:pfam13491 147 LLALLAIGLSLVTGFSWLALAERLG 171
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
330-430 |
5.25e-41 |
|
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: 145.37 E-value: 5.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 330 MPPLALLDEAPPAQETVAVETLEFTSRLIEKKLSDFGVEAKVVAAYPGPVVTRYEIEPATGVKGSQIVNLARDLARSLSL 409
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 1419377277 410 TSIRVVETIPGKNYMALELPN 430
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
758-817 |
1.97e-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: 1.97e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 758 DPMYDQAVQVVLKNRRASISLVQRHLRIGYNRAARLLEQMEQSGVVSAMQSNGNRDILVP 817
Cdd:pfam09397 4 DELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
758-817 |
4.16e-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: 107.11 E-value: 4.16e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 758 DPMYDQAVQVVLKNRRASISLVQRHLRIGYNRAARLLEQMEQSGVVSAMQSNGNRDILVP 817
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
475-676 |
4.85e-25 |
|
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: 112.00 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 475 PHLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMILIDPKMLEMS-VYEGIPHLLApVVT--DMRQAGHALNWAVNEME 551
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLG-TITnlDGAQSMRALASIKAELK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 552 RRYKLMSKLGVRNLAGYNakiaEAAKREEHipnpfsitpdspepLEKLPTIVIIIDELADLmmvvgkKVE------ELI- 624
Cdd:TIGR03928 549 KRQRLFGENNVNHINQYQ----KLYKQGKA--------------KEPMPHLFLISDEFAEL------KSEqpefmkELVs 604
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1419377277 625 -ARIaqkARAAGLHLILATQRPSvDVITGLIKANIPTRIAFQVSSKIDSRTIL 676
Cdd:TIGR03928 605 tARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
454-711 |
5.46e-20 |
|
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: 95.04 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 454 LTVALGKDIAGKPVVADLAK-----M-PHLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMILIDPK----MLEMsvyE 523
Cdd:TIGR03924 409 LRVPIGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---E 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 524 GIPHLLApVVTDMRQAGH-------ALNwavNEMERRYKLMSKLG-VRNLAGYNAKIAEAAkreehipnpfsitpdspeP 595
Cdd:TIGR03924 486 GLPHVSA-VITNLADEAPlvdrmqdALA---GEMNRRQELLRAAGnFANVAEYEKARAAGA------------------D 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 596 LEKLPTIVIIIDELADLMmvvGKKVE--ELIARIAQKARAAGLHLILATQRPSVDVITGLiKANIPTRIAFQVSSKIDSR 673
Cdd:TIGR03924 544 LPPLPALFVVVDEFSELL---SQHPDfaDLFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESR 619
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1419377277 674 TIldqmgaetlLGMGDMLYMP--PGTGL-------PIRVHGAFVSDD 711
Cdd:TIGR03924 620 AV---------LGVPDAYHLPstPGAGYlkvdtaePVRFRAAYVSGP 657
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
28-232 |
1.18e-17 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 88.22 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 28 RLLSEARWFALAALCLYFILIMASYHKVDPGWSHASLVPKVSNLGGRAGAWISDLMLYIFGFSAWWWCLYLVRYVWRGYR 107
Cdd:PRK10263 20 RRLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIVGGCWFAWR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 108 rltrtfllEQPADEDPEHSHEGMiRLIGFVLLLIGSMGLEYLRMRSLHVelpRTPGGVLGQLLGNAAQVGLGSTGGTLML 187
Cdd:PRK10263 100 --------HQSSDEYIDYFAVSL-RIIGVLALILTSCGLAAINADDIWY---FASGGVIGSLLSTTLQPLLHSSGGTIAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1419377277 188 LLLFGIGFSLFFHVSWMAVAERIGeaielsiEWV--ILRYQDREDRR 232
Cdd:PRK10263 168 LCVWAAGLTLFTGWSWVTIAEKLG-------GWIlnILTFASNRTRR 207
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
466-676 |
1.16e-14 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 78.49 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 466 PVVADLAKMPHLLVAGTTGSGKSVGINATILSLLYKSDPQDVRMILID--PKMLEMsvYEGIPHlLAPVVT--DMRQAGH 541
Cdd:TIGR03928 802 PLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDfgTNGLLP--LKKLPH-VADYFTldEEEKIEK 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 542 ALNWAVNEMERRYKLMSKLGVRNLAGYNAKIAeaakreehipnpfsitpdspeplEKLPTIVIIIDELadlmMVVGK--- 618
Cdd:TIGR03928 879 LIRRIKKEIDRRKKLFSEYGVASISMYNKASG-----------------------EKLPQIVIIIDNY----DAVKEepf 931
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1419377277 619 --KVEELIARIAQKARAAGLHLIL-ATQRPSVDVItglIKANIPTRIAFQVSSKIDSRTIL 676
Cdd:TIGR03928 932 yeDFEELLIQLAREGASLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIV 989
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
442-704 |
9.92e-10 |
|
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: 61.16 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 442 VGSKVYADNVSAL--------TVALGKDI-AGKPVVADLAKM--PHLLVAGTTGSGKSVginaTILSLLYKSDPQDVRMI 510
Cdd:COG0433 4 PGSPVYLADDEELeellgdggGILIGKLLsPGVPVYLDLDKLlnRHILILGATGSGKSN----TLQVLLEELSRAGVPVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 511 LIDPK--------------------------------MLEMSVYEGIPHLLAPVVTDMRQAGhALNWAVNEMERRYK--- 555
Cdd:COG0433 80 VFDPHgeysglaepgaeradvgvfdpgagrplpinpwDLFATASELGPLLLSRLDLNDTQRG-VLREALRLADDKGLlll 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 556 ----LMSKLG-VRNLAGYNAKIAEAAKR-----------------------EEHIPNPFSIT------------------ 589
Cdd:COG0433 159 dlkdLIALLEeGEELGEEYGNVSAASAGallrrleslesadglfgepgldlEDLLRTDGRVTvidlsglpeelqstfvlw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 590 ---------PDSPEPLEKLPTIVIIIDELADLMMVVGKKVEELIARIAQKARAAGLHLILATQRPSvDVITGlIKANIPT 660
Cdd:COG0433 239 llrelfearPEVGDADDRKLPLVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGT 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1419377277 661 RIAFQVSSKIDSRTI---LDQMGAETL-----LGMGDMLYMPPGTGLPIRVH 704
Cdd:COG0433 317 QIILRLFNPRDQKAVkaaAETLSEDLLerlpsLGTGEALVLGEGIPLPVLVK 368
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
476-666 |
5.51e-09 |
|
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: 55.30 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 476 HLLVAGTTGSGKSVGINATILSllykSDPQDVRMILIDPKM---LEMSVYEGIPHLLAPVVTDMrqaghaLNWAVNEMER 552
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLD----QAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFNQ------LFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 553 RYKlmsklgvrnlagynakiaeaAKREEHipnpfsitpdspepleklptIVIIIDELADLMMVVGkkveelIARIAQKAR 632
Cdd:cd01127 71 LSP--------------------GRLPRR--------------------VWFILDEFANLGRIPN------LPNLLATGR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1419377277 633 AAGLHLILATQ------RPSVDVITGLIKANIPTRIAFQV 666
Cdd:cd01127 105 KRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
438-656 |
6.57e-08 |
|
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: 56.53 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 438 LSEIVGSKVYADNVSALTVALGKDIAG-KPVVADLAKMPHLLVAGTTGSGKSvGINATILSLLYKSDPQDVrmILIDPKM 516
Cdd:TIGR03928 1059 LEEFRERYEVRKILEEGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKT-NVLKSLLKTLAKQEKEKI--GLIDSID 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 517 LEMSVYEGIPHLlAPVVTDMRQAGHALNWAVNEMERRyklmsklgvrnlagyNAKIAEAAKREEHIPNPfsitpdspepl 596
Cdd:TIGR03928 1136 RGLLAYRDLKEV-ATYIEEKEDLKEILAELKEEIELR---------------EAAYKEALQNETGEPAF----------- 1188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1419377277 597 eklPTIVIIIDELADLMMVVGKKVEELIARIAQKARAAGLHLILATQRPSV----DVITGLIKA 656
Cdd:TIGR03928 1189 ---KPILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ 1249
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
353-641 |
2.41e-05 |
|
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: 47.68 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 353 FTSRlIEKKL-----SDFG--VEAKVVAAYPGPVVTRYEIEPATGVKGSQIVNLARDLARSLSLTSIRVVETIPGKNYMA 425
Cdd:TIGR03925 244 IGTR-IELRLgdpmdSEIDrrAAARVPAGRPGRGLTPDGLHMLIALPRLDGIASVDDLGTRGLVAVIRDVWGGPPAPPVR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 426 LeLPnakrQIVRLSEIVGSkvyaDNVSALTVALGKDIAG-KPVVADLAKMPHLLVAGTTGSGKSVGINATILSLLYKSDP 504
Cdd:TIGR03925 323 L-LP----ARLPLSALPAG----GGAPRLRVPLGLGESDlAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSP 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1419377277 505 QDVRMILIDPKmlemsvyegipHLLAPVVTDMRQAGHAlnwavnemerryklMSKLGVRNLAGynakiAEAAKREEHIPn 584
Cdd:TIGR03925 394 DQARLVVVDYR-----------RTLLGAVPEDYLAGYA--------------ATSAALTELIA-----ALAALLERRLP- 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1419377277 585 pfsiTPD-SPEPLEKL-----PTIVIIIDELADLMMVVGKKVEELIARIAQkARAAGLHLILA 641
Cdd:TIGR03925 443 ----GPDvTPQQLRARswwsgPEIYVVVDDYDLVATGSGNPLAPLVELLPH-ARDIGLHVVVA 500
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
456-514 |
1.23e-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: 1.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1419377277 456 VALGKDIAGKPVVADLAKM---PHLLVAGTTGSGKSVGINATILSLLYksdpQDVRMILIDP 514
Cdd:COG3451 183 IYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLR----YGARIVIFDP 240
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
476-515 |
8.36e-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: 39.58 E-value: 8.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1419377277 476 HLLVAGTTGSGKSVGInatILSLLYKSDPQDvRMILIDPK 515
Cdd:COG3505 1 HVLVIGPTGSGKTVGL---VIPNLTQLARGE-SVVVTDPK 36
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