|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
422-914 |
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: 848.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 422 KTPLPSLDLLEHRPTREQDITQAEIVETSQRIEQQLRNFNVKAKVKDVLVGPVVTRYELELDPGVKASKVTGLDTDLARA 501
Cdd:COG1674 134 LAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 502 LMFRSIRVAEVIPGKPYIGIETPNDHRQIVPLRDVLDSDEFRNSKALLSMALGKDISGKPMVVDLAKMPHLLVAGTTGSG 581
Cdd:COG1674 214 LAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 582 KSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELSIYNDIPHLLTEVVTDMKKAANALRWCVDEMERRYQLLSALRVRNIE 661
Cdd:COG1674 294 KSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 662 GFNEKVDEYEALNMPipnplwkpgdsmdtlPPPLEKLSYIVVIVDEFADLMMVAGKQVEELIARLAQKARAVGIHLILAT 741
Cdd:COG1674 374 GYNEKVREAKAKGEE---------------EEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILAT 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 742 QRPSVDVITGLIKANVPSRIAFTVATKIDSRTILDAGGAESLLGKGDMLYSPQGSTELVRIHGAFMTDDEVVRVVDDWKA 821
Cdd:COG1674 439 QRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKS 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 822 RGKPNYIDGILEGDEEDAGaerlSERGGETDGLFDEVVEFVVSTGSTSISAIQRRFRVGFNRAANIMDQLEEQGIVSPVQ 901
Cdd:COG1674 519 QGEPEYIEEILEEEEEEDE----GGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAE 594
|
490
....*....|....
gi 928589029 902 -NGKREVLARSADY 914
Cdd:COG1674 595 gSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
219-909 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 733.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 219 KTPVQEAVEqptELVNPADRINISGLSKAQDMFYVPMNNGNEVNAFAPENPEfvKYDFEQQETLP-NVSISMQRGQAELS 297
Cdd:PRK10263 626 KLPSQRAAE---EKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQ--RYGEQYQHDVPvNAEDADAAAEAELA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 298 TQHDFTpvwQQTNVFGEE-----------------KSVVDFGSK---FTTS---EDMPNVSLAEPEVNVAEEDP----EQ 350
Cdd:PRK10263 701 RQFAQT---QQQRYSGEQpaganpfslddfefspmKALLDDGPHeplFTPIvepVQQPQQPVAPQQQYQQPQQPvapqPQ 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 351 SELARQFAAQEQQRLREMERRAKDMGVQDVYQQIV-----QGPTAETAPKTANYRPYG-------DSLIHPAFQQH--KK 416
Cdd:PRK10263 778 YQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVApqpqyQQPQQPVAPQPQYQQPQQpvapqpqDTLLHPLLMRNgdSR 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 417 NIEKPKTPLPSLDLLEHRPTREQDITQAEIVETSQRIEQQLRNFNVKAKVKDVLVGPVVTRYELELDPGVKASKVTGLDT 496
Cdd:PRK10263 858 PLHKPTTPLPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSR 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 497 DLARALMFRSIRVAEVIPGKPYIGIETPNDHRQIVPLRDVLDSDEFRNSKALLSMALGKDISGKPMVVDLAKMPHLLVAG 576
Cdd:PRK10263 938 DLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAG 1017
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 577 TTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELSIYNDIPHLLTEVVTDMKKAANALRWCVDEMERRYQLLSALR 656
Cdd:PRK10263 1018 TTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALG 1097
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 657 VRNIEGFNEKVDEYEALNMPIPNPLWKPGDSMDTLPPPLEKLSYIVVIVDEFADLMMVAGKQVEELIARLAQKARAVGIH 736
Cdd:PRK10263 1098 VRNLAGYNEKIAEADRMMRPIPDPYWKPGDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIH 1177
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 737 LILATQRPSVDVITGLIKANVPSRIAFTVATKIDSRTILDAGGAESLLGKGDMLYSPQGSTELVRIHGAFMTDDEVVRVV 816
Cdd:PRK10263 1178 LVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVV 1257
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 817 DDWKARGKPNYIDGILEGDEEDAGAERLsERGGETDGLFDEVVEFVVSTGSTSISAIQRRFRVGFNRAANIMDQLEEQGI 896
Cdd:PRK10263 1258 QDWKARGRPQYVDGITSDSESEGGAGGF-DGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGI 1336
|
730
....*....|....
gi 928589029 897 VS-PVQNGKREVLA 909
Cdd:PRK10263 1337 VSeQGHNGNREVLA 1350
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
533-745 |
5.34e-92 |
|
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: 290.05 E-value: 5.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 533 LRDVLDSDEFRNSKALLSMALGKDISGKPMVVDLAKMP-HLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKV 611
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 612 VELSIYNDIPHLLT-EVVTDMKKAANALRWCVDEMERRYQLLSALRVRNIEGFNEKVDEYEALNMPIPNPLWKPGDSMDT 690
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 928589029 691 LPPPLEKLSYIVVIVDEFADLMMVAGKQ----VEELIARLAQKARAVGIHLILATQRPS 745
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
26-182 |
8.92e-28 |
|
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: 110.37 E-value: 8.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 26 FGLYLIIAWSGYTPLDNSWATSGFAPETI-NKAGAFGAWFVDLFFVFFGYIGNLIPFILFFIPIYLIRSKRVENLTWtkf 104
Cdd:pfam13491 15 LGLFLLLALVSYSPADPSWSTSGSGAAPVhNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRRSLERRWL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 105 alRSFGFILLLCGLTVLATLSLNNPASYL---AGGVLGGSLTLNLYPSLGKFGVSLLAVIFAAVGFIFCSGASFIRLLMK 181
Cdd:pfam13491 92 --RLLGFLLLLLASSALFALRLPSLEFGLpggAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAER 169
|
.
gi 928589029 182 F 182
Cdd:pfam13491 170 L 170
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
849-910 |
3.71e-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: 104.80 E-value: 3.71e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928589029 849 GETDGLFDEVVEFVVSTGSTSISAIQRRFRVGFNRAANIMDQLEEQGIVSPVQ-NGKREVLAR 910
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANgSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
570-775 |
4.15e-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: 109.31 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 570 PHLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELS-IYNDIPHLLTeVVT--DMKKAANALRWCVDEME 646
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLG-TITnlDGAQSMRALASIKAELK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 647 RRYQLLSALRVRNIEGFNEKVDEYEALnMPIPnplwkpgdsmdtlpppleklsYIVVIVDEFADLMmvagKQVEELIARL 726
Cdd:TIGR03928 549 KRQRLFGENNVNHINQYQKLYKQGKAK-EPMP---------------------HLFLISDEFAELK----SEQPEFMKEL 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 928589029 727 AQKA---RAVGIHLILATQRPSvDVITGLIKANVPSRIAFTVATKIDSRTIL 775
Cdd:TIGR03928 603 VSTArigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
26-456 |
4.22e-12 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 70.50 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 26 FGLYLIIAWSGYTPLDNSWATSGFAPETINKAGAFGAWFVDLFFVFFGYIGNLIPFILFFIPIYLIRSKRVEN-LTWTKF 104
Cdd:PRK10263 33 FAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIVGGCWFAWRHQSSDEyIDYFAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 105 ALRSFG---FILLLCGltvLATLSLNNPASYLAGGVLGGSLTLNLYPSLGKFGVSLLAVIFAAVGFIFCSGASFIRLLMK 181
Cdd:PRK10263 113 SLRIIGvlaLILTSCG---LAAINADDIWYFASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAGLTLFTGWSWVTIAEK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 182 FYRWL----------TMQNPP--EDSEKTDETESEKMHMAEPPE----EIVIGKTPVQEAVEQptELVNPADRINISGLS 245
Cdd:PRK10263 190 LGGWIlniltfasnrTRRDDTwvDEDEYEDDEEYEDENHGKQHEsrraRILRGALARRKRLAE--KFINPMGRQTDAALF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 246 KAQDmfyvpMNNGNEVN------AFAPEN----------PEFVKYD--FEQQETLPNVSISMQRGQAELSTQHDFTPVWQ 307
Cdd:PRK10263 268 SGKR-----MDDDEEITytargvAADPDDvlfsgnratqPEYDEYDplLNGAPITEPVAVAAAATTATQSWAAPVEPVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 308 QTNVFGEEksvVDFGSKFTTSEDMPNVSLAEPEVNVAEED-PEQSELARQFAAQEQ--QRLREMERRAKDMGVQDVYQQI 384
Cdd:PRK10263 343 TPPVASVD---VPPAQPTVAWQPVPGPQTGEPVIAPAPEGyPQQSQYAQPAVQYNEplQQPVQPQQPYYAPAAEQPAQQP 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928589029 385 VQGPTAETAPKTANYRPygdslihpafQQHKKNIEKPKTPLPSLDLLEHRPTRE------QDITQAEIVETSQRIEQQ 456
Cdd:PRK10263 420 YYAPAPEQPAQQPYYAP----------APEQPVAGNAWQAEEQQSTFAPQSTYQteqtyqQPAAQEPLYQQPQPVEQQ 487
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
571-763 |
3.59e-06 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 47.60 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 571 HLLVAGTTGSGKSVGVNTMILSLLyrvkPEEVKFIMIDPKvVELSIyndiphllteVVTDMKKAANALrwcvdemerRYQ 650
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPK-GELFL----------VIPDRDDSFAAL---------RAL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 651 LLSALRVRNIEGFNekvdeyealnmpipnplwkpgDSMDTLPPPleklsyIVVIVDEFADLMMVAGkqveelIARLAQKA 730
Cdd:cd01127 57 FFNQLFRALTELAS---------------------LSPGRLPRR------VWFILDEFANLGRIPN------LPNLLATG 103
|
170 180 190
....*....|....*....|....*....|....*....
gi 928589029 731 RAVGIHLILATQ------RPSVDVITGLIKANVPSRIAF 763
Cdd:cd01127 104 RKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYL 142
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
422-914 |
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: 848.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 422 KTPLPSLDLLEHRPTREQDITQAEIVETSQRIEQQLRNFNVKAKVKDVLVGPVVTRYELELDPGVKASKVTGLDTDLARA 501
Cdd:COG1674 134 LAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 502 LMFRSIRVAEVIPGKPYIGIETPNDHRQIVPLRDVLDSDEFRNSKALLSMALGKDISGKPMVVDLAKMPHLLVAGTTGSG 581
Cdd:COG1674 214 LAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 582 KSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELSIYNDIPHLLTEVVTDMKKAANALRWCVDEMERRYQLLSALRVRNIE 661
Cdd:COG1674 294 KSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 662 GFNEKVDEYEALNMPipnplwkpgdsmdtlPPPLEKLSYIVVIVDEFADLMMVAGKQVEELIARLAQKARAVGIHLILAT 741
Cdd:COG1674 374 GYNEKVREAKAKGEE---------------EEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILAT 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 742 QRPSVDVITGLIKANVPSRIAFTVATKIDSRTILDAGGAESLLGKGDMLYSPQGSTELVRIHGAFMTDDEVVRVVDDWKA 821
Cdd:COG1674 439 QRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKS 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 822 RGKPNYIDGILEGDEEDAGaerlSERGGETDGLFDEVVEFVVSTGSTSISAIQRRFRVGFNRAANIMDQLEEQGIVSPVQ 901
Cdd:COG1674 519 QGEPEYIEEILEEEEEEDE----GGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAE 594
|
490
....*....|....
gi 928589029 902 -NGKREVLARSADY 914
Cdd:COG1674 595 gSKPREVLVSPEEL 608
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
219-909 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 733.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 219 KTPVQEAVEqptELVNPADRINISGLSKAQDMFYVPMNNGNEVNAFAPENPEfvKYDFEQQETLP-NVSISMQRGQAELS 297
Cdd:PRK10263 626 KLPSQRAAE---EKAREAQRNQYDSGDQYNDDEIDAMQQDELARQFAQTQQQ--RYGEQYQHDVPvNAEDADAAAEAELA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 298 TQHDFTpvwQQTNVFGEE-----------------KSVVDFGSK---FTTS---EDMPNVSLAEPEVNVAEEDP----EQ 350
Cdd:PRK10263 701 RQFAQT---QQQRYSGEQpaganpfslddfefspmKALLDDGPHeplFTPIvepVQQPQQPVAPQQQYQQPQQPvapqPQ 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 351 SELARQFAAQEQQRLREMERRAKDMGVQDVYQQIV-----QGPTAETAPKTANYRPYG-------DSLIHPAFQQH--KK 416
Cdd:PRK10263 778 YQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVApqpqyQQPQQPVAPQPQYQQPQQpvapqpqDTLLHPLLMRNgdSR 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 417 NIEKPKTPLPSLDLLEHRPTREQDITQAEIVETSQRIEQQLRNFNVKAKVKDVLVGPVVTRYELELDPGVKASKVTGLDT 496
Cdd:PRK10263 858 PLHKPTTPLPSLDLLTPPPSEVEPVDTFALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSR 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 497 DLARALMFRSIRVAEVIPGKPYIGIETPNDHRQIVPLRDVLDSDEFRNSKALLSMALGKDISGKPMVVDLAKMPHLLVAG 576
Cdd:PRK10263 938 DLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAG 1017
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 577 TTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELSIYNDIPHLLTEVVTDMKKAANALRWCVDEMERRYQLLSALR 656
Cdd:PRK10263 1018 TTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALG 1097
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 657 VRNIEGFNEKVDEYEALNMPIPNPLWKPGDSMDTLPPPLEKLSYIVVIVDEFADLMMVAGKQVEELIARLAQKARAVGIH 736
Cdd:PRK10263 1098 VRNLAGYNEKIAEADRMMRPIPDPYWKPGDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIH 1177
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 737 LILATQRPSVDVITGLIKANVPSRIAFTVATKIDSRTILDAGGAESLLGKGDMLYSPQGSTELVRIHGAFMTDDEVVRVV 816
Cdd:PRK10263 1178 LVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVV 1257
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 817 DDWKARGKPNYIDGILEGDEEDAGAERLsERGGETDGLFDEVVEFVVSTGSTSISAIQRRFRVGFNRAANIMDQLEEQGI 896
Cdd:PRK10263 1258 QDWKARGRPQYVDGITSDSESEGGAGGF-DGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGI 1336
|
730
....*....|....
gi 928589029 897 VS-PVQNGKREVLA 909
Cdd:PRK10263 1337 VSeQGHNGNREVLA 1350
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
533-745 |
5.34e-92 |
|
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: 290.05 E-value: 5.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 533 LRDVLDSDEFRNSKALLSMALGKDISGKPMVVDLAKMP-HLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKV 611
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 612 VELSIYNDIPHLLT-EVVTDMKKAANALRWCVDEMERRYQLLSALRVRNIEGFNEKVDEYEALNMPIPNPLWKPGDSMDT 690
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 928589029 691 LPPPLEKLSYIVVIVDEFADLMMVAGKQ----VEELIARLAQKARAVGIHLILATQRPS 745
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
425-525 |
1.08e-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: 147.68 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 425 LPSLDLLEHRPTREQDITQAEIVETSQRIEQQLRNFNVKAKVKDVLVGPVVTRYELELDPGVKASKVTGLDTDLARALMF 504
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 928589029 505 RSIRVAEVIPGKPYIGIETPN 525
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
26-182 |
8.92e-28 |
|
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: 110.37 E-value: 8.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 26 FGLYLIIAWSGYTPLDNSWATSGFAPETI-NKAGAFGAWFVDLFFVFFGYIGNLIPFILFFIPIYLIRSKRVENLTWtkf 104
Cdd:pfam13491 15 LGLFLLLALVSYSPADPSWSTSGSGAAPVhNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRRSLERRWL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 105 alRSFGFILLLCGLTVLATLSLNNPASYL---AGGVLGGSLTLNLYPSLGKFGVSLLAVIFAAVGFIFCSGASFIRLLMK 181
Cdd:pfam13491 92 --RLLGFLLLLLASSALFALRLPSLEFGLpggAGGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAER 169
|
.
gi 928589029 182 F 182
Cdd:pfam13491 170 L 170
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
849-910 |
3.71e-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: 104.80 E-value: 3.71e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928589029 849 GETDGLFDEVVEFVVSTGSTSISAIQRRFRVGFNRAANIMDQLEEQGIVSPVQ-NGKREVLAR 910
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANgSKPREVLVT 63
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
849-909 |
1.37e-26 |
|
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: 103.22 E-value: 1.37e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928589029 849 GETDGLFDEVVEFVVSTGSTSISAIQRRFRVGFNRAANIMDQLEEQGIVSPVQ-NGKREVLA 909
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADgSKPREVLI 62
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
570-775 |
4.15e-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: 109.31 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 570 PHLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELS-IYNDIPHLLTeVVT--DMKKAANALRWCVDEME 646
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMAnLFKNLPHLLG-TITnlDGAQSMRALASIKAELK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 647 RRYQLLSALRVRNIEGFNEKVDEYEALnMPIPnplwkpgdsmdtlpppleklsYIVVIVDEFADLMmvagKQVEELIARL 726
Cdd:TIGR03928 549 KRQRLFGENNVNHINQYQKLYKQGKAK-EPMP---------------------HLFLISDEFAELK----SEQPEFMKEL 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 928589029 727 AQKA---RAVGIHLILATQRPSvDVITGLIKANVPSRIAFTVATKIDSRTIL 775
Cdd:TIGR03928 603 VSTArigRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
543-806 |
1.87e-21 |
|
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: 100.05 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 543 RNSKALLSMALGKDISGKPMVVDL---AK--M-PHLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPK------ 610
Cdd:TIGR03924 403 RPGRDRLRVPIGVGDDGEPVELDLkesAEggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatfl 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 611 VVElsiynDIPHlLTEVVTDMKKAAN-------ALRwcvDEMERRYQLLSALrvrnieGFNEKVDEYEALNMpipnplwk 683
Cdd:TIGR03924 483 GLE-----GLPH-VSAVITNLADEAPlvdrmqdALA---GEMNRRQELLRAA------GNFANVAEYEKARA-------- 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 684 PGDSMDTLPppleklsYIVVIVDEFADLMmvaGKQVE--ELIARLAQKARAVGIHLILATQRPSVDVITGLiKANVPSRI 761
Cdd:TIGR03924 540 AGADLPPLP-------ALFVVVDEFSELL---SQHPDfaDLFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRI 608
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 928589029 762 AFTVATKIDSRTILDAGGAESLLGKGDMLYSPQGSTELVRIHGAF 806
Cdd:TIGR03924 609 GLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAY 653
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
561-775 |
2.90e-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: 83.88 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 561 PMVVDLAKMPHLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELSIYNDIPHlLTEVVT--DMKKAANAL 638
Cdd:TIGR03928 802 PLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKLI 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 639 RWCVDEMERRYQLLSALRVRNIEGFNEKVDEyealnmPIPNplwkpgdsmdtlpppleklsyIVVIVDEFADLMMVAGKQ 718
Cdd:TIGR03928 881 RRIKKEIDRRKKLFSEYGVASISMYNKASGE------KLPQ---------------------IVIIIDNYDAVKEEPFYE 933
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 928589029 719 V-EELIARLAQKARAVGIHLIL-ATQRPSVDVItglIKANVPSRIAFTVATKIDSRTIL 775
Cdd:TIGR03928 934 DfEELLIQLAREGASLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIV 989
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
26-456 |
4.22e-12 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 70.50 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 26 FGLYLIIAWSGYTPLDNSWATSGFAPETINKAGAFGAWFVDLFFVFFGYIGNLIPFILFFIPIYLIRSKRVEN-LTWTKF 104
Cdd:PRK10263 33 FAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIVGGCWFAWRHQSSDEyIDYFAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 105 ALRSFG---FILLLCGltvLATLSLNNPASYLAGGVLGGSLTLNLYPSLGKFGVSLLAVIFAAVGFIFCSGASFIRLLMK 181
Cdd:PRK10263 113 SLRIIGvlaLILTSCG---LAAINADDIWYFASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAGLTLFTGWSWVTIAEK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 182 FYRWL----------TMQNPP--EDSEKTDETESEKMHMAEPPE----EIVIGKTPVQEAVEQptELVNPADRINISGLS 245
Cdd:PRK10263 190 LGGWIlniltfasnrTRRDDTwvDEDEYEDDEEYEDENHGKQHEsrraRILRGALARRKRLAE--KFINPMGRQTDAALF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 246 KAQDmfyvpMNNGNEVN------AFAPEN----------PEFVKYD--FEQQETLPNVSISMQRGQAELSTQHDFTPVWQ 307
Cdd:PRK10263 268 SGKR-----MDDDEEITytargvAADPDDvlfsgnratqPEYDEYDplLNGAPITEPVAVAAAATTATQSWAAPVEPVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 308 QTNVFGEEksvVDFGSKFTTSEDMPNVSLAEPEVNVAEED-PEQSELARQFAAQEQ--QRLREMERRAKDMGVQDVYQQI 384
Cdd:PRK10263 343 TPPVASVD---VPPAQPTVAWQPVPGPQTGEPVIAPAPEGyPQQSQYAQPAVQYNEplQQPVQPQQPYYAPAAEQPAQQP 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928589029 385 VQGPTAETAPKTANYRPygdslihpafQQHKKNIEKPKTPLPSLDLLEHRPTRE------QDITQAEIVETSQRIEQQ 456
Cdd:PRK10263 420 YYAPAPEQPAQQPYYAP----------APEQPVAGNAWQAEEQQSTFAPQSTYQteqtyqQPAAQEPLYQQPQPVEQQ 487
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
561-771 |
3.25e-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: 57.31 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 561 PMVVDLAKMP-HLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMIDPKVVELSIYNDIPHlLTEVVTdmKKAANALR 639
Cdd:TIGR03925 70 PLVVDLSGAAgHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAG--RLDPERVR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 640 WCVDEME----RRYQLLSALRVRNIEGFNEKVDEYEALNMPIpnplwkpGDsmdtlpppleklsyIVVIVD-------EF 708
Cdd:TIGR03925 147 RTVAEVEgllrRRERLFRTHGIDSMAQYRARRAAGRLPEDPF-------GD--------------VFLVIDgwgtlrqDF 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928589029 709 ADLmmvagkqvEELIARLAQKARAVGIHLILATQRPSvdVITGLIKANVPSRIAFTVATKIDS 771
Cdd:TIGR03925 206 EDL--------EDKVTDLAARGLAYGVHVVLTASRWS--EIRPALRDLIGTRIELRLGDPMDS 258
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
529-740 |
7.69e-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: 56.15 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 529 QIVPLRDVLDSDEFRNskalLSMALGKDISG-KPMVVDLAKMPHLLVAGTTGSGKSVGVNTMILSLLYRVKPEEVKFIMI 607
Cdd:TIGR03925 326 ARLPLSALPAGGGAPR----LRVPLGLGESDlAPVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 608 DPKvveLSIYNDIP--HLLTEVVT--DMKKAANALrwcVDEMERRyqllsalrvrniegfnekvdeyealnMPIPnplwk 683
Cdd:TIGR03925 402 DYR---RTLLGAVPedYLAGYAATsaALTELIAAL---AALLERR--------------------------LPGP----- 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928589029 684 pgdsmDTLPPPLEKLSY-----IVVIVDEFADLMMVAGKQVEELIARLAQkARAVGIHLILA 740
Cdd:TIGR03925 445 -----DVTPQQLRARSWwsgpeIYVVVDDYDLVATGSGNPLAPLVELLPH-ARDIGLHVVVA 500
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
530-774 |
2.06e-07 |
|
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: 54.99 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 530 IVPlrDVLDSDEFRNSKAL------LSMALGKDISG-KPMVVDLAKMPHLLVAGTTGSGKSVGVNTMILSLLYRvkpEEV 602
Cdd:TIGR03928 1052 MVP--EELSLEEFRERYEVrkileeGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKE 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 603 KFIMIDPKVVELSIYNDIPHLLTEVVTdmkkaANALRWCVDEMerryqllsalrvrnIEGFNEKVDEY-EALNMPIPNPL 681
Cdd:TIGR03928 1127 KIGLIDSIDRGLLAYRDLKEVATYIEE-----KEDLKEILAEL--------------KEEIELREAAYkEALQNETGEPA 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 682 WKPgdsmdtlpppleklsyIVVIVDEFADLMMVAGKQVEELIARLAQKARAVGIHLILATQRPSV----DVITGLIKAnv 757
Cdd:TIGR03928 1188 FKP----------------ILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ-- 1249
|
250
....*....|....*..
gi 928589029 758 pSRIAFTVATKIDSRTI 774
Cdd:TIGR03928 1250 -LRTGILGMRKSDQSFF 1265
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
571-763 |
3.59e-06 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 47.60 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 571 HLLVAGTTGSGKSVGVNTMILSLLyrvkPEEVKFIMIDPKvVELSIyndiphllteVVTDMKKAANALrwcvdemerRYQ 650
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQA----ARGGSVIITDPK-GELFL----------VIPDRDDSFAAL---------RAL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 651 LLSALRVRNIEGFNekvdeyealnmpipnplwkpgDSMDTLPPPleklsyIVVIVDEFADLMMVAGkqveelIARLAQKA 730
Cdd:cd01127 57 FFNQLFRALTELAS---------------------LSPGRLPRR------VWFILDEFANLGRIPN------LPNLLATG 103
|
170 180 190
....*....|....*....|....*....|....*....
gi 928589029 731 RAVGIHLILATQ------RPSVDVITGLIKANVPSRIAF 763
Cdd:cd01127 104 RKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYL 142
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
550-610 |
1.40e-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: 48.45 E-value: 1.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 928589029 550 SMALGKDIS-GKPMVVDLAKM--PHLLVAGTTGSGKSVGVNTMILSLLyrvkPEEVKFIMIDPK 610
Cdd:COG0433 25 GILIGKLLSpGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELS----RAGVPVLVFDPH 84
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
553-609 |
4.96e-05 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 46.86 E-value: 4.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 928589029 553 LGKDISGKPMVVDLAKM---PHLLVAGTTGSGKSVGVNTMILSLLYRvkpeEVKFIMIDP 609
Cdd:COG3451 185 LLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| |
