|
Name |
Accession |
Description |
Interval |
E-value |
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
27-681 |
0e+00 |
|
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: 791.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 27 PSRMRMIMPVVMVAAMCGMMVMMFRGGG-AMNPMMLMFPAMMLVSMFGMMggaFAGNSSGGAAG--LNEERKDYLRSITD 103
Cdd:TIGR03924 1 GPLLQKLLPVVMVVAVVGMVVMMFASGGrQRNPMFLIFPLMMLVSMLGML---AGGRGGGGKKTpeLDEDRRDYLRYLDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 104 NRKTVHAAEAELHAFLRYTHPGPDEIARLIGGKRMWEVQVASPQFLRVRVGRGRIANQVRVIVPEAAPTSDLDPVGVVEL 183
Cdd:TIGR03924 78 LRREVRETAAAQRAALEWRHPDPDTLWALVGTPRMWERRPGDPDFLEVRVGVGVQPLATRLVVPETGPVEDLEPVTAVAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 184 TRFAKAYSTVGGMPVAINLLSAPQVGIDGDPELVAGLVRAMIAEVAVLHGPDQVAVAAVLSDPDApEWSWLKWLPHSQHP 263
Cdd:TIGR03924 158 RRFLRAHSTVPDLPVAVSLRGFARISLVGDRDQARALARAMLCQLAVFHGPDDVGIAVVTSDPDR-DWDWLKWLPHNQHP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 264 SDNDAIGSSRMVYRTVAELRTKVLAGL-NRGPFSANSQPTLdrTHYLLIVD---VAGPASDRDISGIDGCTWLRLGATEQ 339
Cdd:TIGR03924 237 TRFDAAGPARLVYTSLAELEAALAELLaDRGRFSPDDAASL--PHLVVVVDggdLPGWEDLIGESGLDGVTVIDLGGSLP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 340 NLP--RALRFAVsEDGSLNEVTVRGLRRVGV-ADSLSTAAMTAMARSLSPYRLSTvvEAVAAEQASGGTSWEEMVGIADP 416
Cdd:TIGR03924 315 GLPdrRGLRLVV-EADRLDARTADGVEEFGVaPDQLSIAEAEALARRLARWRAAT--AGTVDAPLTGARDLLELLGIGDP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 417 GNIRVEQVWVRRRDEDRarLNIPFGHDPAGSLVYLDIKESAEEGMGPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLN 496
Cdd:TIGR03924 392 ATLDVDRLWRPRPGRDR--LRVPIGVGDDGEPVELDLKESAEGGMGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLN 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 497 LLLVDFKGGATFLGFERLSHVTAIVTNMEEEADLVTRMEDVINGEMARRQRILRDAGNFASVADYERAREQGADLRPLPT 576
Cdd:TIGR03924 470 LVLVDFKGGATFLGLEGLPHVSAVITNLADEAPLVDRMQDALAGEMNRRQELLRAAGNFANVAEYEKARAAGADLPPLPA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 577 LLIILDEFAELLEQHPNFSKLFVAIGRLGRSLRIHLLLASQKVPANRMGELEAHLSYRVALRTNQTSDSRDAIGTADAYH 656
Cdd:TIGR03924 550 LFVVVDEFSELLSQHPDFADLFVAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFSASESRAVLGVPDAYH 629
|
650 660
....*....|....*....|....*
gi 2329068856 657 LPKKPGSGYLRVGSGDLQRFQAAYV 681
Cdd:TIGR03924 630 LPSTPGAGYLKVDTAEPVRFRAAYV 654
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
743-1317 |
0e+00 |
|
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: 620.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 743 TVMEAVLQQLARHGQPAHKMWLPPLVTPPTLERMIR----------AVPQGALQMPVALVDKPRQQRQDVWSVDMSGAGG 812
Cdd:TIGR03925 1 TVLDVVVDRLAGQGPPAHQVWLPPLPEPPALDDLLPrldvdpwrvdYGQRGRLTVPVGIVDRPFEQRQDPLVVDLSGAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 813 HMAIVGGTQSGKSTALQSFILSAALTHTPEQVQFYCLDFSGGGLAALTNLPHVGSVAAARDGDRIRRTIALVTNLLESRQ 892
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHVGGVAGRLDPERVRRTVAEVEGLLRRRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 893 SMFTEFGIDSIRKFRTLRDGGGTPpwqdRDPYGDVFLVIDGWDVgfgtngpYYDEYT---PVMESIALQGLNYGIHLVVS 969
Cdd:TIGR03925 161 RLFRTHGIDSMAQYRARRAAGRLP----EDPFGDVFLVIDGWGT-------LRQDFEdleDKVTDLAARGLAYGVHVVLT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 970 SSRWIAIRPAIKDLMQTRVEMRLGDLADTTFNthRNVVAAIPANRPGRCISTEGLHMLTALPRIDGVGDpnSAAEGLAAA 1049
Cdd:TIGR03925 230 ASRWSEIRPALRDLIGTRIELRLGDPMDSEID--RRAAARVPAGRPGRGLTPDGLHMLIALPRLDGIAS--VDDLGTRGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1050 AAEITQRYPGRRAPQVKLLPPQVGMDEVragwpVPQTLAQRLVVPFGVRESDLSPATIDFSVSTHFIVLGSTGSGKSTTL 1129
Cdd:TIGR03925 306 VAVIRDVWGGPPAPPVRLLPARLPLSAL-----PAGGGAPRLRVPLGLGESDLAPVYVDFAESPHLLIFGDSESGKTTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1130 AALLESIRRQYDPSQARVLLIDYRRRHLETVPQEMLIGHVTSERDVREALPALVEKMRSRRPPENVTPRQLAERSWWSGP 1209
Cdd:TIGR03925 381 RTIARGIVRRYSPDQARLVVVDYRRTLLGAVPEDYLAGYAATSAALTELIAALAALLERRLPGPDVTPQQLRARSWWSGP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1210 EVFVVIDDYHMVVQRGGmNPLEPLKEIIVDGRDTGLHVIAARNIAQADTALYDNVIGQMKNLNSSGLIMDGSKLDGILIG 1289
Cdd:TIGR03925 461 EIYVVVDDYDLVATGSG-NPLAPLVELLPHARDIGLHVVVARRSGGAARALMDPVLARLKDLGAPGLLLSGDRDEGPLLG 539
|
570 580
....*....|....*....|....*...
gi 2329068856 1290 DVRPTKQPPGRGIFVEPmSSRRDLVQVA 1317
Cdd:TIGR03925 540 GVRPRPLPPGRGVLVTR-GGGPQLIQVA 566
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
786-1033 |
3.93e-38 |
|
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: 142.52 E-value: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 786 QMPVALvdkPRQQRQDVWSVDMSGAGGHMAIVGGTQSGKSTALQSFILSAALTHTPEQVQFYCLDFSGGGLAALTNLPHV 865
Cdd:pfam01580 16 RLPIAL---GKDISGNPEVFDLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 866 GSVAAARDGDRIRRTIALVTNLLESRQSMFTEFGIDSIRKFRtlrDGGGTPPWqdrDPYGDVFLVIdgwdvgfgtngpyy 945
Cdd:pfam01580 93 LSVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYN---GEIAEDPL---DGFGDVFLVI-------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 946 deytpvmesialqglnYGIHLVVSSSRWIAIRPAIKDLMQTRVEMRLGDLADTtfnthrNVVAAIPANRPGRCISTEGLH 1025
Cdd:pfam01580 153 ----------------YGVHVMCTAGRWLEILPYLVVIVDERAELRLAAPKDS------EMRVEDAIVRLAQKGRAAGIH 210
|
....*...
gi 2329068856 1026 MLTALPRI 1033
Cdd:pfam01580 211 LLLATQRP 218
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
421-617 |
4.43e-32 |
|
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: 125.18 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 421 VEQVWVRRRDEDRARLNIPFGHDPAGSLVYLDIKESAEegmgpHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLV 500
Cdd:pfam01580 2 LEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPV-----HLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 501 DFKGGAtFLGFERLSHVTAIvtNMEEEADLVTRMEDVINGEMARRQRILRDAGnFASVADY--ERAR------------- 565
Cdd:pfam01580 77 DPKMGE-LSAYEDIPHLLSV--PVATDPKRALRALEWLVDEMERRYALFRALG-VRSIAGYngEIAEdpldgfgdvflvi 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2329068856 566 -------EQGADLRPLPTLLIILDEFAELLEQHPNFSK-----LFVAIGRLGRSLRIHLLLASQ 617
Cdd:pfam01580 153 ygvhvmcTAGRWLEILPYLVVIVDERAELRLAAPKDSEmrvedAIVRLAQKGRAAGIHLLLATQ 216
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
431-684 |
2.63e-20 |
|
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: 96.92 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 431 EDRARLNIPFGHDPAGSLVYLDIKEsaeegMgPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFKgGATFLG 510
Cdd:COG1674 256 NSKSPLPIALGKDISGEPVVADLAK-----M-PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPK-MVELSV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 511 FERLSH-VTAIVTNMEEEAD----LVtrmedvinGEMARRQRILRDAG--NFAS----VADYERAREQGADLRPLPTLLI 579
Cdd:COG1674 329 YNGIPHlLTPVVTDPKKAANalkwAV--------REMERRYKLFAKAGvrNIAGynekVREAKAKGEEEEGLEPLPYIVV 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 580 ILDEFAELL-------EQhpnfsklfvAIGRL---GRSLRIHLLLASQK-------------VPAnrmgeleahlsyRVA 636
Cdd:COG1674 401 IIDELADLMmvagkevEE---------AIARLaqkARAAGIHLILATQRpsvdvitglikanIPS------------RIA 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2329068856 637 LRTNQTSDSRDAIGTADAYHLpkkPGSG---YLRVGSGDLQRFQAAYVGEK 684
Cdd:COG1674 460 FAVSSKIDSRTILDQGGAEKL---LGRGdmlFLPPGASKPIRVQGAFVSDE 507
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
368-694 |
1.71e-12 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 72.43 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 368 VADSLSTAAMTAMARSLSpYRLSTVveAVAAEQASGGTSWeemVGIADPgNIRVEQVWVR------RRDEDRARLNIPFG 441
Cdd:PRK10263 923 LAPGVKAARISNLSRDLA-RSLSTV--AVRVVEVIPGKPY---VGLELP-NKKRQTVYLRevldnaKFRDNPSPLTVVLG 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 442 HDPAGSLVYLDIKESaeegmgPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFKGGATFLgFERLSH-VTAI 520
Cdd:PRK10263 996 KDIAGEPVVADLAKM------PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSV-YEGIPHlLTEV 1068
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 521 VTNMEEEADlvtRMEDVINgEMARRQRILRDAG--NFASVAD--YERAR-----------------EQGADLRPLPTLLI 579
Cdd:PRK10263 1069 VTDMKDAAN---ALRWCVN-EMERRYKLMSALGvrNLAGYNEkiAEADRmmrpipdpywkpgdsmdAQHPVLKKEPYIVV 1144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 580 ILDEFAELLEQ-HPNFSKLFVAIGRLGRSLRIHLLLASQKVPANRM-GELEAHLSYRVALRTNQTSDSRDAIGTADAYHL 657
Cdd:PRK10263 1145 LVDEFADLMMTvGKKVEELIARLAQKARAAGIHLVLATQRPSVDVItGLIKANIPTRIAFTVSSKIDSRTILDQAGAESL 1224
|
330 340 350
....*....|....*....|....*....|....*..
gi 2329068856 658 pkkpgsgylrVGSGDLqrfqaAYVGEKYTPPAQVSAA 694
Cdd:PRK10263 1225 ----------LGMGDM-----LYSGPNSTLPVRVHGA 1246
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
1104-1152 |
1.88e-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: 51.92 E-value: 1.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2329068856 1104 PATIDFS--VSTHFIVLGSTGSGKSTTLAALLESIRRQydpsQARVLLIDY 1152
Cdd:COG0433 37 PVYLDLDklLNRHILILGATGSGKSNTLQVLLEELSRA----GVPVLVFDP 83
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1104-1189 |
1.71e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.23 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1104 PATIDFSVSTHFIVLGSTGSGKSTTLAALLESIRRQYDPSQARVLLIDYRRRHL---ETVPQeMLIGHVTSERDVREALP 1180
Cdd:PRK10263 1002 PVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELsvyEGIPH-LLTEVVTDMKDAANALR 1080
|
....*....
gi 2329068856 1181 ALVEKMRSR 1189
Cdd:PRK10263 1081 WCVNEMERR 1089
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1119-1163 |
3.49e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 43.68 E-value: 3.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2329068856 1119 GSTGSGKSTTLaALLEsirRQYDPSQARVLL---------IDYRRRHLETVPQE 1163
Cdd:cd03249 36 GSSGCGKSTVV-SLLE---RFYDPTSGEILLdgvdirdlnLRWLRSQIGLVSQE 85
|
|
| 5TM_YidC_Alb3 |
cd20070 |
Five transmembrane core domain of membrane protein insertase YidC, Alb3, and similar proteins; ... |
33-74 |
5.53e-04 |
|
Five transmembrane core domain of membrane protein insertase YidC, Alb3, and similar proteins; This group is composed of the bacterial and chloroplastic members of the YidC/Oxa1/Alb3 protein family of insertases, including bacterial YidC, and chloroplastic ALBINO3 (Alb3) and Alb3-like proteins such as ALBINO3-like protein 1 (also called Alb4). Membrane protein insertase YidC, also called foldase YidC or membrane integrase YidC, facilitates proper folding, insertion, and assembly of inner membrane proteins and complexes. Depending on the nature of the substrate, YidC functions in a Sec-independent (YidC only) or a Sec-dependent manner as part of a complex containing YidC, the SecYEG channel, and SecDFYajC. YidC from Gram-negative bacteria contains an extra transmembrane segment (TM1) at the N-terminus and a large periplasmic domain, located between TM1 and TM2, that adopts a beta-super sandwich fold that is found in sugar-binding proteins such as galactose mutarotase. Alb3 and Alb3-like proteins are required for the post-translational insertion of the light-harvesting chlorophyll-binding proteins (LHCPs) into the chloroplast thylakoid membrane. Alb3 acts independently and may also function cooperatively with the thylakoid cpSecYE translocase to insert proteins co-translationally into the thylakoid membrane, similar to bacterial YidC that can function with the SecYEG translocase. YidC/Oxa1/Alb3 family insertases contain a core domain of five transmembrane (5TM) segments that is essential to insertase function.
Pssm-ID: 410994 [Multi-domain] Cd Length: 181 Bit Score: 42.37 E-value: 5.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2329068856 33 IMPVVMVAAMCGMMVMMFRGGGAMNP----MMLMFPAMMLVSMFGM 74
Cdd:cd20070 112 ILPILMGVTMFLQQKLTPTPTDDQAPqqkmMMYFMPVMFTFIFLSF 157
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1114-1252 |
8.09e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1114 HFIVLGSTGSGKSTTLAALLesirRQYDPSQARVLLIDyrrrhLETVPQEMLIGHVTSERDVREALPALVEKMRSRrppe 1193
Cdd:smart00382 4 VILIVGPPGSGKTTLARALA----RELGPPGGGVIYID-----GEDILEEVLDQLLLIIVGGKKASGSGELRLRLA---- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2329068856 1194 nvtpRQLAERswwSGPEVfVVIDDYHM---VVQRGGMNPLEPLKEIIVDGRDTGLHVIAARN 1252
Cdd:smart00382 71 ----LALARK---LKPDV-LILDEITSlldAEQEALLLLLEELRLLLLLKSEKNLTVILTTN 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
27-681 |
0e+00 |
|
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: 791.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 27 PSRMRMIMPVVMVAAMCGMMVMMFRGGG-AMNPMMLMFPAMMLVSMFGMMggaFAGNSSGGAAG--LNEERKDYLRSITD 103
Cdd:TIGR03924 1 GPLLQKLLPVVMVVAVVGMVVMMFASGGrQRNPMFLIFPLMMLVSMLGML---AGGRGGGGKKTpeLDEDRRDYLRYLDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 104 NRKTVHAAEAELHAFLRYTHPGPDEIARLIGGKRMWEVQVASPQFLRVRVGRGRIANQVRVIVPEAAPTSDLDPVGVVEL 183
Cdd:TIGR03924 78 LRREVRETAAAQRAALEWRHPDPDTLWALVGTPRMWERRPGDPDFLEVRVGVGVQPLATRLVVPETGPVEDLEPVTAVAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 184 TRFAKAYSTVGGMPVAINLLSAPQVGIDGDPELVAGLVRAMIAEVAVLHGPDQVAVAAVLSDPDApEWSWLKWLPHSQHP 263
Cdd:TIGR03924 158 RRFLRAHSTVPDLPVAVSLRGFARISLVGDRDQARALARAMLCQLAVFHGPDDVGIAVVTSDPDR-DWDWLKWLPHNQHP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 264 SDNDAIGSSRMVYRTVAELRTKVLAGL-NRGPFSANSQPTLdrTHYLLIVD---VAGPASDRDISGIDGCTWLRLGATEQ 339
Cdd:TIGR03924 237 TRFDAAGPARLVYTSLAELEAALAELLaDRGRFSPDDAASL--PHLVVVVDggdLPGWEDLIGESGLDGVTVIDLGGSLP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 340 NLP--RALRFAVsEDGSLNEVTVRGLRRVGV-ADSLSTAAMTAMARSLSPYRLSTvvEAVAAEQASGGTSWEEMVGIADP 416
Cdd:TIGR03924 315 GLPdrRGLRLVV-EADRLDARTADGVEEFGVaPDQLSIAEAEALARRLARWRAAT--AGTVDAPLTGARDLLELLGIGDP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 417 GNIRVEQVWVRRRDEDRarLNIPFGHDPAGSLVYLDIKESAEEGMGPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLN 496
Cdd:TIGR03924 392 ATLDVDRLWRPRPGRDR--LRVPIGVGDDGEPVELDLKESAEGGMGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLN 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 497 LLLVDFKGGATFLGFERLSHVTAIVTNMEEEADLVTRMEDVINGEMARRQRILRDAGNFASVADYERAREQGADLRPLPT 576
Cdd:TIGR03924 470 LVLVDFKGGATFLGLEGLPHVSAVITNLADEAPLVDRMQDALAGEMNRRQELLRAAGNFANVAEYEKARAAGADLPPLPA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 577 LLIILDEFAELLEQHPNFSKLFVAIGRLGRSLRIHLLLASQKVPANRMGELEAHLSYRVALRTNQTSDSRDAIGTADAYH 656
Cdd:TIGR03924 550 LFVVVDEFSELLSQHPDFADLFVAIGRLGRSLGVHLLLASQRLDEGRLRGLESHLSYRIGLKTFSASESRAVLGVPDAYH 629
|
650 660
....*....|....*....|....*
gi 2329068856 657 LPKKPGSGYLRVGSGDLQRFQAAYV 681
Cdd:TIGR03924 630 LPSTPGAGYLKVDTAEPVRFRAAYV 654
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
743-1317 |
0e+00 |
|
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: 620.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 743 TVMEAVLQQLARHGQPAHKMWLPPLVTPPTLERMIR----------AVPQGALQMPVALVDKPRQQRQDVWSVDMSGAGG 812
Cdd:TIGR03925 1 TVLDVVVDRLAGQGPPAHQVWLPPLPEPPALDDLLPrldvdpwrvdYGQRGRLTVPVGIVDRPFEQRQDPLVVDLSGAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 813 HMAIVGGTQSGKSTALQSFILSAALTHTPEQVQFYCLDFSGGGLAALTNLPHVGSVAAARDGDRIRRTIALVTNLLESRQ 892
Cdd:TIGR03925 81 HVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLASLADLPHVGGVAGRLDPERVRRTVAEVEGLLRRRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 893 SMFTEFGIDSIRKFRTLRDGGGTPpwqdRDPYGDVFLVIDGWDVgfgtngpYYDEYT---PVMESIALQGLNYGIHLVVS 969
Cdd:TIGR03925 161 RLFRTHGIDSMAQYRARRAAGRLP----EDPFGDVFLVIDGWGT-------LRQDFEdleDKVTDLAARGLAYGVHVVLT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 970 SSRWIAIRPAIKDLMQTRVEMRLGDLADTTFNthRNVVAAIPANRPGRCISTEGLHMLTALPRIDGVGDpnSAAEGLAAA 1049
Cdd:TIGR03925 230 ASRWSEIRPALRDLIGTRIELRLGDPMDSEID--RRAAARVPAGRPGRGLTPDGLHMLIALPRLDGIAS--VDDLGTRGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1050 AAEITQRYPGRRAPQVKLLPPQVGMDEVragwpVPQTLAQRLVVPFGVRESDLSPATIDFSVSTHFIVLGSTGSGKSTTL 1129
Cdd:TIGR03925 306 VAVIRDVWGGPPAPPVRLLPARLPLSAL-----PAGGGAPRLRVPLGLGESDLAPVYVDFAESPHLLIFGDSESGKTTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1130 AALLESIRRQYDPSQARVLLIDYRRRHLETVPQEMLIGHVTSERDVREALPALVEKMRSRRPPENVTPRQLAERSWWSGP 1209
Cdd:TIGR03925 381 RTIARGIVRRYSPDQARLVVVDYRRTLLGAVPEDYLAGYAATSAALTELIAALAALLERRLPGPDVTPQQLRARSWWSGP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1210 EVFVVIDDYHMVVQRGGmNPLEPLKEIIVDGRDTGLHVIAARNIAQADTALYDNVIGQMKNLNSSGLIMDGSKLDGILIG 1289
Cdd:TIGR03925 461 EIYVVVDDYDLVATGSG-NPLAPLVELLPHARDIGLHVVVARRSGGAARALMDPVLARLKDLGAPGLLLSGDRDEGPLLG 539
|
570 580
....*....|....*....|....*...
gi 2329068856 1290 DVRPTKQPPGRGIFVEPmSSRRDLVQVA 1317
Cdd:TIGR03925 540 GVRPRPLPPGRGVLVTR-GGGPQLIQVA 566
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
12-1272 |
7.12e-140 |
|
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: 460.22 E-value: 7.12e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 12 ELRLQPPTELPKPVPPSRMRMIMP-VVMVAAMCGMMVMMFRGggamnPMMLMFPAMMLVSM-FGMMGgaFAGNSSGGAAG 89
Cdd:TIGR03928 20 KVKISKPPQEPDKPKRGLLRIILPpLVMIAVTVLISIFQPRG-----IFIIASIAMSLVTIiFSTTT--YFREKKKYKKD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 90 LNEERKDYLRSITDNRKTVHAAEAELHAFLRYTHPGPDEIARLIGGK--RMWEVQVASPQFLRVRVGRGRIANQVRVIVP 167
Cdd:TIGR03928 93 VEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPSVEELKEMVENVnsRIWEKTPEHHDFLHVRLGTGNVPSSFEIKFP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 168 EAAPTSDLDPVgVVELTRFAKAYSTVGGMPVAINLLSAPqVGIDGDPELVAGLVRAMIAEVAVLHGPDQVAVAAVLSDPD 247
Cdd:TIGR03928 173 EEEFSQRKDEL-LDEAQELKEKYNTIENVPIVLDLSNGP-IGYVGKRSLVLEELQNLVGQLAFFHSYHDVQFVTIFPEEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 248 APEWSWLKWLPHSQHPsDNDAIGssrMVYRtvAELRTKVLAGLN--------RGPFSANSQPTLDRTHYLLIV------- 312
Cdd:TIGR03928 251 KKKWEWMRWLPHFWLR-DINVRG---FVYN--ERTRDQLLNSLYqilkerklALDDANSKEKKRFSPHYVFLItdrklil 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 313 -DVAGPASDRDISGIdGCTWLRLGATEQNLPRALRFAVS----EDGSLNEVTVRGLRRVGVADSLSTAAMTAMARSLSPY 387
Cdd:TIGR03928 325 dHVIMEYLNEDPSEL-GISLIFVQDVMESLPENVKTVIDiknrNEGEIVLEEGELVEKSFTPDHLDNEDLEEYSRTLAPL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 388 RLSTVVEAVAAEQASggtsWEEMVGIADPGNIRVEQVWvrRRDEDRARLNIPFGHDPAGSLVYLDIKESAEegmGPHGMC 467
Cdd:TIGR03928 404 NHLQNLKNSIPESVT----FLEMYGVKKVEELNIQERW--AKNETYKSLAVPIGLRGKDDIVYLNLHEKAH---GPHGLV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 468 IGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFKGGATFLGFERLSHVTAIVTNMEE---EADLVTrmedvINGEMAR 544
Cdd:TIGR03928 475 AGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFKNLPHLLGTITNLDGaqsMRALAS-----IKAELKK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 545 RQRILRDAgNFASVADYERAREQGADLRPLPTLLIILDEFAELLEQHPNFSKLFVAIGRLGRSLRIHLLLASQKvPANRM 624
Cdd:TIGR03928 550 RQRLFGEN-NVNHINQYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMKELVSTARIGRSLGVHLILATQK-PSGVV 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 625 -GELEAHLSYRVALRTNQTSDSRDAIGTADAYHLpKKPGSGYLRVGSGDL-QRFQAAYVGEKYTPPAQvsaasaqrarrp 702
Cdd:TIGR03928 628 dDQIWSNSRFKLALKVQDASDSNEILKTPDAAEI-TVPGRAYLQVGNNEVyELFQSAWSGAPYDPDKD------------ 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 703 gggyrppqrfTTGH--IADTRPAVVEPMVAQETPEAADGESI----TVMEAVLQQLAR-----HGQPAHKMWLPPLV--- 768
Cdd:TIGR03928 695 ----------KKEEedIYMINDLGQYELLNEDLSGLKRKKEIkevpTELEAVIDEIQAyteelNIEALPSPWLPPLEeki 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 769 ----TPPTLERMIRAVPQGALQMPVALVDKPRQQRQDVWSVDMSGAGgHMAIVGGTQSGKSTALQSFILSAALTHTPEQV 844
Cdd:TIGR03928 765 ylddLHAVEFDKLWSKPKEPLQATIGLLDDPELQSQEPLTLDLSKDG-HLAIFGSPGYGKSTFLQTLIMSLARQHSPEQL 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 845 QFYCLDFSGGGLAALTNLPHVGSVAAARDGDRIRRTIALVTNLLESRQSMFTEFGIDSIRKFRTLrdGGGTPPwqdrdpy 924
Cdd:TIGR03928 844 HFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKLFSEYGVASISMYNKA--SGEKLP------- 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 925 gDVFLVIDGWDvGFGtNGPYYDEYTPVMESIALQGLNYGIHLVVSSSRWIAIRPAIKDLMQTRVEMRLGDLADTtfnthR 1004
Cdd:TIGR03928 915 -QIVIIIDNYD-AVK-EEPFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLIDKSEY-----R 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1005 NVVAA---IPANRPGRcisteGLHML-------TALPRIDgvGDPNSAAEGLAAAAAEITQRYPGRRAPQVKLLPPQVGM 1074
Cdd:TIGR03928 987 SIVGRtkfTIEEIPGR-----GLIKKdeptlfqTALPVKG--EDDLEVIENIKAEIQKMNEAWTGERPKPIPMVPEELSL 1059
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1075 DEVRAGWPVPQTLAqRLVVPFGVRESDLSPATIDFSVSTHFIVLGSTGSGKSTTLAALLESIRRQYDPSqarVLLIDYR- 1153
Cdd:TIGR03928 1060 EEFRERYEVRKILE-EGSIPIGLDEETVEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQEKEK---IGLIDSId 1135
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1154 RRHLETVPQEMLIGHVTSERDVREALPALVEKMRSR-------RPPENVTPRQlaerswwsgPEVFVVIDDYHMVVQRGG 1226
Cdd:TIGR03928 1136 RGLLAYRDLKEVATYIEEKEDLKEILAELKEEIELReaaykeaLQNETGEPAF---------KPILLIIDDLEDFIQRTD 1206
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*.
gi 2329068856 1227 MNPLEPLKEIIVDGRDTGLHVIAARNIAQADTAlYDNVIGQMKNLN 1272
Cdd:TIGR03928 1207 LEIQDILALIMKNGKKLGIHFIVAGTHSELSKS-YDGVPKEIKQLR 1251
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
786-1033 |
3.93e-38 |
|
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: 142.52 E-value: 3.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 786 QMPVALvdkPRQQRQDVWSVDMSGAGGHMAIVGGTQSGKSTALQSFILSAALTHTPEQVQFYCLDFSGGGLAALTNLPHV 865
Cdd:pfam01580 16 RLPIAL---GKDISGNPEVFDLKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 866 GSVAAARDGDRIRRTIALVTNLLESRQSMFTEFGIDSIRKFRtlrDGGGTPPWqdrDPYGDVFLVIdgwdvgfgtngpyy 945
Cdd:pfam01580 93 LSVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYN---GEIAEDPL---DGFGDVFLVI-------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 946 deytpvmesialqglnYGIHLVVSSSRWIAIRPAIKDLMQTRVEMRLGDLADTtfnthrNVVAAIPANRPGRCISTEGLH 1025
Cdd:pfam01580 153 ----------------YGVHVMCTAGRWLEILPYLVVIVDERAELRLAAPKDS------EMRVEDAIVRLAQKGRAAGIH 210
|
....*...
gi 2329068856 1026 MLTALPRI 1033
Cdd:pfam01580 211 LLLATQRP 218
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
421-617 |
4.43e-32 |
|
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: 125.18 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 421 VEQVWVRRRDEDRARLNIPFGHDPAGSLVYLDIKESAEegmgpHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLV 500
Cdd:pfam01580 2 LEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPV-----HLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 501 DFKGGAtFLGFERLSHVTAIvtNMEEEADLVTRMEDVINGEMARRQRILRDAGnFASVADY--ERAR------------- 565
Cdd:pfam01580 77 DPKMGE-LSAYEDIPHLLSV--PVATDPKRALRALEWLVDEMERRYALFRALG-VRSIAGYngEIAEdpldgfgdvflvi 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2329068856 566 -------EQGADLRPLPTLLIILDEFAELLEQHPNFSK-----LFVAIGRLGRSLRIHLLLASQ 617
Cdd:pfam01580 153 ygvhvmcTAGRWLEILPYLVVIVDERAELRLAAPKDSEmrvedAIVRLAQKGRAAGIHLLLATQ 216
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
464-994 |
7.02e-29 |
|
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: 125.87 E-value: 7.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 464 HGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFkGGATFLGFERLSHVTAIVTNMEEE--ADLVTRMEDvingE 541
Cdd:TIGR03928 812 HLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDF-GTNGLLPLKKLPHVADYFTLDEEEkiEKLIRRIKK----E 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 542 MARRQRILRDAGnFASVADYERAREQgadlrPLPTLLIILDEFAELLEQH--PNFSKLFVAIGRLGRSLRIHLLLASQKV 619
Cdd:TIGR03928 887 IDRRKKLFSEYG-VASISMYNKASGE-----KLPQIVIIIDNYDAVKEEPfyEDFEELLIQLAREGASLGIYLVMTAGRQ 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 620 PANRMgELEAHLSYRVALRTNQTSDSRDAIGTADaYHLPKKPGSGYLRVGSGDLqrFQaAYVGEKYTPPAQVSAASAQRA 699
Cdd:TIGR03928 961 NAVRM-PLMNNIKTKIALYLIDKSEYRSIVGRTK-FTIEEIPGRGLIKKDEPTL--FQ-TALPVKGEDDLEVIENIKAEI 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 700 RRPGGGYrppqrfttghiADTRPAVVePMVaqetPeaadgESITVMEAVlqqlarhGQPAHKMWLPplvtpptlermira 779
Cdd:TIGR03928 1036 QKMNEAW-----------TGERPKPI-PMV----P-----EELSLEEFR-------ERYEVRKILE-------------- 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 780 vpqgALQMPVALvdkprqQRQDVWSVDMS-GAGGHMAIVGGTQSGKSTALQSFILSAALThtpEQVQFYCLDFSGGGLAA 858
Cdd:TIGR03928 1074 ----EGSIPIGL------DEETVEPVYIDlTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGLIDSIDRGLLA 1140
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 859 LTNLPHVGSVAAARDGdrIRRTIALVTNLLESRQSMFTEfgidsirkfrTLRDGGGTPPWQdrdpygDVFLVIDGWDvGF 938
Cdd:TIGR03928 1141 YRDLKEVATYIEEKED--LKEILAELKEEIELREAAYKE----------ALQNETGEPAFK------PILLIIDDLE-DF 1201
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2329068856 939 GTNgpYYDEYTPVMESIALQGLNYGIHLVVS------SSRWIAIRPAIKDLMQTRVEMRLGD 994
Cdd:TIGR03928 1202 IQR--TDLEIQDILALIMKNGKKLGIHFIVAgthselSKSYDGVPKEIKQLRTGILGMRKSD 1261
|
|
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
431-684 |
2.63e-20 |
|
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: 96.92 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 431 EDRARLNIPFGHDPAGSLVYLDIKEsaeegMgPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFKgGATFLG 510
Cdd:COG1674 256 NSKSPLPIALGKDISGEPVVADLAK-----M-PHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPK-MVELSV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 511 FERLSH-VTAIVTNMEEEAD----LVtrmedvinGEMARRQRILRDAG--NFAS----VADYERAREQGADLRPLPTLLI 579
Cdd:COG1674 329 YNGIPHlLTPVVTDPKKAANalkwAV--------REMERRYKLFAKAGvrNIAGynekVREAKAKGEEEEGLEPLPYIVV 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 580 ILDEFAELL-------EQhpnfsklfvAIGRL---GRSLRIHLLLASQK-------------VPAnrmgeleahlsyRVA 636
Cdd:COG1674 401 IIDELADLMmvagkevEE---------AIARLaqkARAAGIHLILATQRpsvdvitglikanIPS------------RIA 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2329068856 637 LRTNQTSDSRDAIGTADAYHLpkkPGSG---YLRVGSGDLQRFQAAYVGEK 684
Cdd:COG1674 460 FAVSSKIDSRTILDQGGAEKL---LGRGdmlFLPPGASKPIRVQGAFVSDE 507
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
460-968 |
5.97e-18 |
|
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: 89.28 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 460 GMGPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFkGGATFLGFERLSHVTAIVTNMEEEadLVTRMEDVIN 539
Cdd:TIGR03925 77 GAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDF-GGGGLASLADLPHVGGVAGRLDPE--RVRRTVAEVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 540 GEMARRQRILRDAGnFASVADYERAREQGaDLRPLP---TLLIIlDEFAELLEQHPNFSKLFVAIGRLGRSLRIHLLLAS 616
Cdd:TIGR03925 154 GLLRRRERLFRTHG-IDSMAQYRARRAAG-RLPEDPfgdVFLVI-DGWGTLRQDFEDLEDKVTDLAARGLAYGVHVVLTA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 617 QKVPANRMGeLEAHLSYRVALRTNQTSDSRdaIGTADAYHLP-KKPGSGYlrvgSGDLQRFQAAYvgekytpPAQVSAAS 695
Cdd:TIGR03925 231 SRWSEIRPA-LRDLIGTRIELRLGDPMDSE--IDRRAAARVPaGRPGRGL----TPDGLHMLIAL-------PRLDGIAS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 696 AQRARRPGGGYRppqrfttghIADTRPAVVEPMVaqetpeaadgesitvmeavlqqlarhgqpahKMwLPPLVTPptlER 775
Cdd:TIGR03925 297 VDDLGTRGLVAV---------IRDVWGGPPAPPV-------------------------------RL-LPARLPL---SA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 776 MIRAVPQGALQMPVALvdkpRQQRQDVWSVDMsGAGGHMAIVGGTQSGKSTALQSFILSAALTHTPEQVQFYCLDFSGGG 855
Cdd:TIGR03925 333 LPAGGGAPRLRVPLGL----GESDLAPVYVDF-AESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRTL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 856 LAAltnLPHVGSVAAARDGDRIRRTIALVTNLLESRqsmftefgidsirkfrtlRDGGGTPPWQ--DRDPYG--DVFLVI 931
Cdd:TIGR03925 408 LGA---VPEDYLAGYAATSAALTELIAALAALLERR------------------LPGPDVTPQQlrARSWWSgpEIYVVV 466
|
490 500 510
....*....|....*....|....*....|....*...
gi 2329068856 932 DGWD-VGFGTNGPyydeYTPVMESIAlQGLNYGIHLVV 968
Cdd:TIGR03925 467 DDYDlVATGSGNP----LAPLVELLP-HARDIGLHVVV 499
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
811-1302 |
5.17e-17 |
|
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: 87.35 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 811 GGHMAIVGGTQSGKSTALQSFILSAALTHTPEQVQFYCLDFSGGGLAAL-TNLPH-VGSVAAArDGDRIRRTIALVTNLL 888
Cdd:TIGR03928 469 GPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLfKNLPHlLGTITNL-DGAQSMRALASIKAEL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 889 ESRQSMFTEFGIDSIRKFRTLRDGGgtppwQDRDPYGDVFLVIDgwdvGFG---TNGP-YYDEYTpvmeSIALQGLNYGI 964
Cdd:TIGR03928 548 KKRQRLFGENNVNHINQYQKLYKQG-----KAKEPMPHLFLISD----EFAelkSEQPeFMKELV----STARIGRSLGV 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 965 HL---------VV-----SSSRW-IAIRpaIKDLMQTRVEMRLGDLADTTfNTHR-------NVV--------AAIPANR 1014
Cdd:TIGR03928 615 HLilatqkpsgVVddqiwSNSRFkLALK--VQDASDSNEILKTPDAAEIT-VPGRaylqvgnNEVyelfqsawSGAPYDP 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1015 PGRCISTEGLHMLTAL-------PRIDGVGDPNSAAEGLAAAAAEIT--QRYPGRRA------PQVKLLPPQVGMDEVRA 1079
Cdd:TIGR03928 692 DKDKKEEEDIYMINDLgqyellnEDLSGLKRKKEIKEVPTELEAVIDeiQAYTEELNiealpsPWLPPLEEKIYLDDLHA 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1080 --GWPVPQTLAQRLVVPFG----VRESDLSPATIDFSVSTHFIVLGSTGSGKSTTLAALLESIRRQYDPSQARVLLIDYR 1153
Cdd:TIGR03928 772 veFDKLWSKPKEPLQATIGllddPELQSQEPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFG 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1154 RRHL----------------ETVPQEMLIGHVTSERDVREALPALVE----KMRSRRPPENVtprqlaerswwsgPEVFV 1213
Cdd:TIGR03928 852 TNGLlplkklphvadyftldEEEKIEKLIRRIKKEIDRRKKLFSEYGvasiSMYNKASGEKL-------------PQIVI 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1214 VIDDYHMVVQRGGMNPLEPLKEIIV-DGRDTGLHVIAArniAQADTALYDNVIGQMKnLNSSGLIMDGSKLDGILiGDVR 1292
Cdd:TIGR03928 919 IIDNYDAVKEEPFYEDFEELLIQLArEGASLGIYLVMT---AGRQNAVRMPLMNNIK-TKIALYLIDKSEYRSIV-GRTK 993
|
570
....*....|.
gi 2329068856 1293 PTKQP-PGRGI 1302
Cdd:TIGR03928 994 FTIEEiPGRGL 1004
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
368-694 |
1.71e-12 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 72.43 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 368 VADSLSTAAMTAMARSLSpYRLSTVveAVAAEQASGGTSWeemVGIADPgNIRVEQVWVR------RRDEDRARLNIPFG 441
Cdd:PRK10263 923 LAPGVKAARISNLSRDLA-RSLSTV--AVRVVEVIPGKPY---VGLELP-NKKRQTVYLRevldnaKFRDNPSPLTVVLG 995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 442 HDPAGSLVYLDIKESaeegmgPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFKGGATFLgFERLSH-VTAI 520
Cdd:PRK10263 996 KDIAGEPVVADLAKM------PHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSV-YEGIPHlLTEV 1068
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 521 VTNMEEEADlvtRMEDVINgEMARRQRILRDAG--NFASVAD--YERAR-----------------EQGADLRPLPTLLI 579
Cdd:PRK10263 1069 VTDMKDAAN---ALRWCVN-EMERRYKLMSALGvrNLAGYNEkiAEADRmmrpipdpywkpgdsmdAQHPVLKKEPYIVV 1144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 580 ILDEFAELLEQ-HPNFSKLFVAIGRLGRSLRIHLLLASQKVPANRM-GELEAHLSYRVALRTNQTSDSRDAIGTADAYHL 657
Cdd:PRK10263 1145 LVDEFADLMMTvGKKVEELIARLAQKARAAGIHLVLATQRPSVDVItGLIKANIPTRIAFTVSSKIDSRTILDQAGAESL 1224
|
330 340 350
....*....|....*....|....*....|....*..
gi 2329068856 658 pkkpgsgylrVGSGDLqrfqaAYVGEKYTPPAQVSAA 694
Cdd:PRK10263 1225 ----------LGMGDM-----LYSGPNSTLPVRVHGA 1246
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
809-972 |
1.46e-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: 59.22 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 809 GAGGHMAIVGGTQSGKSTALQSFILSAALTHTPEQVQFYCLDFSGG-GLAALTNLPHVGSV----AAARD-GDRIRRTIA 882
Cdd:TIGR03924 433 GMGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKGGaTFLGLEGLPHVSAVitnlADEAPlVDRMQDALA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 883 lvtNLLESRQSMFTEFG-IDSIRKFRTLRDGGgtppwQDRDPYGDVFLVIDgwdvGFG---TNGPyydEYTPVMESIALQ 958
Cdd:TIGR03924 513 ---GEMNRRQELLRAAGnFANVAEYEKARAAG-----ADLPPLPALFVVVD----EFSellSQHP---DFADLFVAIGRL 577
|
170
....*....|....
gi 2329068856 959 GLNYGIHLVVSSSR 972
Cdd:TIGR03924 578 GRSLGVHLLLASQR 591
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
1090-1189 |
3.23e-08 |
|
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: 55.46 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1090 RLVVPFGVRESDlSPATIDFSVST-HFIVLGSTGSGKSTTLAALLESIRRQYDPSQARVLLIDYRRRHLETVPQEMLIGH 1168
Cdd:pfam01580 16 RLPIALGKDISG-NPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLS 94
|
90 100
....*....|....*....|....
gi 2329068856 1169 V---TSERDVREALPALVEKMRSR 1189
Cdd:pfam01580 95 VpvaTDPKRALRALEWLVDEMERR 118
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
1104-1152 |
1.88e-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: 51.92 E-value: 1.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2329068856 1104 PATIDFS--VSTHFIVLGSTGSGKSTTLAALLESIRRQydpsQARVLLIDY 1152
Cdd:COG0433 37 PVYLDLDklLNRHILILGATGSGKSNTLQVLLEELSRA----GVPVLVFDP 83
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
1103-1151 |
9.56e-06 |
|
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: 48.13 E-value: 9.56e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2329068856 1103 SPATIDFS--VSTHFIVLGSTGSGKSTTLAALLESIRRQYDpsqARVLLID 1151
Cdd:pfam01935 12 VPVYLDVNklVSRHFAILGSTGSGKSNTVAVLLEELLEKKG---ATVLIFD 59
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
429-545 |
1.23e-05 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 49.61 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 429 RDEDRARLNIPFGHDPAG-SLVYLDIKESaeegmgPHGMCIGATGSGKSEFLRTLVLSAVATHSPDVLNLLLVDFkggat 507
Cdd:TIGR03925 335 AGGGAPRLRVPLGLGESDlAPVYVDFAES------PHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDY----- 403
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2329068856 508 flgfeRLSHVTAIVTNMEEE----ADLVTRMEDVINGEMARR 545
Cdd:TIGR03925 404 -----RRTLLGAVPEDYLAGyaatSAALTELIAALAALLERR 440
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1107-1179 |
1.21e-04 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 43.79 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1107 IDFSVS---THFIVlGSTGSGKSTtlaaLLESIRRQYDPSQARVLL---------IDYRRRHLETVPQEM-LIGHVTSER 1173
Cdd:pfam00005 4 VSLTLNpgeILALV-GPNGAGKST----LLKLIAGLLSPTEGTILLdgqdltddeRKSLRKEIGYVFQDPqLFPRLTVRE 78
|
....*.
gi 2329068856 1174 DVREAL 1179
Cdd:pfam00005 79 NLRLGL 84
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
449-609 |
1.61e-04 |
|
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: 45.75 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 449 VYLDIKESaeegMGPHGMCIGATGSGKSEFLRTLVLSAVATHSPdvlnLLLVDFKG---GATFLGFERLShVTAIVTNME 525
Cdd:COG0433 38 VYLDLDKL----LNRHILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDPHGeysGLAEPGAERAD-VGVFDPGAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 526 EEA-----DLVTRMEDV-----INGEMARRQR-ILRDAgnfasvadYERAREQGADLRPLPTLLIILDEFAELLEQHPNF 594
Cdd:COG0433 109 RPLpinpwDLFATASELgplllSRLDLNDTQRgVLREA--------LRLADDKGLLLLDLKDLIALLEEGEELGEEYGNV 180
|
170
....*....|....*
gi 2329068856 595 SKlfVAIGRLGRSLR 609
Cdd:COG0433 181 SA--ASAGALLRRLE 193
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1104-1189 |
1.71e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.23 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1104 PATIDFSVSTHFIVLGSTGSGKSTTLAALLESIRRQYDPSQARVLLIDYRRRHL---ETVPQeMLIGHVTSERDVREALP 1180
Cdd:PRK10263 1002 PVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELsvyEGIPH-LLTEVVTDMKDAANALR 1080
|
....*....
gi 2329068856 1181 ALVEKMRSR 1189
Cdd:PRK10263 1081 WCVNEMERR 1089
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1119-1163 |
3.49e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 43.68 E-value: 3.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2329068856 1119 GSTGSGKSTTLaALLEsirRQYDPSQARVLL---------IDYRRRHLETVPQE 1163
Cdd:cd03249 36 GSSGCGKSTVV-SLLE---RFYDPTSGEILLdgvdirdlnLRWLRSQIGLVSQE 85
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1107-1166 |
4.02e-04 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 42.76 E-value: 4.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2329068856 1107 IDFSV---STHFIVlGSTGSGKSTTLAALLesirRQYDPSQARVLL---------IDYRRRHLETVPQEMLI 1166
Cdd:cd03228 21 VSLTIkpgEKVAIV-GPSGSGKSTLLKLLL----RLYDPTSGEILIdgvdlrdldLESLRKNIAYVPQDPFL 87
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
1103-1151 |
4.16e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 44.55 E-value: 4.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2329068856 1103 SPATIDFSVST---HFIVLGSTGSGKSTTLAALLESIRRQydpsQARVLLID 1151
Cdd:COG3451 192 TPVFFDFHDGLdngNTLILGPSGSGKSFLLKLLLLQLLRY----GARIVIFD 239
|
|
| 5TM_YidC_Alb3 |
cd20070 |
Five transmembrane core domain of membrane protein insertase YidC, Alb3, and similar proteins; ... |
33-74 |
5.53e-04 |
|
Five transmembrane core domain of membrane protein insertase YidC, Alb3, and similar proteins; This group is composed of the bacterial and chloroplastic members of the YidC/Oxa1/Alb3 protein family of insertases, including bacterial YidC, and chloroplastic ALBINO3 (Alb3) and Alb3-like proteins such as ALBINO3-like protein 1 (also called Alb4). Membrane protein insertase YidC, also called foldase YidC or membrane integrase YidC, facilitates proper folding, insertion, and assembly of inner membrane proteins and complexes. Depending on the nature of the substrate, YidC functions in a Sec-independent (YidC only) or a Sec-dependent manner as part of a complex containing YidC, the SecYEG channel, and SecDFYajC. YidC from Gram-negative bacteria contains an extra transmembrane segment (TM1) at the N-terminus and a large periplasmic domain, located between TM1 and TM2, that adopts a beta-super sandwich fold that is found in sugar-binding proteins such as galactose mutarotase. Alb3 and Alb3-like proteins are required for the post-translational insertion of the light-harvesting chlorophyll-binding proteins (LHCPs) into the chloroplast thylakoid membrane. Alb3 acts independently and may also function cooperatively with the thylakoid cpSecYE translocase to insert proteins co-translationally into the thylakoid membrane, similar to bacterial YidC that can function with the SecYEG translocase. YidC/Oxa1/Alb3 family insertases contain a core domain of five transmembrane (5TM) segments that is essential to insertase function.
Pssm-ID: 410994 [Multi-domain] Cd Length: 181 Bit Score: 42.37 E-value: 5.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2329068856 33 IMPVVMVAAMCGMMVMMFRGGGAMNP----MMLMFPAMMLVSMFGM 74
Cdd:cd20070 112 ILPILMGVTMFLQQKLTPTPTDDQAPqqkmMMYFMPVMFTFIFLSF 157
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1114-1252 |
8.09e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1114 HFIVLGSTGSGKSTTLAALLesirRQYDPSQARVLLIDyrrrhLETVPQEMLIGHVTSERDVREALPALVEKMRSRrppe 1193
Cdd:smart00382 4 VILIVGPPGSGKTTLARALA----RELGPPGGGVIYID-----GEDILEEVLDQLLLIIVGGKKASGSGELRLRLA---- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2329068856 1194 nvtpRQLAERswwSGPEVfVVIDDYHM---VVQRGGMNPLEPLKEIIVDGRDTGLHVIAARN 1252
Cdd:smart00382 71 ----LALARK---LKPDV-LILDEITSlldAEQEALLLLLEELRLLLLLKSEKNLTVILTTN 124
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1116-1163 |
1.68e-03 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 42.84 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2329068856 1116 IVlGSTGSGKStTLAALLEsirRQYDPSQARVLL--IDYR-------RRHLETVPQE 1163
Cdd:COG1132 371 LV-GPSGSGKS-TLVNLLL---RFYDPTSGRILIdgVDIRdltleslRRQIGVVPQD 422
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
1115-1138 |
2.07e-03 |
|
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.
Pssm-ID: 410875 [Multi-domain] Cd Length: 223 Bit Score: 41.37 E-value: 2.07e-03
10 20
....*....|....*....|....
gi 2329068856 1115 FIVLGSTGSGKSTTLAALLESIRR 1138
Cdd:cd01131 24 VLVTGPTGSGKSTTLAAMIDYINE 47
|
|
| TrwB_AAD_bind |
pfam10412 |
Type IV secretion-system coupling protein DNA-binding domain; The plasmid conjugative coupling ... |
1105-1151 |
3.36e-03 |
|
Type IV secretion-system coupling protein DNA-binding domain; The plasmid conjugative coupling protein TrwB forms hexamers from six structurally very similar protomers. This hexamer contains a central channel running from the cytosolic pole (made up by the AADs) to the membrane pole ending at the transmembrane pore shaped by 12 transmembrane helices, rendering an overall mushroom-like structure. The TrwB_AAD (all-alpha domain) domain appears to be the DNA-binding domain of the structure. TrwB, a basic integral inner-membrane nucleoside-triphosphate-binding protein, is the structural prototype for the type IV secretion system coupling proteins, a family of proteins essential for macromolecular transport between cells and export.
Pssm-ID: 431268 [Multi-domain] Cd Length: 386 Bit Score: 41.51 E-value: 3.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1105 ATIDFSVST---HFIVLGSTGSGKSTTLAALLESIRRQYDpsqaRVLLID 1151
Cdd:pfam10412 5 AGVPLPKRSetrHTLIIGTTGSGKTQALRGLLDQARARGD----RAIIFD 50
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
1114-1153 |
3.45e-03 |
|
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: 39.51 E-value: 3.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2329068856 1114 HFIVLGSTGSGKSTTLAALLESIRRQ------YDPSQARVLLIDYR 1153
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARggsviiTDPKGELFLVIPDR 46
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1116-1178 |
4.33e-03 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 1116 IVlGSTGSGKSTTLAALLesirRQYDPSQARVLL---------IDYRRRHLETVPQEMLIGHVT------------SERD 1174
Cdd:cd03253 32 IV-GPSGSGKSTILRLLF----RFYDVSSGSILIdgqdirevtLDSLRRAIGVVPQDTVLFNDTigynirygrpdaTDEE 106
|
....
gi 2329068856 1175 VREA 1178
Cdd:cd03253 107 VIEA 110
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1117-1163 |
5.85e-03 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 39.88 E-value: 5.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2329068856 1117 VLGSTGSGKSTTLAALLesirRQYDPSQARVLL--IDYR-------RRHLETVPQE 1163
Cdd:cd03245 35 IIGRVGSGKSTLLKLLA----GLYKPTSGSVLLdgTDIRqldpadlRRNIGYVPQD 86
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
464-617 |
6.58e-03 |
|
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: 38.35 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2329068856 464 HGMCIGATGSGKSEFLRTLVLSAVATHSPdvlnLLLVDFKgGATFLGF-ERLSHVTAIVTnmeeeadLVTRMEDVINGEM 542
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQAARGGS----VIITDPK-GELFLVIpDRDDSFAALRA-------LFFNQLFRALTEL 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2329068856 543 ARRQRILRDagnfasvadyerareqgadlrplPTLLIILDEFAeLLEQHPNFSKLfvaIGRlGRSLRIHLLLASQ 617
Cdd:cd01127 69 ASLSPGRLP-----------------------RRVWFILDEFA-NLGRIPNLPNL---LAT-GRKRGISVVLILQ 115
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
1116-1136 |
7.16e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 40.07 E-value: 7.16e-03
|
| |
