|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
557-1078 |
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: 877.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 557 GRAPAQRSLVSAYNAPFELPSVEFLTQPKPRgrDSTLSPEVLQENARLLEGVLEDFGVKGEIIEVRPGPVVTLYELEPAP 636
Cdd:COG1674 119 GALALLLLAAAEALALAVLPPLDLLDPPPPK--KEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 637 GIKSSRVIGLADDIARSMSAIAARV-AVIPGKNAIGIELPNQRRETVYLREIMAAESFAQNKGKLALTLGKTIGGEPVIA 715
Cdd:COG1674 197 GVKVSKITNLADDIALALAAKSVRIeAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 716 DLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPKMLELSIYDGIPHLLTPVVTDPKKAVVALKWAVRE 795
Cdd:COG1674 277 DLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVRE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 796 MEDRYRKMSKVGVRNIDGFNERVASAIERGEtisrtvqtgfdretgepvfetEEFDLQPLPYIVVLIDEMADLMMVAGKD 875
Cdd:COG1674 357 MERRYKLFAKAGVRNIAGYNEKVREAKAKGE---------------------EEEGLEPLPYIVVIIDELADLMMVAGKE 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 876 IEGTVQRLAQMARAAGIHVIMATQRPSVDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGQGDMLFMA-GGGR 954
Cdd:COG1674 416 VEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPpGASK 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 955 IQRVHGPFVGDNEVEAIVNHLKAQGVPDYLDAILVDEDEEADapaaggkngggaSGDVDEGADLYDQAVAVVLRDGKAST 1034
Cdd:COG1674 496 PIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDE------------GGDDDEDDELFDEAVELVVETQKAST 563
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2392095750 1035 SYVQRRLGIGYNRAASIIERMEKEGIVGPANHAGKREILVPTEE 1078
Cdd:COG1674 564 SLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEE 607
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
245-1075 |
1.50e-175 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 550.84 E-value: 1.50e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 245 DSWEPEEEVSaDTRfaPPKPP---------RAAQHRDIRVA--EPYAAPASAYVDPLDGFEAEDEADFPPAYAAPAV--- 310
Cdd:PRK10263 488 PVVEPEPVVE-ETK--PARPPlyyfeeveeKRAREREQLAAwyQPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVspl 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 311 -----QPHHAAPAASAFRAP-----------------------------------LARAPMSVPAQTAAVSAAFVAPAAR 350
Cdd:PRK10263 565 asgvkKATLATGAAATVAAPvfslansggprpqvkegigpqlprpkrirvptrreLASYGIKLPSQRAAEEKAREAQRNQ 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 351 REpSFAEPAAAPGAAFTADDWSRGAALAAQADWSDEAEADAQIQARAaeapfaqdpyDDGAAEAE--RAFEGHEAYEAYE 428
Cdd:PRK10263 645 YD-SGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAED----------ADAAAEAElaRQFAQTQQQRYSG 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 429 DQEAGrAAPVAYDDYEEAREEEAEADfvlEASDRVVAAGGGVQAEPAAVGGWRGLLQNNIVAFPGRKEKGAAPEPAMRAA 508
Cdd:PRK10263 714 EQPAG-ANPFSLDDFEFSPMKALLDD---GPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQP 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 509 QGPAAPRMPAAPAAQAGHATAVRPAAPPMAPAAASTVSAEQQRLRTGSGRAPaQRSLV------SAYNAPFE-----LPS 577
Cdd:PRK10263 790 QYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQP-QDTLLhpllmrNGDSRPLHkpttpLPS 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 578 VEFLTQPKprgrdSTLSPE---VLQENARLLEGVLEDFGVKGEIIEVRPGPVVTLYELEPAPGIKSSRVIGLADDIARSM 654
Cdd:PRK10263 869 LDLLTPPP-----SEVEPVdtfALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 655 SAIAARVA-VIPGKNAIGIELPNQRRETVYLREIMAAESFAQNKGKLALTLGKTIGGEPVIADLAKMPHLLVAGTTGSGK 733
Cdd:PRK10263 944 STVAVRVVeVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGK 1023
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 734 SVAINTMILSLLYRMTPAQCRLIMIDPKMLELSIYDGIPHLLTPVVTDPKKAVVALKWAVREMEDRYRKMSKVGVRNIDG 813
Cdd:PRK10263 1024 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAG 1103
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 814 FNERVASAIERGETISRTV-QTGFDRETGEPVfeteefdLQPLPYIVVLIDEMADLMMVAGKDIEGTVQRLAQMARAAGI 892
Cdd:PRK10263 1104 YNEKIAEADRMMRPIPDPYwKPGDSMDAQHPV-------LKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGI 1176
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 893 HVIMATQRPSVDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGQGDMLFMAGGGRIQ-RVHGPFVGDNEVEAI 971
Cdd:PRK10263 1177 HLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPvRVHGAFVRDQEVHAV 1256
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 972 VNHLKAQGVPDYLDAILVDEDEEAdapaaggkngGGASGDVDEGAD-LYDQAVAVVLRDGKASTSYVQRRLGIGYNRAAS 1050
Cdd:PRK10263 1257 VQDWKARGRPQYVDGITSDSESEG----------GAGGFDGAEELDpLFDQAVQFVTEKRKASISGVQRQFRIGYNRAAR 1326
|
890 900
....*....|....*....|....*
gi 2392095750 1051 IIERMEKEGIVGPANHAGKREILVP 1075
Cdd:PRK10263 1327 IIEQMEAQGIVSEQGHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
684-902 |
4.75e-66 |
|
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: 221.87 E-value: 4.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 684 LREIMAAESFAQNKGKLALTLGKTIGGEPVIADLAKMP-HLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPKM 762
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 763 LELSIYDGIPHLLT-PVVTDPKKAVVALKWAVREMEDRYRKMSKVGVRNIDGFNERVASAIERGETISRTVQTGFDretg 841
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVH---- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2392095750 842 epVFETEEFDLQPLPYIVVLIDEMADLMMVAGKD----IEGTVQRLAQMARAAGIHVIMATQRPS 902
Cdd:pfam01580 157 --VMCTAGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1013-1075 |
3.47e-29 |
|
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: 110.58 E-value: 3.47e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2392095750 1013 DEGADLYDQAVAVVLRDGKASTSYVQRRLGIGYNRAASIIERMEKEGIVGPANHAGKREILVP 1075
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
17-176 |
9.30e-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: 110.75 E-value: 9.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 17 RRQGEvAGGVALAGLAAWLGVALATWTVSDPSFSHANSN--EVQNWAGQAGASAADLLMQLFGMGAVLLVALPVIWAAFL 94
Cdd:pfam13491 2 RLLRE-LLGLALLLLGLFLLLALVSYSPADPSWSTSGSGaaPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 95 FFGRPaegIWRRAWFALGGTVLFSAVAGCIDL---PAGWPLPIGLGGIAGDVVLKLPAALLGDFPSGLfayVLAAVIAVP 171
Cdd:pfam13491 81 FRRRS---LERRWLRLLGFLLLLLASSALFALrlpSLEFGLPGGAGGVIGRLLANALVTLLGFTGATL---LLLALLAIG 154
|
....*
gi 2392095750 172 ATWLF 176
Cdd:pfam13491 155 LSLVT 159
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
700-968 |
1.70e-18 |
|
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: 91.59 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 700 LALTLGKTIGGEPVIADL---AKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPK---MLELsiYDGIPH 773
Cdd:TIGR03928 446 LAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPH 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 774 LLTpVVTD-----PKKAVVALKwavREMEDRYRKMSKVGVRNIDGFnervasaiergetisrtvQTGFDRETGEpvfete 848
Cdd:TIGR03928 524 LLG-TITNldgaqSMRALASIK---AELKKRQRLFGENNVNHINQY------------------QKLYKQGKAK------ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 849 efdlQPLPYIVVLIDEMADL------MMvagKDIEGTvqrlAQMARAAGIHVIMATQRPSvDVITGTIKANFPTRISFQV 922
Cdd:TIGR03928 576 ----EPMPHLFLISDEFAELkseqpeFM---KELVST----ARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKV 643
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2392095750 923 TSKIDSRTILGEQGAEQLLgqgdmlfMAGGGRIQrvhgpfVGDNEV 968
Cdd:TIGR03928 644 QDASDSNEILKTPDAAEIT-------VPGRAYLQ------VGNNEV 676
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
722-922 |
1.73e-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: 48.75 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 722 HLLVAGTTGSGKSVAINTMILsllyRMTPAQCRLIMIDPKM---LELSIYDGIPHLLTPVVTDpkkavvALKWAVREMED 798
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLL----DQAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 799 RYRKMskvgvrnidgFNERVasaiergetisrtvqtgfdretgepvfeteefdlqplpyiVVLIDEMAdlMMVAGKDIEg 878
Cdd:cd01127 71 LSPGR----------LPRRV----------------------------------------WFILDEFA--NLGRIPNLP- 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2392095750 879 tvqRLAQMARAAGIHVIMATQ------RPSVDVITGTIKANFPTRISFQV 922
Cdd:cd01127 98 ---NLLATGRKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
260-439 |
9.80e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.38 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 260 APPKPPRAAQHRDIRVAEPYAAPASAYVDPLDGFEAEDEADFPPAYAAPAVQPHHAAPAASAFRAPLARAPMSVPAQTAA 339
Cdd:PRK07003 372 VPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 340 VSAAFVAPAARREPSFAEPAAAPGAAFTADDWSRGAALAAQADWSDEAEADAQIQARAAEAPFAQDPYDDGAAEAERAFE 419
Cdd:PRK07003 452 KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPE 531
|
170 180
....*....|....*....|
gi 2392095750 420 GHEAYEAyEDQEAGRAAPVA 439
Cdd:PRK07003 532 ARPPTPA-AAAPAARAGGAA 550
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
557-1078 |
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: 877.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 557 GRAPAQRSLVSAYNAPFELPSVEFLTQPKPRgrDSTLSPEVLQENARLLEGVLEDFGVKGEIIEVRPGPVVTLYELEPAP 636
Cdd:COG1674 119 GALALLLLAAAEALALAVLPPLDLLDPPPPK--KEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 637 GIKSSRVIGLADDIARSMSAIAARV-AVIPGKNAIGIELPNQRRETVYLREIMAAESFAQNKGKLALTLGKTIGGEPVIA 715
Cdd:COG1674 197 GVKVSKITNLADDIALALAAKSVRIeAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 716 DLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPKMLELSIYDGIPHLLTPVVTDPKKAVVALKWAVRE 795
Cdd:COG1674 277 DLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVRE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 796 MEDRYRKMSKVGVRNIDGFNERVASAIERGEtisrtvqtgfdretgepvfetEEFDLQPLPYIVVLIDEMADLMMVAGKD 875
Cdd:COG1674 357 MERRYKLFAKAGVRNIAGYNEKVREAKAKGE---------------------EEEGLEPLPYIVVIIDELADLMMVAGKE 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 876 IEGTVQRLAQMARAAGIHVIMATQRPSVDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGQGDMLFMA-GGGR 954
Cdd:COG1674 416 VEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPpGASK 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 955 IQRVHGPFVGDNEVEAIVNHLKAQGVPDYLDAILVDEDEEADapaaggkngggaSGDVDEGADLYDQAVAVVLRDGKAST 1034
Cdd:COG1674 496 PIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEEDE------------GGDDDEDDELFDEAVELVVETQKAST 563
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2392095750 1035 SYVQRRLGIGYNRAASIIERMEKEGIVGPANHAGKREILVPTEE 1078
Cdd:COG1674 564 SLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEE 607
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
245-1075 |
1.50e-175 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 550.84 E-value: 1.50e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 245 DSWEPEEEVSaDTRfaPPKPP---------RAAQHRDIRVA--EPYAAPASAYVDPLDGFEAEDEADFPPAYAAPAV--- 310
Cdd:PRK10263 488 PVVEPEPVVE-ETK--PARPPlyyfeeveeKRAREREQLAAwyQPIPEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVspl 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 311 -----QPHHAAPAASAFRAP-----------------------------------LARAPMSVPAQTAAVSAAFVAPAAR 350
Cdd:PRK10263 565 asgvkKATLATGAAATVAAPvfslansggprpqvkegigpqlprpkrirvptrreLASYGIKLPSQRAAEEKAREAQRNQ 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 351 REpSFAEPAAAPGAAFTADDWSRGAALAAQADWSDEAEADAQIQARAaeapfaqdpyDDGAAEAE--RAFEGHEAYEAYE 428
Cdd:PRK10263 645 YD-SGDQYNDDEIDAMQQDELARQFAQTQQQRYGEQYQHDVPVNAED----------ADAAAEAElaRQFAQTQQQRYSG 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 429 DQEAGrAAPVAYDDYEEAREEEAEADfvlEASDRVVAAGGGVQAEPAAVGGWRGLLQNNIVAFPGRKEKGAAPEPAMRAA 508
Cdd:PRK10263 714 EQPAG-ANPFSLDDFEFSPMKALLDD---GPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQP 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 509 QGPAAPRMPAAPAAQAGHATAVRPAAPPMAPAAASTVSAEQQRLRTGSGRAPaQRSLV------SAYNAPFE-----LPS 577
Cdd:PRK10263 790 QYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQP-QDTLLhpllmrNGDSRPLHkpttpLPS 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 578 VEFLTQPKprgrdSTLSPE---VLQENARLLEGVLEDFGVKGEIIEVRPGPVVTLYELEPAPGIKSSRVIGLADDIARSM 654
Cdd:PRK10263 869 LDLLTPPP-----SEVEPVdtfALEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSL 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 655 SAIAARVA-VIPGKNAIGIELPNQRRETVYLREIMAAESFAQNKGKLALTLGKTIGGEPVIADLAKMPHLLVAGTTGSGK 733
Cdd:PRK10263 944 STVAVRVVeVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGK 1023
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 734 SVAINTMILSLLYRMTPAQCRLIMIDPKMLELSIYDGIPHLLTPVVTDPKKAVVALKWAVREMEDRYRKMSKVGVRNIDG 813
Cdd:PRK10263 1024 SVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAG 1103
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 814 FNERVASAIERGETISRTV-QTGFDRETGEPVfeteefdLQPLPYIVVLIDEMADLMMVAGKDIEGTVQRLAQMARAAGI 892
Cdd:PRK10263 1104 YNEKIAEADRMMRPIPDPYwKPGDSMDAQHPV-------LKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGI 1176
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 893 HVIMATQRPSVDVITGTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGQGDMLFMAGGGRIQ-RVHGPFVGDNEVEAI 971
Cdd:PRK10263 1177 HLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPvRVHGAFVRDQEVHAV 1256
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 972 VNHLKAQGVPDYLDAILVDEDEEAdapaaggkngGGASGDVDEGAD-LYDQAVAVVLRDGKASTSYVQRRLGIGYNRAAS 1050
Cdd:PRK10263 1257 VQDWKARGRPQYVDGITSDSESEG----------GAGGFDGAEELDpLFDQAVQFVTEKRKASISGVQRQFRIGYNRAAR 1326
|
890 900
....*....|....*....|....*
gi 2392095750 1051 IIERMEKEGIVGPANHAGKREILVP 1075
Cdd:PRK10263 1327 IIEQMEAQGIVSEQGHNGNREVLAP 1351
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
684-902 |
4.75e-66 |
|
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: 221.87 E-value: 4.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 684 LREIMAAESFAQNKGKLALTLGKTIGGEPVIADLAKMP-HLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPKM 762
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 763 LELSIYDGIPHLLT-PVVTDPKKAVVALKWAVREMEDRYRKMSKVGVRNIDGFNERVASAIERGETISRTVQTGFDretg 841
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVFLVIYGVH---- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2392095750 842 epVFETEEFDLQPLPYIVVLIDEMADLMMVAGKD----IEGTVQRLAQMARAAGIHVIMATQRPS 902
Cdd:pfam01580 157 --VMCTAGRWLEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
575-676 |
2.50e-39 |
|
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: 141.13 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 575 LPSVEFLTQPKPRgrDSTLSPEVLQENARLLEGVLEDFGVKGEIIEVRPGPVVTLYELEPAPGIKSSRVIGLADDIARSM 654
Cdd:pfam17854 1 LPPLDLLEPPPTS--SQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALAL 78
|
90 100
....*....|....*....|...
gi 2392095750 655 SAIAARV-AVIPGKNAIGIELPN 676
Cdd:pfam17854 79 SAPSIRIvAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
1013-1075 |
5.58e-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: 112.85 E-value: 5.58e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2392095750 1013 DEGADLYDQAVAVVLRDGKASTSYVQRRLGIGYNRAASIIERMEKEGIVGPANHAGKREILVP 1075
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
1013-1075 |
3.47e-29 |
|
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: 110.58 E-value: 3.47e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2392095750 1013 DEGADLYDQAVAVVLRDGKASTSYVQRRLGIGYNRAASIIERMEKEGIVGPANHAGKREILVP 1075
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
17-176 |
9.30e-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: 110.75 E-value: 9.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 17 RRQGEvAGGVALAGLAAWLGVALATWTVSDPSFSHANSN--EVQNWAGQAGASAADLLMQLFGMGAVLLVALPVIWAAFL 94
Cdd:pfam13491 2 RLLRE-LLGLALLLLGLFLLLALVSYSPADPSWSTSGSGaaPVHNWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 95 FFGRPaegIWRRAWFALGGTVLFSAVAGCIDL---PAGWPLPIGLGGIAGDVVLKLPAALLGDFPSGLfayVLAAVIAVP 171
Cdd:pfam13491 81 FRRRS---LERRWLRLLGFLLLLLASSALFALrlpSLEFGLPGGAGGVIGRLLANALVTLLGFTGATL---LLLALLAIG 154
|
....*
gi 2392095750 172 ATWLF 176
Cdd:pfam13491 155 LSLVT 159
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
700-968 |
1.70e-18 |
|
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: 91.59 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 700 LALTLGKTIGGEPVIADL---AKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPK---MLELsiYDGIPH 773
Cdd:TIGR03928 446 LAVPIGLRGKDDIVYLNLhekAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPH 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 774 LLTpVVTD-----PKKAVVALKwavREMEDRYRKMSKVGVRNIDGFnervasaiergetisrtvQTGFDRETGEpvfete 848
Cdd:TIGR03928 524 LLG-TITNldgaqSMRALASIK---AELKKRQRLFGENNVNHINQY------------------QKLYKQGKAK------ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 849 efdlQPLPYIVVLIDEMADL------MMvagKDIEGTvqrlAQMARAAGIHVIMATQRPSvDVITGTIKANFPTRISFQV 922
Cdd:TIGR03928 576 ----EPMPHLFLISDEFAELkseqpeFM---KELVST----ARIGRSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKV 643
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2392095750 923 TSKIDSRTILGEQGAEQLLgqgdmlfMAGGGRIQrvhgpfVGDNEV 968
Cdd:TIGR03928 644 QDASDSNEILKTPDAAEIT-------VPGRAYLQ------VGNNEV 676
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
711-973 |
8.42e-13 |
|
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: 73.10 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 711 EPVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPKMLELSIYDGIPHlLTPVVT--DPKKAVVA 788
Cdd:TIGR03928 801 EPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 789 LKWAVREMEDRYRKMSKVGVRNIDGFNERvasaiergetisrtvqtgfdreTGEpvfeteefdlqPLPYIVVLIDEMaDL 868
Cdd:TIGR03928 880 IRRIKKEIDRRKKLFSEYGVASISMYNKA----------------------SGE-----------KLPQIVIIIDNY-DA 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 869 MMVAG--KDIEGTVQRLAQMARAAGIHVIM-ATQRPSVDVitgTIKANFPTRISFQVTSKIDSRTILGEQGAEQLLGQGD 945
Cdd:TIGR03928 926 VKEEPfyEDFEELLIQLAREGASLGIYLVMtAGRQNAVRM---PLMNNIKTKIALYLIDKSEYRSIVGRTKFTIEEIPGR 1002
|
250 260
....*....|....*....|....*...
gi 2392095750 946 MLFMAGGGRIQRVHGPFVGDNEVEAIVN 973
Cdd:TIGR03928 1003 GLIKKDEPTLFQTALPVKGEDDLEVIEN 1030
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
701-955 |
6.50e-09 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 59.96 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 701 ALTLGKTIGGEPVIADLAKM---PHLLVAGTTGSGKSVAINTMILSLLYRmtpaQCRLIMIDP--------KMLE----- 764
Cdd:COG3451 182 GIYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFDPggsyeilvRALGgtyid 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 765 -----------LSIYDGIPH------LLTPVVTDPKKAV-----VALKWAVREMedrYRKMSKVGVRNIDGFNERVASAI 822
Cdd:COG3451 258 lspgsptglnpFDLEDTEEKrdflleLLELLLGREGEPLtpeerAAIDRAVRAL---YRRADPEERTTLSDLYELLKEQP 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 823 ERGE---TISRTVQTG-----FDRETGEP-------VFETEEF----DLQP--LPYI-----------------VVLIDE 864
Cdd:COG3451 335 EAKDlaaRLEPYTKGGsygwlFDGPTNLDlsdarfvVFDLTELldnpELRPpvLLYLlhriwnrlrknndgrptLIVIDE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 865 MADLMmvagkDIEGTVQRLAQMARAA---GIHVIMATQRPSvDV----ITGTIKANFPTRIsFQVTSKIDSRTI-----L 932
Cdd:COG3451 415 AWLLL-----DNPAFAEFLEEWLKTLrkyNGAVIFATQSVE-DFlsspIAEAIIENSATKI-LLPQPKADIEDYaellgL 487
|
330 340
....*....|....*....|....*..
gi 2392095750 933 GEQGAEQLL----GQGDMLFMAGGGRI 955
Cdd:COG3451 488 SERELELIRsagrGKRDFLIKQGNGSV 514
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
704-963 |
1.65e-08 |
|
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: 58.83 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 704 LGKTIGGEPVIADLAK-----M-PHLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPK----MLELsiyDGIPH 773
Cdd:TIGR03924 413 IGVGDDGEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---EGLPH 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 774 lLTPVVTD--PKKAVVA-LKWAVR-EMEDRYRKMSKVG-VRNIDGFNERvasaiergetisrtvqtgfdRETGEpvfete 848
Cdd:TIGR03924 490 -VSAVITNlaDEAPLVDrMQDALAgEMNRRQELLRAAGnFANVAEYEKA--------------------RAAGA------ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 849 efDLQPLPYIVVLIDEMADLmMVAGKDIEGTVQRLAQMARAAGIHVIMATQRPSVDVITGtIKANFPTRISFQVTSKIDS 928
Cdd:TIGR03924 543 --DLPPLPALFVVVDEFSEL-LSQHPDFADLFVAIGRLGRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASES 618
|
250 260 270
....*....|....*....|....*....|....*.
gi 2392095750 929 RTILGEQGAEQLLGQ-GDMLFMAGGGRIQRVHGPFV 963
Cdd:TIGR03924 619 RAVLGVPDAYHLPSTpGAGYLKVDTAEPVRFRAAYV 654
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
722-922 |
1.73e-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: 48.75 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 722 HLLVAGTTGSGKSVAINTMILsllyRMTPAQCRLIMIDPKM---LELSIYDGIPHLLTPVVTDpkkavvALKWAVREMED 798
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLL----DQAARGGSVIITDPKGelfLVIPDRDDSFAALRALFFN------QLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 799 RYRKMskvgvrnidgFNERVasaiergetisrtvqtgfdretgepvfeteefdlqplpyiVVLIDEMAdlMMVAGKDIEg 878
Cdd:cd01127 71 LSPGR----------LPRRV----------------------------------------WFILDEFA--NLGRIPNLP- 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2392095750 879 tvqRLAQMARAAGIHVIMATQ------RPSVDVITGTIKANFPTRISFQV 922
Cdd:cd01127 98 ---NLLATGRKRGISVVLILQslaqleAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
701-952 |
1.99e-06 |
|
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: 51.53 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 701 ALTLGKTIG-GEPVIADLAKM--PHLLVAGTTGSGKSVAintmILSLLYRMTPAQCRLIMIDPK------------MLEL 765
Cdd:COG0433 25 GILIGKLLSpGVPVYLDLDKLlnRHILILGATGSGKSNT----LQVLLEELSRAGVPVLVFDPHgeysglaepgaeRADV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 766 SIYDGIPHLLTPVV---------------------TDPKKAVV--ALKWA----------------VREMEDRYRKMSKV 806
Cdd:COG0433 101 GVFDPGAGRPLPINpwdlfataselgplllsrldlNDTQRGVLreALRLAddkglllldlkdlialLEEGEELGEEYGNV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 807 GVRNIDGFNERVASAI-------ERGETISRTVQT----------GFDRETGEPV------------FETEEFDLQPLPy 857
Cdd:COG0433 181 SAASAGALLRRLESLEsadglfgEPGLDLEDLLRTdgrvtvidlsGLPEELQSTFvlwllrelfearPEVGDADDRKLP- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 858 IVVLIDEmADLmmVAGKDIEGTVQRLAQMA---RAAGIHVIMATQRPSvDVITgTIKANFPTRISFQVTSKIDSRTI--- 931
Cdd:COG0433 260 LVLVIDE-AHL--LAPAAPSALLEILERIAregRKFGVGLILATQRPS-DIDE-DVLSQLGTQIILRLFNPRDQKAVkaa 334
|
330 340
....*....|....*....|....*.
gi 2392095750 932 ---LGEQGAEQL--LGQGDMLFMAGG 952
Cdd:COG0433 335 aetLSEDLLERLpsLGTGEALVLGEG 360
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
711-761 |
5.35e-06 |
|
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: 50.38 E-value: 5.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2392095750 711 EPVIADLAKMPHLLVAGTTGSGKSVAINTMILSLLYRMTPAQCRLIMIDPK 761
Cdd:TIGR03925 354 APVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR 404
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
260-439 |
9.80e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.38 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 260 APPKPPRAAQHRDIRVAEPYAAPASAYVDPLDGFEAEDEADFPPAYAAPAVQPHHAAPAASAFRAPLARAPMSVPAQTAA 339
Cdd:PRK07003 372 VPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 340 VSAAFVAPAARREPSFAEPAAAPGAAFTADDWSRGAALAAQADWSDEAEADAQIQARAAEAPFAQDPYDDGAAEAERAFE 419
Cdd:PRK07003 452 KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPE 531
|
170 180
....*....|....*....|
gi 2392095750 420 GHEAYEAyEDQEAGRAAPVA 439
Cdd:PRK07003 532 ARPPTPA-AAAPAARAGGAA 550
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
18-417 |
1.78e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 42.31 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 18 RQGEVAGGVALAGLAAWLGVALATWTVSDPSFSHANSNEVQNWAGQAGASAADLLMQLFGMGAVLLVALPVIWAAFLFFG 97
Cdd:COG3903 537 AHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAA 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 98 RPAEGIWRRAWFALGGTVLFSAVAGCIDLPAGWPLPIGLGGIAGDVVLKLPAALLGDFPSGLFAYVLAAVIAVPATWLFL 177
Cdd:COG3903 617 AAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAA 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 178 NGAGIIDRDRPQARLRGAAEAGDEAESRLALVAGACVHHfysVRAAVSRRIAEEREQLRQGEFGNRFDSWEPEEEVSADT 257
Cdd:COG3903 697 AAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAA---LAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALA 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 258 RFAPPKPPRAAQHRDIRVAEPYAAPASAYVDPLDGFEAEDEADFPPAYAAPAVQPHHAAPAASAFRAPLARAPMSVPAQT 337
Cdd:COG3903 774 ALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAA 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 338 AAVSAAFVAPAARREPSFAEPAAAPGAAFTADDWSRGAALAAQADWSDEAEADAQIQARAAEAPFAQDPYDDGAAEAERA 417
Cdd:COG3903 854 LAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
704-883 |
6.18e-03 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 39.27 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 704 LGKTIGGE--PVIADLAKM--PHLLVAGTTGSGKSvaiNTM--ILSLLYRMTPAqcRLIMIDP-----KMLELSIYDGIp 772
Cdd:pfam01935 3 IGRLLDGSevPVYLDVNKLvsRHFAILGSTGSGKS---NTVavLLEELLEKKGA--TVLIFDPhgeygTLFRDLGAENV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392095750 773 HLLTPvvtdpkkavvalkwavremedryRKMSKVGVRNIDgFNErVASAIERGETISRTVQTGFDRETGEPVFETEEFDL 852
Cdd:pfam01935 77 NVITP-----------------------DPELKINPWLLS-PED-LADLLEELNLPNAEVQRSILEEALDQLKSEELGKL 131
|
170 180 190
....*....|....*....|....*....|.
gi 2392095750 853 QPLPYIVVLIDEMADLMMVAGKDIEGTVQRL 883
Cdd:pfam01935 132 SIDELIEKILEELLTEAAELNKLSNDAIRRV 162
|
|
| |
