|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
314-783 |
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: 896.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 314 MPSLDILADPKHTGQQTDKKNIYENARKLERTFQSFGVKAKVTQVHLGPAVTKYEVYPDVGVKVSKIVNLSDDLALALAA 393
Cdd:COG1674 137 LPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 394 KDIRIEAPIPGKSAIGIEVPNAEVAMVSLKEVLESKLNDKPDAKLLIGLGRNISGEAVLAELNKMPHLLVAGATGSGKSV 473
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 474 CVNGIITSILMRAKPHEVKMMMIDPKMVELNVYNGIPHLLAPVVTDPKKASQALKKVVNEMERRYELFSHTGTRNIEGYN 553
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 554 DHIK--RSNAEEEVKQPELPYIVVIVDELADLMMVASSDVEDSITRLSQMARAAGIHLIIATQRPSVDVITGVIKANIPS 631
Cdd:COG1674 377 EKVReaKAKGEEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 632 RIAFSVSSQTDSRTILDMGGAEKLLGRGDMLFLPVGANKPVRVQGAFLSDEEVEHVVDHVITQQKAQYQEEMIPEEVSET 711
Cdd:COG1674 457 RIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEED 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820052007 712 HS---EVTDDLYDEAVDLIIGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVLLSKEQYDEL 783
Cdd:COG1674 537 EGgddDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
264-774 |
5.90e-160 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 499.61 E-value: 5.90e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 264 QEERVEPLIPEKTQETVQTAKDEPSGGAQDSetaAAPPMTFTELENKDYQ-----MPSLDILADPKHTGQQTDKKNIYEN 338
Cdd:PRK10263 814 QPQYQQPQQPVAPQPQYQQPQQPVAPQPQDT---LLHPLLMRNGDSRPLHkpttpLPSLDLLTPPPSEVEPVDTFALEQM 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 339 ARKLERTFQSFGVKAKVTQVHLGPAVTKYEVYPDVGVKVSKIVNLSDDLALALAAKDIRIEAPIPGKSAIGIEVPNAEVA 418
Cdd:PRK10263 891 ARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQ 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 419 MVSLKEVLE-SKLNDKPdAKLLIGLGRNISGEAVLAELNKMPHLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMID 497
Cdd:PRK10263 971 TVYLREVLDnAKFRDNP-SPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMID 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 498 PKMVELNVYNGIPHLLAPVVTDPKKASQALKKVVNEMERRYELFSHTGTRNIEGYNDHIKRS------------------ 559
Cdd:PRK10263 1050 PKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEAdrmmrpipdpywkpgdsm 1129
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 560 NAEEEVKQpELPYIVVIVDELADLMMVASSDVEDSITRLSQMARAAGIHLIIATQRPSVDVITGVIKANIPSRIAFSVSS 639
Cdd:PRK10263 1130 DAQHPVLK-KEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSS 1208
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 640 QTDSRTILDMGGAEKLLGRGDMLFLPVGANKPVRVQGAFLSDEEVEHVVDHVITQQKAQYQEEMIPEEVSE------THS 713
Cdd:PRK10263 1209 KIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGITSDSESEggaggfDGA 1288
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820052007 714 EVTDDLYDEAVDLIIGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVL 774
Cdd:PRK10263 1289 EELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
422-617 |
1.42e-76 |
|
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: 246.52 E-value: 1.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 422 LKEVLESKLNDKPDAKLLIGLGRNISGEAVLAELNKMP-HLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPKM 500
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 501 VELNVYNGIPHLLA-PVVTDPKKASQALKKVVNEMERRYELFSHTGTRNIEGYNDHIKRSNAEEEVKQ------------ 567
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820052007 568 -----PELPYIVVIVDELADLMMVASSD----VEDSITRLSQMARAAGIHLIIATQRPS 617
Cdd:pfam01580 161 agrwlEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
714-776 |
5.00e-32 |
|
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: 118.28 E-value: 5.00e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820052007 714 EVTDDLYDEAVDLIIGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVLLS 776
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
459-669 |
2.27e-27 |
|
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: 119.32 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 459 PHLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPK---MVelNVYNGIPHLLApVVT--DPKKASQALKKVVNE 533
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFKNLPHLLG-TITnlDGAQSMRALASIKAE 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 534 MERRYELFSHTGTRNIEGYNDHIKrsnaEEEVKQPeLPYIVVIVDELADLmmvaSSDVEDSITRLSQMA---RAAGIHLI 610
Cdd:TIGR03928 547 LKKRQRLFGENNVNHINQYQKLYK----QGKAKEP-MPHLFLISDEFAEL----KSEQPEFMKELVSTArigRSLGVHLI 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820052007 611 IATQRPSvDVITGVIKANIPSRIAFSVSSQTDSRTILDMGGAEKLL--GRGdmlFLPVGAN 669
Cdd:TIGR03928 618 LATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITvpGRA---YLQVGNN 674
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
18-188 |
9.42e-07 |
|
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: 49.51 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 18 LKYELSGLLCVAISIIAVLQL------------------------GVVG----QTFVYLFRFFAgewfILCLIGLFLLGI 69
Cdd:pfam13491 3 LLRELLGLALLLLGLFLLLALvsyspadpswstsgsgaapvhnwgGRFGawlaDLLLQLFGYSA----WLLPVALLYWGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 70 SLFwKKKSPSLLTRRKAGLYCIIASILLLSHVqlfknlshhgsirsasvigNTWELFMIDmkqqaasPDLGGGMIGAVLF 149
Cdd:pfam13491 79 RLF-RRRSLERRWLRLLGFLLLLLASSALFAL-------------------RLPSLEFGL-------PGGAGGVIGRLLA 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820052007 150 AASHFLFASTGSQIMAIVLILMGLILVTGRSLQETLKKW 188
Cdd:pfam13491 132 NALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAERL 170
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
460-637 |
9.69e-07 |
|
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: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 460 HLLVAGATGSGKSVCVNGIITSILMRakphEVKMMMIDPKMvELNVyngiphllapVVTDPKKASQALKKVvnemerrye 539
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPKG-ELFL----------VIPDRDDSFAALRAL--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 540 LFSHTGTRNIEGYNDHIKRSNaeeevkqpelPYIVVIVDELADLMMVassdveDSITRLSQMARAAGIHLIIATQ----- 614
Cdd:cd01127 57 FFNQLFRALTELASLSPGRLP----------RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaql 120
|
170 180
....*....|....*....|....
gi 1820052007 615 -RPSVDVITGVIKANIPSRIAFSV 637
Cdd:cd01127 121 eAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
314-783 |
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: 896.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 314 MPSLDILADPKHTGQQTDKKNIYENARKLERTFQSFGVKAKVTQVHLGPAVTKYEVYPDVGVKVSKIVNLSDDLALALAA 393
Cdd:COG1674 137 LPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 394 KDIRIEAPIPGKSAIGIEVPNAEVAMVSLKEVLESKLNDKPDAKLLIGLGRNISGEAVLAELNKMPHLLVAGATGSGKSV 473
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 474 CVNGIITSILMRAKPHEVKMMMIDPKMVELNVYNGIPHLLAPVVTDPKKASQALKKVVNEMERRYELFSHTGTRNIEGYN 553
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 554 DHIK--RSNAEEEVKQPELPYIVVIVDELADLMMVASSDVEDSITRLSQMARAAGIHLIIATQRPSVDVITGVIKANIPS 631
Cdd:COG1674 377 EKVReaKAKGEEEEGLEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 632 RIAFSVSSQTDSRTILDMGGAEKLLGRGDMLFLPVGANKPVRVQGAFLSDEEVEHVVDHVITQQKAQYQEEMIPEEVSET 711
Cdd:COG1674 457 RIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEED 536
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820052007 712 HS---EVTDDLYDEAVDLIIGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVLLSKEQYDEL 783
Cdd:COG1674 537 EGgddDEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPAEGSKPREVLVSPEELEEL 611
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
264-774 |
5.90e-160 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 499.61 E-value: 5.90e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 264 QEERVEPLIPEKTQETVQTAKDEPSGGAQDSetaAAPPMTFTELENKDYQ-----MPSLDILADPKHTGQQTDKKNIYEN 338
Cdd:PRK10263 814 QPQYQQPQQPVAPQPQYQQPQQPVAPQPQDT---LLHPLLMRNGDSRPLHkpttpLPSLDLLTPPPSEVEPVDTFALEQM 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 339 ARKLERTFQSFGVKAKVTQVHLGPAVTKYEVYPDVGVKVSKIVNLSDDLALALAAKDIRIEAPIPGKSAIGIEVPNAEVA 418
Cdd:PRK10263 891 ARLVEARLADFRIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQ 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 419 MVSLKEVLE-SKLNDKPdAKLLIGLGRNISGEAVLAELNKMPHLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMID 497
Cdd:PRK10263 971 TVYLREVLDnAKFRDNP-SPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMID 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 498 PKMVELNVYNGIPHLLAPVVTDPKKASQALKKVVNEMERRYELFSHTGTRNIEGYNDHIKRS------------------ 559
Cdd:PRK10263 1050 PKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIAEAdrmmrpipdpywkpgdsm 1129
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 560 NAEEEVKQpELPYIVVIVDELADLMMVASSDVEDSITRLSQMARAAGIHLIIATQRPSVDVITGVIKANIPSRIAFSVSS 639
Cdd:PRK10263 1130 DAQHPVLK-KEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSS 1208
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 640 QTDSRTILDMGGAEKLLGRGDMLFLPVGANKPVRVQGAFLSDEEVEHVVDHVITQQKAQYQEEMIPEEVSE------THS 713
Cdd:PRK10263 1209 KIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGITSDSESEggaggfDGA 1288
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820052007 714 EVTDDLYDEAVDLIIGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVL 774
Cdd:PRK10263 1289 EELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
422-617 |
1.42e-76 |
|
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: 246.52 E-value: 1.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 422 LKEVLESKLNDKPDAKLLIGLGRNISGEAVLAELNKMP-HLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPKM 500
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 501 VELNVYNGIPHLLA-PVVTDPKKASQALKKVVNEMERRYELFSHTGTRNIEGYNDHIKRSNAEEEVKQ------------ 567
Cdd:pfam01580 81 GELSAYEDIPHLLSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEDPLDGFGDVflviygvhvmct 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820052007 568 -----PELPYIVVIVDELADLMMVASSD----VEDSITRLSQMARAAGIHLIIATQRPS 617
Cdd:pfam01580 161 agrwlEILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
314-414 |
1.89e-46 |
|
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: 160.39 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 314 MPSLDILADPKHTGQQTDKKNIYENARKLERTFQSFGVKAKVTQVHLGPAVTKYEVYPDVGVKVSKIVNLSDDLALALAA 393
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 1820052007 394 KDIRIEAPIPGKSAIGIEVPN 414
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
714-776 |
1.38e-33 |
|
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: 122.86 E-value: 1.38e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820052007 714 EVTDDLYDEAVDLIIGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVLLS 776
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
714-776 |
5.00e-32 |
|
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: 118.28 E-value: 5.00e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820052007 714 EVTDDLYDEAVDLIIGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVLLS 776
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
459-669 |
2.27e-27 |
|
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: 119.32 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 459 PHLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPK---MVelNVYNGIPHLLApVVT--DPKKASQALKKVVNE 533
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMA--NLFKNLPHLLG-TITnlDGAQSMRALASIKAE 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 534 MERRYELFSHTGTRNIEGYNDHIKrsnaEEEVKQPeLPYIVVIVDELADLmmvaSSDVEDSITRLSQMA---RAAGIHLI 610
Cdd:TIGR03928 547 LKKRQRLFGENNVNHINQYQKLYK----QGKAKEP-MPHLFLISDEFAEL----KSEQPEFMKELVSTArigRSLGVHLI 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820052007 611 IATQRPSvDVITGVIKANIPSRIAFSVSSQTDSRTILDMGGAEKLL--GRGdmlFLPVGAN 669
Cdd:TIGR03928 618 LATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITvpGRA---YLQVGNN 674
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
459-680 |
7.81e-17 |
|
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: 85.02 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 459 PHLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPK-------MVELnvyngiPHLLApVVTDpkKASQA----- 526
Cdd:TIGR03924 436 PHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatflgLEGL------PHVSA-VITN--LADEAplvdr 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 527 LKKVVN-EMERRYELFSHTGT-RNIEGYNdHIKRSNAEeevkQPELPYIVVIVDELADLMmvAS----SDVEDSITRLsq 600
Cdd:TIGR03924 507 MQDALAgEMNRRQELLRAAGNfANVAEYE-KARAAGAD----LPPLPALFVVVDEFSELL--SQhpdfADLFVAIGRL-- 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 601 mARAAGIHLIIATQRPSVDVITGvIKANIPSRIAFSVSSQTDSRTILDMGGAEKLLGRGDMLFLPVGANKPVRVQGAFLS 680
Cdd:TIGR03924 578 -GRSLGVHLLLASQRLDEGRLRG-LESHLSYRIGLKTFSASESRAVLGVPDAYHLPSTPGAGYLKVDTAEPVRFRAAYVS 655
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
454-659 |
6.44e-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: 72.71 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 454 ELNKMPHLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPKMVELNVYNGIPHLlAPVVT--DPKKASQALKKVV 531
Cdd:TIGR03928 806 DLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHV-ADYFTldEEEKIEKLIRRIK 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 532 NEMERRYELFSHTGTRNIEGYNdhikrsnaeeEVKQPELPYIVVIVDELaDLMMVAS--SDVEDSITRLSQMARAAGIHL 609
Cdd:TIGR03928 885 KEIDRRKKLFSEYGVASISMYN----------KASGEKLPQIVIIIDNY-DAVKEEPfyEDFEELLIQLAREGASLGIYL 953
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820052007 610 II-ATQRPSVDVitgVIKANIPSRIAFSVSSQTDSRTI-----LDMggaEKLLGRG 659
Cdd:TIGR03928 954 VMtAGRQNAVRM---PLMNNIKTKIALYLIDKSEYRSIvgrtkFTI---EEIPGRG 1003
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
460-708 |
3.50e-12 |
|
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: 69.64 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 460 HLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPKMVELNVYNGIPHlLAPVVT--DPKKASQALKKVVNEMERR 537
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPH-VGGVAGrlDPERVRRTVAEVEGLLRRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 538 YELFSHTGTRNIEGYNDHIKRSNAeeevkqPELPY--IVVIVDELADLMMvASSDVEDSITRLSQMARAAGIHLIIATQR 615
Cdd:TIGR03925 160 ERLFRTHGIDSMAQYRARRAAGRL------PEDPFgdVFLVIDGWGTLRQ-DFEDLEDKVTDLAARGLAYGVHVVLTASR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 616 PSvdVITGVIKANIPSRIAF----SVSSQTDSRTILDMggAEKLLGRG------DMLF-LPVGANKPvrvQGAFLSDEEV 684
Cdd:TIGR03925 233 WS--EIRPALRDLIGTRIELrlgdPMDSEIDRRAAARV--PAGRPGRGltpdglHMLIaLPRLDGIA---SVDDLGTRGL 305
|
250 260
....*....|....*....|....
gi 1820052007 685 EHVVDHVITQQKAQyQEEMIPEEV 708
Cdd:TIGR03925 306 VAVIRDVWGGPPAP-PVRLLPARL 328
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
413-675 |
3.30e-08 |
|
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: 56.54 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 413 PNAEVAMVSlKEVLESKLNDKPdaKLLIGLGRNiSGEAVLAELNKM--PHLLVAGATGSGKSVCVNGIITSiLMRAKphe 490
Cdd:COG0433 4 PGSPVYLAD-DEELEELLGDGG--GILIGKLLS-PGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEE-LSRAG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 491 VKMMMIDPK------------MVELNVYNG--------------------IPHLLAP----------------------- 515
Cdd:COG0433 76 VPVLVFDPHgeysglaepgaeRADVGVFDPgagrplpinpwdlfataselGPLLLSRldlndtqrgvlrealrladdkgl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 516 ----------VVTDPKKASQALKKV-----------VNEMERRYELFSHTGTR--------------NIEGYNDHIKR-- 558
Cdd:COG0433 156 llldlkdliaLLEEGEELGEEYGNVsaasagallrrLESLESADGLFGEPGLDledllrtdgrvtviDLSGLPEELQStf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 559 ---------SNAEEEVKQPELPY-IVVIVDELADLMMVASSDVEDSITRLSQMARAAGIHLIIATQRPSvDVITGVIkAN 628
Cdd:COG0433 236 vlwllrelfEARPEVGDADDRKLpLVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDEDVL-SQ 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1820052007 629 IPSRIAFSVSSQTDSRTI------LDMGGAEKL--LGRGDMLFLPVGANKPVRVQ 675
Cdd:COG0433 314 LGTQIILRLFNPRDQKAVkaaaetLSEDLLERLpsLGTGEALVLGEGIPLPVLVK 368
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
420-674 |
6.32e-08 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 56.53 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 420 VSLKEVLESKLNDKPDAKLLIGLGRNISG-EAVLAELNKMPHLLVAGATGSGKSvcvnGIITSILMR-AKPHEVKMMMID 497
Cdd:TIGR03928 1057 LSLEEFRERYEVRKILEEGSIPIGLDEETvEPVYIDLTENPHLLIVGESDDGKT----NVLKSLLKTlAKQEKEKIGLID 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 498 PKMVELNVYNGIPHLlAPVVTDPKKASQALKKVVNEMERRyelfshtgtrniEGYNDHIKRSNAEEEVKQPelpyIVVIV 577
Cdd:TIGR03928 1133 SIDRGLLAYRDLKEV-ATYIEEKEDLKEILAELKEEIELR------------EAAYKEALQNETGEPAFKP----ILLII 1195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 578 DELADLMMVASSDVEDSITRLSQMARAAGIHLIIATQRPSV----DVITGVIKAnipSRIAFSVSSQTDSRTI-LDMGGA 652
Cdd:TIGR03928 1196 DDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVAGTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQSFFkLPFTRS 1272
|
250 260
....*....|....*....|..
gi 1820052007 653 EKLLGRGDMLFLPVGANKPVRV 674
Cdd:TIGR03928 1273 EKELEPGEGYFVVNGKYQKIKI 1294
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
382-612 |
1.60e-07 |
|
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: 54.61 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 382 NLSDDLALALAAKDIRIEAPIPGKSAIGIEV-PnaevAMVSLKEVLEskLNDKPDAKLLIGLGRNiSGEAVLAELNKMPH 460
Cdd:TIGR03925 293 GIASVDDLGTRGLVAVIRDVWGGPPAPPVRLlP----ARLPLSALPA--GGGAPRLRVPLGLGES-DLAPVYVDFAESPH 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 461 LLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPKmvelnvyngipHLLAPVVTDpkkasqalkkvvnEMERRYEL 540
Cdd:TIGR03925 366 LLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR-----------RTLLGAVPE-------------DYLAGYAA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 541 FSHTGTRNIEGYNDHIKRSNAEEEVKQPEL--------PYIVVIVDELaDLMMVASSDVEDSITRLSQMARAAGIHLIIA 612
Cdd:TIGR03925 422 TSAALTELIAALAALLERRLPGPDVTPQQLrarswwsgPEIYVVVDDY-DLVATGSGNPLAPLVELLPHARDIGLHVVVA 500
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
18-188 |
9.42e-07 |
|
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: 49.51 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 18 LKYELSGLLCVAISIIAVLQL------------------------GVVG----QTFVYLFRFFAgewfILCLIGLFLLGI 69
Cdd:pfam13491 3 LLRELLGLALLLLGLFLLLALvsyspadpswstsgsgaapvhnwgGRFGawlaDLLLQLFGYSA----WLLPVALLYWGW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 70 SLFwKKKSPSLLTRRKAGLYCIIASILLLSHVqlfknlshhgsirsasvigNTWELFMIDmkqqaasPDLGGGMIGAVLF 149
Cdd:pfam13491 79 RLF-RRRSLERRWLRLLGFLLLLLASSALFAL-------------------RLPSLEFGL-------PGGAGGVIGRLLA 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 1820052007 150 AASHFLFASTGSQIMAIVLILMGLILVTGRSLQETLKKW 188
Cdd:pfam13491 132 NALVTLLGFTGATLLLLALLAIGLSLVTGFSWLALAERL 170
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
460-637 |
9.69e-07 |
|
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: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 460 HLLVAGATGSGKSVCVNGIITSILMRakphEVKMMMIDPKMvELNVyngiphllapVVTDPKKASQALKKVvnemerrye 539
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAAR----GGSVIITDPKG-ELFL----------VIPDRDDSFAALRAL--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 540 LFSHTGTRNIEGYNDHIKRSNaeeevkqpelPYIVVIVDELADLMMVassdveDSITRLSQMARAAGIHLIIATQ----- 614
Cdd:cd01127 57 FFNQLFRALTELASLSPGRLP----------RRVWFILDEFANLGRI------PNLPNLLATGRKRGISVVLILQslaql 120
|
170 180
....*....|....*....|....
gi 1820052007 615 -RPSVDVITGVIKANIPSRIAFSV 637
Cdd:cd01127 121 eAVYGKDGAQTILGNCNTKLYLGT 144
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
314-432 |
8.80e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily is composed of uncharacterized bacterial proteins with similarity to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes.
Pssm-ID: 143490 [Multi-domain] Cd Length: 353 Bit Score: 39.07 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820052007 314 MPSLDIladpkhtgqqtDKKNIYENARKLERTFQSFGVK-AKVTQVHLG-PAVTkyEVYPDVGVKV---SKIVNLsddla 388
Cdd:cd06815 1 YPRLEI-----------NLSKIRHNAKVLVELCKSRGIEvTGVTKVVCGdPEIA--EALLEGGITHladSRIENL----- 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1820052007 389 laLAAKDIRIEAP-----IPGKSAIGIEVPNAEVAMVSLKEVLEsKLND 432
Cdd:cd06815 63 --KKLKDLGISGPkmllrIPMLSEVEDVVKYADISLNSELETIK-ALSE 108
|
|
| |
