|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
243-762 |
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: 918.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 243 PTTPPKVAAKAKQKPLFDDIPTGPMPVMELLDEPEPPKNHFSEEALEAMSRLVELKLKDFGVEAQVMEVHPGPVITRFEI 322
Cdd:COG1674 113 LAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 323 ELAPGVKVSKISNLAKDLARSLSTISVRVVEVIPGKTYVGIEIPNESREVVRLREVLACDEFEKSKSPLSMALGKDIAGN 402
Cdd:COG1674 193 EPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 403 PIVVNMAKMPHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPKMLELSVYEGIPHLLCEVVTDMKDAANALRW 482
Cdd:COG1674 273 PVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKW 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 483 SVGEMERRYRLMSAMGVRNLAGFNKKVQDAIKAGepikdplwqptdgleEEPPTLEKLPSIVIVIDELADMMMIVGKKVE 562
Cdd:COG1674 353 AVREMERRYKLFAKAGVRNIAGYNEKVREAKAKG---------------EEEEGLEPLPYIVVIIDELADLMMVAGKEVE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 563 ELIARIAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFQVSSKIDSRTILDQMGAEQLLGMGDMLYLPGGSNIPT 642
Cdd:COG1674 418 EAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPI 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 643 RIHGAFVDDDEVHRVVEDWKKRGEPEYLDEVISGTSEvpvpgipgMEGDGGDSEQDELFDQAVAIVTETRRASISGIQRR 722
Cdd:COG1674 498 RVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEE--------EDEGGDDDEDDELFDEAVELVVETQKASTSLLQRR 569
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2772083734 723 LKIGYNRAARMVEAMEAAGIVSEMGSNGAREVLAPPPPKD 762
Cdd:COG1674 570 LRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELE 609
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
218-759 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 805.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 218 QEALKQDKVKRETRSPVKIEPKVHQPTTPPkvaAKAKQKPLFDDI------------PTGPMPVMELLDEPEPPKNHFSE 285
Cdd:PRK10263 808 QQPVAPQPQYQQPQQPVAPQPQYQQPQQPV---APQPQDTLLHPLlmrngdsrplhkPTTPLPSLDLLTPPPSEVEPVDT 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 286 EALEAMSRLVELKLKDFGVEAQVMEVHPGPVITRFEIELAPGVKVSKISNLAKDLARSLSTISVRVVEVIPGKTYVGIEI 365
Cdd:PRK10263 885 FALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLEL 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 366 PNESREVVRLREVLACDEFEKSKSPLSMALGKDIAGNPIVVNMAKMPHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLR 445
Cdd:PRK10263 965 PNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVR 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 446 LIMIDPKMLELSVYEGIPHLLCEVVTDMKDAANALRWSVGEMERRYRLMSAMGVRNLAGFNKKVQDAIKAGEPIKDPLWQ 525
Cdd:PRK10263 1045 FIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEADRMMRPIPDPYWK 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 526 PTDGLEEEPPTLEKLPSIVIVIDELADMMMIVGKKVEELIARIAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAF 605
Cdd:PRK10263 1125 PGDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAF 1204
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 606 QVSSKIDSRTILDQMGAEQLLGMGDMLYLPGGSNIPTRIHGAFVDDDEVHRVVEDWKKRGEPEYLDEVisgTSEVPVPGi 685
Cdd:PRK10263 1205 TVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGI---TSDSESEG- 1280
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2772083734 686 pGMEGDGGDSEQDELFDQAVAIVTETRRASISGIQRRLKIGYNRAARMVEAMEAAGIVSEMGSNGAREVLAPPP 759
Cdd:PRK10263 1281 -GAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPPP 1353
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
375-587 |
9.12e-80 |
|
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: 254.61 E-value: 9.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 375 LREVLACDEFEKSKSPLSMALGKDIAGNPIVVNMAKMP-HLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPKM 453
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 454 LELSVYEGIPHLL-CEVVTDMKDAANALRWSVGEMERRYRLMSAMGVRNLAGFNKKVQDAIKAGEPIKDPLWQPTDGLEE 532
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2772083734 533 EPPTLEKLPSIVIVIDELADMMMIVGKK----VEELIARIAQKARAAGIHLILATQRPS 587
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
8-183 |
1.43e-39 |
|
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: 143.88 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 8 RKRLSEGGMILLVTLALFFFLALLTYNPNDPGSFTNGSG-APVQNSAGKGGAWFADFFLHLFGYLAFLIPVIFAYSGYLL 86
Cdd:pfam13491 1 ERLLRELLGLALLLLGLFLLLALVSYSPADPSWSTSGSGaAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 87 YVERNIEHehpkafWAVKGLGLLMAVVGGAGLCSLHFFDPAIQPSYTSGGILGEFIISLVIDGLGLYGTTLILLALFLSG 166
Cdd:pfam13491 81 FRRRSLER------RWLRLLGFLLLLLASSALFALRLPSLEFGLPGGAGGVIGRLLANALVTLLGFTGATLLLLALLAIG 154
|
170
....*....|....*..
gi 2772083734 167 LTLFTGISWLRMMDRVG 183
Cdd:pfam13491 155 LSLVTGFSWLALAERLG 171
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
695-757 |
7.74e-31 |
|
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: 114.82 E-value: 7.74e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2772083734 695 SEQDELFDQAVAIVTETRRASISGIQRRLKIGYNRAARMVEAMEAAGIVSEMGSNGAREVLAP 757
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
412-652 |
2.80e-22 |
|
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: 101.97 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 412 PHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPK----MLELsvyEGIPHlLCEVVTDMKDAAN-------AL 480
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---EGLPH-VSAVITNLADEAPlvdrmqdAL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 481 RwsvGEMERRYRLMSAMG-VRNLAGFNKkvqdAIKAGEPikdplwqptdgleeepptLEKLPSIVIVIDELADMMmivGK 559
Cdd:TIGR03924 512 A---GEMNRRQELLRAAGnFANVAEYEK----ARAAGAD------------------LPPLPALFVVVDEFSELL---SQ 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 560 KVE--ELIARIAQKARAAGIHLILATQRPSVDVITGLiKANIPSRIAFQVSSKIDSRTILDQMGAEQL---LGMGdmlYL 634
Cdd:TIGR03924 564 HPDfaDLFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLpstPGAG---YL 639
|
250
....*....|....*...
gi 2772083734 635 PGGSNIPTRIHGAFVDDD 652
Cdd:TIGR03924 640 KVDTAEPVRFRAAYVSGP 657
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
9-187 |
2.42e-18 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 90.14 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 9 KRLSEGGMILLVTLALFFFLALLTYNPNDPGSFTNGSGAPVQNSAGKGGAWFADFFLHLFGYLAFLIPVIFAysGYLLYV 88
Cdd:PRK10263 20 RRLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIV--GGCWFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 89 ERNIEHEHPKAFWAV--KGLGLLMAVVGGAGLCSLHFFDPAIqpsYTSGGILGEFIISLVIDGLGLYGTTLILLALFLSG 166
Cdd:PRK10263 98 WRHQSSDEYIDYFAVslRIIGVLALILTSCGLAAINADDIWY---FASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAG 174
|
170 180
....*....|....*....|.
gi 2772083734 167 LTLFTGISWLRMMDRVGVWVV 187
Cdd:PRK10263 175 LTLFTGWSWVTIAEKLGGWIL 195
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
413-607 |
1.56e-08 |
|
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: 54.15 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 413 HLLVAGTTGSGKSVGVNAMIISMLYKATpedlRLIMIDPKMlELSVyegiphllceVVTDMKDAANALRwsvgemerryR 492
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKG-ELFL----------VIPDRDDSFAALR----------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 493 LMSAMgvrnLAGFNKKVQDAIKAGEPIKdplwqptdgleeepptleklpsIVIVIDELADMMMIVGkkveelIARIAQKA 572
Cdd:cd01127 56 LFFNQ----LFRALTELASLSPGRLPRR----------------------VWFILDEFANLGRIPN------LPNLLATG 103
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2772083734 573 RAAGIHLILATQ------RPSVDVITGLIKANIPSRIAFQV 607
Cdd:cd01127 104 RKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
243-762 |
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: 918.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 243 PTTPPKVAAKAKQKPLFDDIPTGPMPVMELLDEPEPPKNHFSEEALEAMSRLVELKLKDFGVEAQVMEVHPGPVITRFEI 322
Cdd:COG1674 113 LAAAALGALALLLLAAAEALALAVLPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 323 ELAPGVKVSKISNLAKDLARSLSTISVRVVEVIPGKTYVGIEIPNESREVVRLREVLACDEFEKSKSPLSMALGKDIAGN 402
Cdd:COG1674 193 EPAPGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 403 PIVVNMAKMPHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPKMLELSVYEGIPHLLCEVVTDMKDAANALRW 482
Cdd:COG1674 273 PVVADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKW 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 483 SVGEMERRYRLMSAMGVRNLAGFNKKVQDAIKAGepikdplwqptdgleEEPPTLEKLPSIVIVIDELADMMMIVGKKVE 562
Cdd:COG1674 353 AVREMERRYKLFAKAGVRNIAGYNEKVREAKAKG---------------EEEEGLEPLPYIVVIIDELADLMMVAGKEVE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 563 ELIARIAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFQVSSKIDSRTILDQMGAEQLLGMGDMLYLPGGSNIPT 642
Cdd:COG1674 418 EAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPI 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 643 RIHGAFVDDDEVHRVVEDWKKRGEPEYLDEVISGTSEvpvpgipgMEGDGGDSEQDELFDQAVAIVTETRRASISGIQRR 722
Cdd:COG1674 498 RVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEE--------EDEGGDDDEDDELFDEAVELVVETQKASTSLLQRR 569
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2772083734 723 LKIGYNRAARMVEAMEAAGIVSEMGSNGAREVLAPPPPKD 762
Cdd:COG1674 570 LRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELE 609
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
218-759 |
0e+00 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 805.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 218 QEALKQDKVKRETRSPVKIEPKVHQPTTPPkvaAKAKQKPLFDDI------------PTGPMPVMELLDEPEPPKNHFSE 285
Cdd:PRK10263 808 QQPVAPQPQYQQPQQPVAPQPQYQQPQQPV---APQPQDTLLHPLlmrngdsrplhkPTTPLPSLDLLTPPPSEVEPVDT 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 286 EALEAMSRLVELKLKDFGVEAQVMEVHPGPVITRFEIELAPGVKVSKISNLAKDLARSLSTISVRVVEVIPGKTYVGIEI 365
Cdd:PRK10263 885 FALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLEL 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 366 PNESREVVRLREVLACDEFEKSKSPLSMALGKDIAGNPIVVNMAKMPHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLR 445
Cdd:PRK10263 965 PNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVR 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 446 LIMIDPKMLELSVYEGIPHLLCEVVTDMKDAANALRWSVGEMERRYRLMSAMGVRNLAGFNKKVQDAIKAGEPIKDPLWQ 525
Cdd:PRK10263 1045 FIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEADRMMRPIPDPYWK 1124
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 526 PTDGLEEEPPTLEKLPSIVIVIDELADMMMIVGKKVEELIARIAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAF 605
Cdd:PRK10263 1125 PGDSMDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAF 1204
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 606 QVSSKIDSRTILDQMGAEQLLGMGDMLYLPGGSNIPTRIHGAFVDDDEVHRVVEDWKKRGEPEYLDEVisgTSEVPVPGi 685
Cdd:PRK10263 1205 TVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGI---TSDSESEG- 1280
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2772083734 686 pGMEGDGGDSEQDELFDQAVAIVTETRRASISGIQRRLKIGYNRAARMVEAMEAAGIVSEMGSNGAREVLAPPP 759
Cdd:PRK10263 1281 -GAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPPP 1353
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
375-587 |
9.12e-80 |
|
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: 254.61 E-value: 9.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 375 LREVLACDEFEKSKSPLSMALGKDIAGNPIVVNMAKMP-HLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPKM 453
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 454 LELSVYEGIPHLL-CEVVTDMKDAANALRWSVGEMERRYRLMSAMGVRNLAGFNKKVQDAIKAGEPIKDPLWQPTDGLEE 532
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVHVMCT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2772083734 533 EPPTLEKLPSIVIVIDELADMMMIVGKK----VEELIARIAQKARAAGIHLILATQRPS 587
Cdd:pfam01580 161 AGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
267-367 |
5.48e-42 |
|
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: 148.07 E-value: 5.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 267 MPVMELLDEPEPPKNHFSEEALEAMSRLVELKLKDFGVEAQVMEVHPGPVITRFEIELAPGVKVSKISNLAKDLARSLST 346
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 2772083734 347 ISVRVVEVIPGKTYVGIEIPN 367
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
8-183 |
1.43e-39 |
|
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: 143.88 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 8 RKRLSEGGMILLVTLALFFFLALLTYNPNDPGSFTNGSG-APVQNSAGKGGAWFADFFLHLFGYLAFLIPVIFAYSGYLL 86
Cdd:pfam13491 1 ERLLRELLGLALLLLGLFLLLALVSYSPADPSWSTSGSGaAPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 87 YVERNIEHehpkafWAVKGLGLLMAVVGGAGLCSLHFFDPAIQPSYTSGGILGEFIISLVIDGLGLYGTTLILLALFLSG 166
Cdd:pfam13491 81 FRRRSLER------RWLRLLGFLLLLLASSALFALRLPSLEFGLPGGAGGVIGRLLANALVTLLGFTGATLLLLALLAIG 154
|
170
....*....|....*..
gi 2772083734 167 LTLFTGISWLRMMDRVG 183
Cdd:pfam13491 155 LSLVTGFSWLALAERLG 171
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
695-757 |
7.74e-31 |
|
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: 114.82 E-value: 7.74e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2772083734 695 SEQDELFDQAVAIVTETRRASISGIQRRLKIGYNRAARMVEAMEAAGIVSEMGSNGAREVLAP 757
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
695-757 |
2.49e-30 |
|
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: 113.62 E-value: 2.49e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2772083734 695 SEQDELFDQAVAIVTETRRASISGIQRRLKIGYNRAARMVEAMEAAGIVSEMGSNGAREVLAP 757
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
412-652 |
2.80e-22 |
|
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: 101.97 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 412 PHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPK----MLELsvyEGIPHlLCEVVTDMKDAAN-------AL 480
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---EGLPH-VSAVITNLADEAPlvdrmqdAL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 481 RwsvGEMERRYRLMSAMG-VRNLAGFNKkvqdAIKAGEPikdplwqptdgleeepptLEKLPSIVIVIDELADMMmivGK 559
Cdd:TIGR03924 512 A---GEMNRRQELLRAAGnFANVAEYEK----ARAAGAD------------------LPPLPALFVVVDEFSELL---SQ 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 560 KVE--ELIARIAQKARAAGIHLILATQRPSVDVITGLiKANIPSRIAFQVSSKIDSRTILDQMGAEQL---LGMGdmlYL 634
Cdd:TIGR03924 564 HPDfaDLFVAIGRLGRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHLpstPGAG---YL 639
|
250
....*....|....*...
gi 2772083734 635 PGGSNIPTRIHGAFVDDD 652
Cdd:TIGR03924 640 KVDTAEPVRFRAAYVSGP 657
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
412-617 |
5.73e-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: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 412 PHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPK---MLELsvYEGIPHLLcEVVTDMkDAANALRWSV---G 485
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLL-GTITNL-DGAQSMRALAsikA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 486 EMERRYRLMSAMGVRNLAGFNKKvqdaIKAGEPikdplwqptdgleEEPptlekLPSIVIVIDELADMmmivgkKVE--- 562
Cdd:TIGR03928 546 ELKKRQRLFGENNVNHINQYQKL----YKQGKA-------------KEP-----MPHLFLISDEFAEL------KSEqpe 597
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 563 ---ELI--ARIaqkARAAGIHLILATQRPSvDVITGLIKANIPSRIAFQVSSKIDSRTIL 617
Cdd:TIGR03928 598 fmkELVstARI---GRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
9-187 |
2.42e-18 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 90.14 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 9 KRLSEGGMILLVTLALFFFLALLTYNPNDPGSFTNGSGAPVQNSAGKGGAWFADFFLHLFGYLAFLIPVIFAysGYLLYV 88
Cdd:PRK10263 20 RRLLEALLILIVLFAVWLMAALLSFNPSDPSWSQTAWHEPIHNLGGMPGAWLADTLFFIFGVMAYTIPVIIV--GGCWFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 89 ERNIEHEHPKAFWAV--KGLGLLMAVVGGAGLCSLHFFDPAIqpsYTSGGILGEFIISLVIDGLGLYGTTLILLALFLSG 166
Cdd:PRK10263 98 WRHQSSDEYIDYFAVslRIIGVLALILTSCGLAAINADDIWY---FASGGVIGSLLSTTLQPLLHSSGGTIALLCVWAAG 174
|
170 180
....*....|....*....|.
gi 2772083734 167 LTLFTGISWLRMMDRVGVWVV 187
Cdd:PRK10263 175 LTLFTGWSWVTIAEKLGGWIL 195
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
382-617 |
8.99e-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: 75.41 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 382 DEFEKSKSPLSMALG-KDIAGN----PIVVNMAKMPHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPKMLEL 456
Cdd:TIGR03928 776 KLWSKPKEPLQATIGlLDDPELqsqePLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGL 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 457 SVYEGIPHlLCEVVT--DMKDAANALRWSVGEMERRYRLMSAMGVRNLAGFNKKVQdaikagepikdplwqptdgleeep 534
Cdd:TIGR03928 856 LPLKKLPH-VADYFTldEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKASG------------------------ 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 535 ptlEKLPSIVIVIDELadmmMIVGK-----KVEELIARIAQKARAAGIHLIL-ATQRPSVDVItglIKANIPSRIAFQVS 608
Cdd:TIGR03928 911 ---EKLPQIVIIIDNY----DAVKEepfyeDFEELLIQLAREGASLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLI 980
|
....*....
gi 2772083734 609 SKIDSRTIL 617
Cdd:TIGR03928 981 DKSEYRSIV 989
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
413-607 |
1.56e-08 |
|
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: 54.15 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 413 HLLVAGTTGSGKSVGVNAMIISMLYKATpedlRLIMIDPKMlELSVyegiphllceVVTDMKDAANALRwsvgemerryR 492
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGG----SVIITDPKG-ELFL----------VIPDRDDSFAALR----------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 493 LMSAMgvrnLAGFNKKVQDAIKAGEPIKdplwqptdgleeepptleklpsIVIVIDELADMMMIVGkkveelIARIAQKA 572
Cdd:cd01127 56 LFFNQ----LFRALTELASLSPGRLPRR----------------------VWFILDEFANLGRIPN------LPNLLATG 103
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2772083734 573 RAAGIHLILATQ------RPSVDVITGLIKANIPSRIAFQV 607
Cdd:cd01127 104 RKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
392-645 |
2.06e-07 |
|
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: 53.84 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 392 SMALGKDIAGN-PIVVNMAKM--PHLLVAGTTGSGKSVGVnAMIISMLYKA----------------------------- 439
Cdd:COG0433 25 GILIGKLLSPGvPVYLDLDKLlnRHILILGATGSGKSNTL-QVLLEELSRAgvpvlvfdphgeysglaepgaeradvgvf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 440 TPEDLRLIMIDPKMLELSVYEGIPHLLC-------------EVVTDMKDAANA------LRWSVGEMERRYRLMSAMGVR 500
Cdd:COG0433 104 DPGAGRPLPINPWDLFATASELGPLLLSrldlndtqrgvlrEALRLADDKGLLlldlkdLIALLEEGEELGEEYGNVSAA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 501 NLAGFNKKVQDAIKAGEPIKDPLWQPTDGLEEEPPT----LEKLPS------------------------------IVIV 546
Cdd:COG0433 184 SAGALLRRLESLESADGLFGEPGLDLEDLLRTDGRVtvidLSGLPEelqstfvlwllrelfearpevgdaddrklpLVLV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 547 IDELADMMMIVGKKVEELIARIAQKARAAGIHLILATQRPSvDVITGlIKANIPSRIAFQVSSKIDSRTI---LDQMGAE 623
Cdd:COG0433 264 IDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLFNPRDQKAVkaaAETLSED 341
|
330 340
....*....|....*....|....*..
gi 2772083734 624 QL-----LGMGDMLYLPGGSNIPTRIH 645
Cdd:COG0433 342 LLerlpsLGTGEALVLGEGIPLPVLVK 368
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
389-451 |
8.52e-06 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 49.18 E-value: 8.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2772083734 389 SPLSMALGKDIAGNPIVVNMAKM---PHLLVAGTTGSGKSVGVNAMIISMLYKatpeDLRLIMIDP 451
Cdd:COG3451 179 DPWGIYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDP 240
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
403-452 |
1.47e-03 |
|
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: 41.90 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2772083734 403 PIVVNMAKMPHLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPK 452
Cdd:TIGR03925 355 PVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR 404
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
413-614 |
1.67e-03 |
|
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: 41.90 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 413 HLLVAGTTGSGKSVGVNAMIISMLYKATPEDLRLIMIDPKMLELSVYEGIPHllceV--VTDMKDAANALRwSVGEME-- 488
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH----VggVAGRLDPERVRR-TVAEVEgl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2772083734 489 --RRYRLMSAMGVRNLAGFnkkvQDAIKAGEPIKDPLwqpTDgleeepptleklpsIVIVIDELADMmmiVGK--KVEEL 564
Cdd:TIGR03925 156 lrRRERLFRTHGIDSMAQY----RARRAAGRLPEDPF---GD--------------VFLVIDGWGTL---RQDfeDLEDK 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2772083734 565 IARIAQKARAAGIHLILATQRPSvdVITGLIKANIPSRIAFQ----VSSKIDSR 614
Cdd:TIGR03925 212 VTDLAARGLAYGVHVVLTASRWS--EIRPALRDLIGTRIELRlgdpMDSEIDRR 263
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
413-452 |
2.56e-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: 40.74 E-value: 2.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2772083734 413 HLLVAGTTGSGKSVGVnamIISMLYKATPEDlRLIMIDPK 452
Cdd:COG3505 1 HVLVIGPTGSGKTVGL---VIPNLTQLARGE-SVVVTDPK 36
|
|
| |
