|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-492 |
1.12e-132 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 396.74 E-value: 1.12e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 15 AFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLP--------DAIFP-- 82
Cdd:COG0488 7 SFGgrPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPldddltvlDTVLDgd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 83 ------LTMLDAVLAQLPLAERDSLRW-----------------KAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARA 139
Cdd:COG0488 87 aelralEAELEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 140 LIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKTLHYFalPCT--------AAR 211
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLY--PGNysayleqrAER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 212 KALEAKDESDAQRHKAEQKE-IDRVTASAKRlatwgkvydnedlARKAKQMEKQVERLKESQTALTAGSQwTLTLRGDAL 290
Cdd:COG0488 245 LEQEAAAYAKQQKKIAKEEEfIRRFRAKARK-------------AKQAQSRIKALEKLEREEPPRRDKTV-EIRFPPPER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 291 RADRLLEMENLSVppAPGLPPLF-NIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWQQfadESAESG-LKIHPRVSPGYYD 368
Cdd:COG0488 311 LGKKVLELEGLSK--SYGDKTLLdDLSL-RIDRGDRIGLIGPNGAGKSTLLKLLAGE---LEPDSGtVKLGETVKIGYFD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 369 QTLNQLPDDATLLDALEPFAPDPQNRK-MALISA-GFPWSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLD 446
Cdd:COG0488 385 QHQEELDPDKTVLDELRDGAPGGTEQEvRGYLGRfLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 556426975 447 MEGKEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEW 492
Cdd:COG0488 465 IETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-567 |
1.01e-62 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 217.73 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPdaIFPLTMLDA 88
Cdd:PRK10636 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETP--ALPQPALEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VL----------AQLPLA-ERD------------------SLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARA 139
Cdd:PRK10636 84 VIdgdreyrqleAQLHDAnERNdghaiatihgkldaidawTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 140 LIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKTL-----HYFALPCTAARK-- 212
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLfeytgNYSSFEVQRATRla 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 213 ALEAKDESDAQRHKAEQKEIDRVTASAKrlatwgkvydnedlarKAKQMEKQVERLKESQTALTA--GSQWTLTLRGDAL 290
Cdd:PRK10636 244 QQQAMYESQQERVAHLQSYIDRFRAKAT----------------KAKQAQSRIKMLERMELIAPAhvDNPFHFSFRAPES 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 291 RADRLLEMENLSVppAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHPRVspGYYDQ- 369
Cdd:PRK10636 308 LPNPLLKMEKVSA--GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL--GYFAQh 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 370 TLNQLPDDATLLDALEPFAPDPQNRKMALISAGFPWsrHGQKIST----LSGGERSRLLFVGLTLARYSLLMLDEPTNHL 445
Cdd:PRK10636 384 QLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGF--QGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 446 DMEGKEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLS----------EW--------------------HDA 495
Cdd:PRK10636 462 DLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEpfdgdledyqQWlsdvqkqenqtdeapkennaNSA 541
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 496 EAVFERLRESAGLATSTAPVIDTAAVQPSPYDDLLERLVALETLLED----DLARKPK-HQKPHLQAQWRKEIEEIE 567
Cdd:PRK10636 542 QARKDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDselyDQSRKAElTACLQQQASAKSGLEECE 618
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
16-493 |
2.38e-58 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 203.20 E-value: 2.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 16 FGT--LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALA--------------------------GHC 67
Cdd:PRK15064 11 FGAkpLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlgklrqdqfafeeftvldtvimGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 68 LMARVEQHlPDAIFPLT-------MLDAVLaQLPLAERD--SLRWKAETLLAGMGF-TPQDMALQSAtLSGGQHTRLLLA 137
Cdd:PRK15064 91 ELWEVKQE-RDRIYALPemseedgMKVADL-EVKFAEMDgyTAEARAGELLLGVGIpEEQHYGLMSE-VAPGWKLRVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 138 RALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTN-------GSWILRDKTLHYFALPCTAA 210
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCThmadldyGELRVYPGNYDEYMTAATQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 211 RKALEAkdesDAQRHKAEQKE----IDRVTASAK--RLATwgkvydnedlaRKAKQMEK-QVERLKESqtaltagSQWTL 283
Cdd:PRK15064 248 RERLLA----DNAKKKAQIAElqsfVSRFSANASkaKQAT-----------SRAKQIDKiKLEEVKPS-------SRQNP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 284 TLRGDALRA-DRL-LEMENLSvpPAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIwqqFADESAESG-LKIHP 360
Cdd:PRK15064 306 FIRFEQDKKlHRNaLEVENLT--KGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL---VGELEPDSGtVKWSE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 361 RVSPGYYDQ-TLNQLPDDATLLDALEPFAPDPQNRKMALISAG---FPWSRHGQKISTLSGGERSRLLFVGLTLARYSLL 436
Cdd:PRK15064 381 NANIGYYAQdHAYDFENDLTLFDWMSQWRQEGDDEQAVRGTLGrllFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 437 MLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWH 493
Cdd:PRK15064 461 VMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFS 517
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-471 |
1.43e-56 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 199.01 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 22 SLSFTlkKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALA----------------GHCLMARVEQHLPDAIFPLTM 85
Cdd:TIGR03719 25 SLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvgylpqepqldpTKTVRENVEEGVAEIKDALDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 LDAVLAQL--PLAERDSLRWKAETLL----AGMGFTPQ---DMALQS----------ATLSGGQHTRLLLARALIHDPDL 146
Cdd:TIGR03719 103 FNEISAKYaePDADFDKLAAEQAELQeiidAADAWDLDsqlEIAMDAlrcppwdadvTKLSGGERRRVALCRLLLSKPDM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 147 LLLDEPSNHLDLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTNgsWIL---RDKTLHYFA-----LPCTAARKALEAKD 218
Cdd:TIGR03719 183 LLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILeldRGRGIPWEGnysswLEQKQKRLEQEEKE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 219 ESdaQRHKAEQKEIDRVTASAKrlatwgkvydnedlARKAKQmEKQVERLKESQTALTAGSQWTLTLR---GDALrADRL 295
Cdd:TIGR03719 261 ES--ARQKTLKRELEWVRQSPK--------------GRQAKS-KARLARYEELLSQEFQKRNETAEIYippGPRL-GDKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSvpPAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIWQQfadESAESG-LKIHPRVSPGYYDQTLNQL 374
Cdd:TIGR03719 323 IEAENLT--KAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ---EQPDSGtIEIGETVKLAYVDQSRDAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 375 PDDATL-------LDALEPFAPDPQNRkmALISA-GFPWSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLD 446
Cdd:TIGR03719 398 DPNKTVweeisggLDIIKLGKREIPSR--AYVGRfNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
490 500
....*....|....*....|....*
gi 556426975 447 MEGKEALAQTLQQFEGGVLLVSHDR 471
Cdd:TIGR03719 476 VETLRALEEALLNFAGCAVVISHDR 500
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-558 |
5.94e-56 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 199.02 E-value: 5.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 15 AFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDG---------------------TDSP--AAGTV-------- 61
Cdd:PRK11147 12 SFSdaPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqQDPPrnVEGTVydfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 62 -ALAG-----HCLMARVEQHLPDAIfpLTMLDAVLAQLPLAERDSLRWKAETLLAGMGFTPqDMALQSatLSGGQHTRLL 135
Cdd:PRK11147 92 eEQAEylkryHDISHLVETDPSEKN--LNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP-DAALSS--LSGGWLRKAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 136 LARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVtnGSWIL---RDKTLHYfalPCTAArK 212
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNM--ATRIVdldRGKLVSY---PGNYD-Q 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 213 ALEAKDEsdAQRHKAEQK-EIDRVTAS----------AKRLATWGKVydnedlaRKAKQMekQVERLKESQTALTAGSQW 281
Cdd:PRK11147 241 YLLEKEE--ALRVEELQNaEFDRKLAQeevwirqgikARRTRNEGRV-------RALKAL--RRERSERREVMGTAKMQV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 282 tltlrGDALRADRLL-EMENLSVP-PAPGLPPLFNIEMARlksGDRVAIVGRNGCGKSSLMRLIWQQFAdesAESGlKIH 359
Cdd:PRK11147 310 -----EEASRSGKIVfEMENVNYQiDGKQLVKDFSAQVQR---GDKIALIGPNGCGKTTLLKLMLGQLQ---ADSG-RIH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 360 --PRVSPGYYDQTLNQLPDDATLLDALepfAPDPQN-----RKMALISA----GFPWSRHGQKISTLSGGERSRLLFVGL 428
Cdd:PRK11147 378 cgTKLEVAYFDQHRAELDPEKTVMDNL---AEGKQEvmvngRPRHVLGYlqdfLFHPKRAMTPVKALSGGERNRLLLARL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 429 TLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIE-EGKLSE----WHDAE---AVFE 500
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRyvggYHDARqqqAQYL 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 501 RLRESAGLATSTAPVIDTAAVQPSP----YDDL--LERLVALETLLEDDLARkpkhqkphLQAQ 558
Cdd:PRK11147 535 ALKQPAVKKKEEAAAPKAETVKRSSkklsYKLQreLEQLPQLLEDLEAEIEA--------LQAQ 590
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-505 |
5.63e-53 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 192.38 E-value: 5.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLK-----VLDG---------TDSPAAGTVALAGHCLM-------------AR 71
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGipkncqilhVEQEVVGDDTTALQCVLntdiertqlleeeAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 72 VEQHLPDAIFPLTM-------------------LDAVLAQLPLAERDSLRWKAETLLAGMGFTPQDMALQSATLSGGQHT 132
Cdd:PLN03073 272 LVAQQRELEFETETgkgkgankdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRM 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 133 RLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKTLH-----YFALPC 207
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVtykgdYDTFER 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 208 TAA------RKALEAKDESDAQRhkaeQKEIDRVTASAKRlatwgkvydnedlARKAKQMEKQVERLKESqtaltagsqw 281
Cdd:PLN03073 432 TREeqlknqQKAFESNERSRSHM----QAFIDKFRYNAKR-------------ASLVQSRIKALDRLGHV---------- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 282 tltlrgDALRADRLLEME-----NLSVPPA----------PGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIwqq 346
Cdd:PLN03073 485 ------DAVVNDPDYKFEfptpdDRPGPPIisfsdasfgyPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI--- 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 347 FADESAESGLKIH-PRVSPGYYDQ------TLNQLPddatLLDALEPFAPDPQNRKMA-LISAGFPWSRHGQKISTLSGG 418
Cdd:PLN03073 556 SGELQPSSGTVFRsAKVRMAVFSQhhvdglDLSSNP----LLYMMRCFPGVPEQKLRAhLGSFGVTGNLALQPMYTLSGG 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 419 ERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAV 498
Cdd:PLN03073 632 QKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHD 711
|
....*..
gi 556426975 499 FERLRES 505
Cdd:PLN03073 712 YKKTLQS 718
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-471 |
3.76e-52 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 187.25 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 22 SLSFTlkKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALA----------------GHCLMARVEQHLPDAIFPLTM 85
Cdd:PRK11819 27 SLSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApgikvgylpqepqldpEKTVRENVEEGVAEVKAALDR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 LDAVLAQL--PLAERDSLR---------------WKAETLLagmgftpqDMALQS----------ATLSGGQHTRLLLAR 138
Cdd:PRK11819 105 FNEIYAAYaePDADFDALAaeqgelqeiidaadaWDLDSQL--------EIAMDAlrcppwdakvTKLSGGERRRVALCR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 139 ALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTNgsWIL---RDKTLHYFA-----LPCTAA 210
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILeldRGRGIPWEGnysswLEQKAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 211 RKALEAKdeSDAQRHKAEQKEIDRVTASAK--------RLATwgkvYD---NEDLARKAKQMEKQV---ERLkesqtalt 276
Cdd:PRK11819 255 RLAQEEK--QEAARQKALKRELEWVRQSPKarqakskaRLAR----YEellSEEYQKRNETNEIFIppgPRL-------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 277 aGSQwtlTLRGDALR---ADRLLeMENLS--VPPapglpplfniemarlksGDRVAIVGRNGCGKSSLMRLIWQQfadES 351
Cdd:PRK11819 321 -GDK---VIEAENLSksfGDRLL-IDDLSfsLPP-----------------GGIVGIIGPNGAGKSTLFKMITGQ---EQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 352 AESG-LKIHPRVSPGYYDQTLNQLPDDATL-------LDALEpfapdPQNRKM---ALISA-GFPWSRHGQKISTLSGGE 419
Cdd:PRK11819 376 PDSGtIKIGETVKLAYVDQSRDALDPNKTVweeisggLDIIK-----VGNREIpsrAYVGRfNFKGGDQQKKVGVLSGGE 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 556426975 420 RSRlLFVGLTLARYS-LLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDR 471
Cdd:PRK11819 451 RNR-LHLAKTLKQGGnVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDR 502
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-203 |
3.50e-49 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 178.33 E-value: 3.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 3 TLLTAQSLRVdtAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLpDAI 80
Cdd:COG0488 314 KVLELEGLSK--SYGdkTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 81 FP-LTMLDAVLAQLPLAERDSLRwkaeTLLAGMGFTPqDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDL 158
Cdd:COG0488 391 DPdKTVLDELRDGAPGGTEQEVR----GYLGRFLFSG-DDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556426975 159 PTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKTLHYF 203
Cdd:COG0488 466 ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-199 |
4.52e-47 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 161.46 E-value: 4.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQhlpdaifplt 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 mldavlaqlplaerdslrwkaetllagmgftpqdmalqsatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWL 164
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 556426975 165 EHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKT 199
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
296-488 |
6.08e-44 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 152.99 E-value: 6.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVppAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAEsgLKIHPRVSPGYYDQtlnqlp 375
Cdd:cd03221 1 IELENLSK--TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVKIGYFEQ------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 376 ddatlldalepfapdpqnrkmalisagfpwsrhgqkistLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQ 455
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 456 TLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
298-492 |
1.51e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 139.81 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 298 MENLSVppAPGLPPLF-NIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfA-DESAESG-LKIHPRVSPGYYDQTLnQL 374
Cdd:COG0488 1 LENLSK--SFGGRPLLdDVSL-SINPGDRIGLVGRNGAGKSTLLKIL----AgELEPDSGeVSIPKGLRIGYLPQEP-PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 375 PDDATLLDAL-------------------EPFAPDPQNRKMALISA---------------------GFPWSRHGQKIST 414
Cdd:COG0488 73 DDDLTVLDTVldgdaelraleaeleeleaKLAEPDEDLERLAELQEefealggweaearaeeilsglGFPEEDLDRPVSE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 415 LSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEW 492
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLY 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-181 |
5.42e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 118.22 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MAR----V 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsrreLARriayV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 73 EQHLPDAiFPLTMLDAV-LAQLP-------LAERDslRWKAETLLAGMGFTpqDMALQS-ATLSGGQHTRLLLARALIHD 143
Cdd:COG1120 81 PQEPPAP-FGLTVRELVaLGRYPhlglfgrPSAED--REAVEEALERTGLE--HLADRPvDELSGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556426975 144 PDLLLLDEPSNHLDLP----TMLWLEHFLQNWSGSFVLVSHD 181
Cdd:COG1120 156 PPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHD 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-189 |
8.86e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 8.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVdtAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR------V 72
Cdd:COG1121 3 MMPAIELENLTV--SYGgrPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrrigyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 73 EQHLP-DAIFPLTMLDAVL----AQLPLAERDS--LRWKAETLLA--GMgftpQDMALQS-ATLSGGQHTRLLLARALIH 142
Cdd:COG1121 81 PQRAEvDWDFPITVRDVVLmgryGRRGLFRRPSraDREAVDEALErvGL----EDLADRPiGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556426975 143 DPDLLLLDEPSNHLDLPTMLWLEHFLQNWSG---SFVLVSHDrqlLDAVT 189
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD---LGAVR 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-200 |
6.40e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclMARVEQHLPD------ 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG---KPLSAMPPPEwrrqva 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 79 ------AIFPLTMLDAVLAQLPLAERDSLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:COG4619 78 yvpqepALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556426975 153 SNHLDLPTML----WLEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKTL 200
Cdd:COG4619 158 TSALDPENTRrveeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-188 |
7.58e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 113.73 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVdtAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLP---- 77
Cdd:COG4133 2 MLEAENLSC--RRGerLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 ----DAIFP-LTMLDAVLAQLPLAERDSLRWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:COG4133 80 lghaDGLKPeLTVRENLRFWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 556426975 153 SNHLDLPTMLWLEHFLQNWS---GSFVLVSHDRQLLDAV 188
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-181 |
2.10e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 108.68 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 6 TAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarveqhlpdaifpltm 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 ldaVLAQLPLAERdslrwkAETllagMGFTPQDMAL---------QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:cd03214 62 ---DLASLSPKEL------ARK----IAYVPQALELlglahladrPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180
....*....|....*....|....*....
gi 556426975 157 DLPTMLWLEHFLQNWSGSF----VLVSHD 181
Cdd:cd03214 129 DIAHQIELLELLRRLARERgktvVMVLHD 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-197 |
2.77e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; 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: 213179 [Multi-domain] Cd Length: 157 Bit Score: 107.72 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 6 TAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarveqhlpdaifpltm 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 ldavlaqlplaerDSLRWKAETLLAGMGFTPQdmalqsatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLE 165
Cdd:cd00267 62 -------------DIAKLPLEELRRRIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 556426975 166 HFLQNWSG---SFVLVSHDRQLLDAVTNGSWILRD 197
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-501 |
2.66e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 112.69 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAFGTLF--DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAA---GTVALAGHCL------- 68
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLlelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 69 ----MARVEQHLPDAIFPLTMLDAVL--AQLPLAERDSLRWKAETLLAGMGFtPQDMALQSATLSGGQHTRLLLARALIH 142
Cdd:COG1123 81 rgrrIGMVFQDPMTQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 143 DPDLLLLDEPSNHLDLPT----MLWLEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKTLhyfalpctaarkaleakd 218
Cdd:COG1123 160 DPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI------------------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 219 esdaqrhkAEQKEIDRVTASAKRLATWGKVYDNEDLARKAKQMekqverlkesqtaltagsqwtltlrgdalrADRLLEM 298
Cdd:COG1123 222 --------VEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAA------------------------------AEPLLEV 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 299 ENLSV----PPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLI--------------WQQFADESAESGLKIHP 360
Cdd:COG1123 264 RNLSKrypvRGKGGVRAVDDVSL-TLRRGETLGLVGESGSGKSTLARLLlgllrptsgsilfdGKDLTKLSRRSLRELRR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 361 RVspgyydQTLNQLPDDA-----TLLDAL-EP-----FAPDPQNRKMAL-------ISAGFpWSRHgqkISTLSGGERSR 422
Cdd:COG1123 343 RV------QMVFQDPYSSlnprmTVGDIIaEPlrlhgLLSRAERRERVAellervgLPPDL-ADRY---PHELSGGQRQR 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 423 llfvgLTLARY-----SLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWH 493
Cdd:COG1123 413 -----VAIARAlalepKLLILDEPTSALDVSVQAQILNLLrdlqRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....*...
gi 556426975 494 DAEAVFER 501
Cdd:COG1123 488 PTEEVFAN 495
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-154 |
3.63e-26 |
|
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: 104.27 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLP---------DAIFP-LTMLDAV 89
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkeigyvfqdPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQLPLAE--RDSLRWKAETLLAGMGFTPQD---MALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:pfam00005 81 RLGLLLKGlsKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-202 |
5.54e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 106.48 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQH------LPDAI-FP--LTMLD--A 88
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqigvLPDERgLYdrLTVREniR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VLAQLPLAERDSLRWKAETLLAGMGFTPqDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFL 168
Cdd:COG4555 97 YFAELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREIL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 556426975 169 QNWSGS---FVLVSHDRQLLDAVTNGSWILRDKTLHY 202
Cdd:COG4555 176 RALKKEgktVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-197 |
7.94e-26 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 105.24 E-value: 7.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR-----------VEQHlP 77
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelrrkvglVFQN-P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 DA-IFPLTMLDAV---LAQLPLAERDSLRwKAETLLAGMGFtpQDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:cd03225 85 DDqFFGPTVEEEVafgLENLGLPEEEIEE-RVEEALELVGL--EGLRDRSpFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556426975 153 SNHLDLPTMLWLEHFLQNWSG---SFVLVSHDRQLLDAVTNGSWILRD 197
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-181 |
9.47e-26 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain] Cd Length: 173 Bit Score: 103.63 E-value: 9.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarveqhlpdaifpltmldavlaqlplaerdS 100
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---------------------------------D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 101 LRWKAETLLAGMGFTPQDMAL-------QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWS- 172
Cdd:cd03230 64 IKKEPEEVKRRIGYLPEEPSLyenltvrENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKk 143
|
170
....*....|.
gi 556426975 173 --GSFVLVSHD 181
Cdd:cd03230 144 egKTILLSSHI 154
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-203 |
2.24e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 104.15 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG------HCLMARVEQHLP-DAIFPLTMLDAVL----A 91
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekeRKRIGYVPQRRSiDRDFPISVRDVVLmglyG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 92 QLPLAERDSLRWK--AETLLAGMGFTpqDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFL 168
Cdd:cd03235 98 HKGLFRRLSKADKakVDEALERVGLS--ELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 556426975 169 QNWSG---SFVLVSHDRQLLDAVTNGSwILRDKTLHYF 203
Cdd:cd03235 176 RELRRegmTILVVTHDLGLVLEYFDRV-LLLNRTVVAS 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-188 |
4.83e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 104.11 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR-----------VEQHLPDAIFPLTMLDAV 89
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRrrkafrrrvqmVFQDPYASLHPRHTVDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQlPLAERDSLRWKAE--TLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT---MLWL 164
Cdd:COG1124 102 LAE-PLRIHGLPDREERiaELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeILNL 180
|
170 180
....*....|....*....|....*
gi 556426975 165 EHFLQNWSG-SFVLVSHDRQLLDAV 188
Cdd:COG1124 181 LKDLREERGlTYLFVSHDLAVVAHL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-157 |
1.28e-24 |
|
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: 100.54 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarveqhlpdaifPLTMLDavlaqlplaeR 98
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV---------------DLRDLD----------L 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 99 DSLRWKaetllagMGFTPQDMALQSAT-----LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03228 72 ESLRKN-------IAYVPQDPFLFSGTireniLSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
18-178 |
9.43e-24 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 100.66 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH-----------CLMARVEQHLPDAIfPLTML 86
Cdd:TIGR03873 15 LIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrraraRRVALVEQDSDTAV-PLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 DAV-LAQLPLAERdslrWKAET---------LLAGMGFTpqDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPSNH 155
Cdd:TIGR03873 94 DVVaLGRIPHRSL----WAGDSphdaavvdrALARTELS--HLADRDmSTLSGGERQRVHVARALAQEPKLLLLDEPTNH 167
|
170 180
....*....|....*....|...
gi 556426975 156 LDLPTMLWLEHFLQNWSGSFVLV 178
Cdd:TIGR03873 168 LDVRAQLETLALVRELAATGVTV 190
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-181 |
4.07e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.21 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM---ARVEQH---LPD--AIFP-LT---MLD- 87
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVArdpAEVRRRigyVPQepALYPdLTvreNLRf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 -AVLAQLPLAERDSlrwKAETLLAGMGFTPqDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEH 166
Cdd:COG1131 97 fARLYGLPRKEARE---RIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWE 172
|
170
....*....|....*...
gi 556426975 167 FLQNWSG---SFVLVSHD 181
Cdd:COG1131 173 LLRELAAegkTVLLSTHY 190
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-185 |
4.34e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQH--LPDAiFPLTMLDAVLAQLpLAERDS 100
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRseVPDS-LPLTVRDLVAMGR-WARRGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 101 LRW-------KAETLLAGMGFTpqDMA-LQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWS 172
Cdd:NF040873 89 WRRltrddraAVDDALERVGLA--DLAgRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEH 166
|
170
....*....|....*.
gi 556426975 173 G---SFVLVSHDRQLL 185
Cdd:NF040873 167 ArgaTVVVVTHDLELV 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-188 |
6.30e-23 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 102.71 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 15 AFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHlPDAIFP-LTMLDAVLA 91
Cdd:TIGR03719 331 AFGdkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS-RDALDPnKTVWEEISG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 92 QLPLAERDSLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNW 171
Cdd:TIGR03719 410 GLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF 489
|
170
....*....|....*..
gi 556426975 172 SGSFVLVSHDRQLLDAV 188
Cdd:TIGR03719 490 AGCAVVISHDRWFLDRI 506
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
297-488 |
9.92e-23 |
|
ATP-binding cassette transporter nucleotide-binding domain; 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: 213179 [Multi-domain] Cd Length: 157 Bit Score: 94.62 E-value: 9.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 297 EMENLSVPpAPGLPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLKIHPRVSPGYYDQTLNQLPd 376
Cdd:cd00267 1 EIENLSFR-YGGRTALDNVSLT-LKAGEIVALVGPNGSGKSTLLRAI----------AGLLKPTSGEILIDGKDIAKLP- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 377 datlldalepfaPDPQNRKMALISagfpwsrhgQkistLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQT 456
Cdd:cd00267 68 ------------LEELRRRIGYVP---------Q----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 556426975 457 LQQF-EGG--VLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:cd00267 123 LRELaEEGrtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-181 |
1.07e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213264 [Multi-domain] Cd Length: 214 Bit Score: 96.60 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLK-----KGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM-ARVEQHLPD------------AIFP-LT 84
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdSRKKINLPPqqrkiglvfqqyALFPhLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAVLAQLPLAERDSLRWKAETLLAGMGFTPQDMAlQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWL 164
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNR-YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|.
gi 556426975 165 EHFLQNWSGSF----VLVSHD 181
Cdd:cd03297 171 LPELKQIKKNLnipvIFVTHD 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-190 |
1.30e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 95.79 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 17 GTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR--------VEQHLPDAIFPLTMLDA 88
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerrksigyVMQDVDYQLFTDSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VLAQLPLAERDSLrwKAETLLAGMG-FTPQDmaLQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTM-----L 162
Cdd:cd03226 93 LLLGLKELDAGNE--QAETVLKDLDlYALKE--RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMervgeL 168
|
170 180
....*....|....*....|....*...
gi 556426975 163 WLEhfLQNWSGSFVLVSHDRQLLDAVTN 190
Cdd:cd03226 169 IRE--LAAQGKAVIVITHDYEFLAKVCD 194
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-206 |
1.40e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 96.63 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHL----------PDA-IFPLTML 86
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvglvfqnPDDqLFAPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 DAV---LAQLPLAERDSLRwKAETLLAGMGFTpqDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTML 162
Cdd:COG1122 95 EDVafgPENLGLPREEIRE-RVEEALELVGLE--HLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556426975 163 WLEHFLQNWSG---SFVLVSHDRQLLDAVTNGSWILRDKTLHYFALP 206
Cdd:COG1122 172 ELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-186 |
1.66e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 96.35 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLRVDTAFGTL--FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARV------- 72
Cdd:COG4181 15 TKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedaRARLrarhvgf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 73 ----EQHLPDaifpLTMLDAVLAQLPLAERDSLRWKAETLLAGMGF------TPqdmalqsATLSGGQHTRLLLARALIH 142
Cdd:COG4181 95 vfqsFQLLPT----LTALENVMLPLELAGRRDARARARALLERVGLghrldhYP-------AQLSGGEQQRVALARAFAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556426975 143 DPDLLLLDEPSNHLDLPT---MLWLEHFLQNWSGS-FVLVSHDRQLLD 186
Cdd:COG4181 164 EPAILFADEPTGNLDAATgeqIIDLLFELNRERGTtLVLVTHDPALAA 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-197 |
2.73e-22 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 101.09 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 13 DTAFG-----TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAI-FPLTML 86
Cdd:PLN03073 513 DASFGypggpLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLdLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 DAVLAQLPLAERDSLRwkaeTLLAGMGFTpQDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLE 165
Cdd:PLN03073 593 LYMMRCFPGVPEQKLR----AHLGSFGVT-GNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
170 180 190
....*....|....*....|....*....|..
gi 556426975 166 HFLQNWSGSFVLVSHDRQLLDAVTNGSWILRD 197
Cdd:PLN03073 668 QGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-181 |
3.76e-22 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. 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: 213260 [Multi-domain] Cd Length: 220 Bit Score: 94.85 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmARVEQHLPD--------AIFP-LTMLDA 88
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDrgyvfqqdALLPwLTVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VLaqLPL----AERDSLRWKAETLLAGMGftpqdmaLQSA------TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDL 158
Cdd:cd03293 94 VA--LGLelqgVPKAEARERAEELLELVG-------LSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDA 164
|
170 180
....*....|....*....|....*..
gi 556426975 159 PTMLWL-EHFLQNWSG---SFVLVSHD 181
Cdd:cd03293 165 LTREQLqEELLDIWREtgkTVLLVTHD 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-188 |
5.07e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 93.05 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarveqhlpdaifpltmldavlaqlplaeR 98
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--------------------------------A 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 99 DSLRWKAETLLAGMGFTPQDMALQSAT-----LSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQN--- 170
Cdd:cd03246 65 DISQWDPNELGDHVGYLPQDDELFSGSiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlka 144
|
170
....*....|....*...
gi 556426975 171 WSGSFVLVSHDRQLLDAV 188
Cdd:cd03246 145 AGATRIVIAHRPETLASA 162
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-182 |
1.16e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain] Cd Length: 213 Bit Score: 93.35 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG---HCLMAR------VEQHlpDAIFP-LTMLD 87
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPErrnigmVFQD--YALFPhLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AVlaQLPLAER----DSLRWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLW 163
Cdd:cd03259 92 NI--AFGLKLRgvpkAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180
....*....|....*....|...
gi 556426975 164 LEHFLQNWSGSF----VLVSHDR 182
Cdd:cd03259 169 LREELKELQRELgittIYVTHDQ 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-181 |
1.35e-21 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 93.72 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL------MARVEQHLPDAIF--PLTMLD----- 87
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrLRKIRRKEIQMVFqdPMSSLNprmti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 ------AVLAQLPLAERDSLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT- 160
Cdd:cd03257 102 geqiaePLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVq 181
|
170 180
....*....|....*....|....
gi 556426975 161 --MLWLEHFLQNWSG-SFVLVSHD 181
Cdd:cd03257 182 aqILDLLKKLQEELGlTLLFITHD 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-188 |
1.56e-21 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 98.30 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHlpDAIFPLTML 86
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrdldeddlrrrIAVVPQR--PHLFDTTLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 D---------------AVLAQLPLAER-DSLRWKAETLLAGMGftpqdmalqsATLSGGQHTRLLLARALIHDPDLLLLD 150
Cdd:COG4987 427 EnlrlarpdatdeelwAALERVGLGDWlAALPDGLDTWLGEGG----------RRLSGGERRRLALARALLRDAPILLLD 496
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556426975 151 EPSNHLDLPT-MLWLEHFLQNWSG-SFVLVSHDRQLLDAV 188
Cdd:COG4987 497 EPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLERM 536
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
18-181 |
1.60e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.39 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmARVEQHLPD--------AIFP-LTMLDA 88
Cdd:COG1116 25 TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPDrgvvfqepALLPwLTVLDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 V-----LAQLPLAERDSlrwKAETLLAGMGFT------PqdmalqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG1116 101 ValgleLRGVPKAERRE---RARELLELVGLAgfedayP-------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
170 180
....*....|....*....|....*....
gi 556426975 158 LPT--MLWlEHFLQNWSG---SFVLVSHD 181
Cdd:COG1116 171 ALTreRLQ-DELLRLWQEtgkTVLFVTHD 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-186 |
1.82e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 98.27 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 15 AFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHlPDAIFP-LTMLDAV-- 89
Cdd:PRK11819 333 SFGdrLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQS-RDALDPnKTVWEEIsg 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 -LAQLPLAERDSlrwKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFL 168
Cdd:PRK11819 412 gLDIIKVGNREI---PSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEAL 488
|
170
....*....|....*...
gi 556426975 169 QNWSGSFVLVSHDRQLLD 186
Cdd:PRK11819 489 LEFPGCAVVISHDRWFLD 506
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-180 |
3.06e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 93.23 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAG-TVALAGHCL----MARVEQHL----PD--AIFP--LT 84
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRggedVWELRKRIglvsPAlqLRFPrdET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAVLAqlplAERDSL-RW---------KAETLLAGMGFTpqDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:COG1119 97 VLDVVLS----GFFDSIgLYreptdeqreRARELLELLGLA--HLADRPfGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190
....*....|....*....|....*....|.
gi 556426975 154 NHLDLPTMLWLEHFLQNWSGS----FVLVSH 180
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-189 |
3.59e-21 |
|
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: 92.27 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL----MARVEQH---LPDAI--FPLTMLDAVLA 91
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldPADLRRNigyVPQDVtlFYGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 92 QLPLAERDSLRWKAEtlLAGMG-FT---PQDMALQ----SATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLW 163
Cdd:cd03245 101 GAPLADDERILRAAE--LAGVTdFVnkhPNGLDLQigerGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180
....*....|....*....|....*...
gi 556426975 164 LEHFLQNWSG--SFVLVSHDRQLLDAVT 189
Cdd:cd03245 179 LKERLRQLLGdkTLIIITHRPSLLDLVD 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-184 |
4.55e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 91.78 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmarveQHLPDA------------IFP-------LT 84
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-----SKLSEKelaafrrrhigfVFQsfnllpdLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAVLAQLPLAERDSLRWK--AETLLAGMGFtPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT-- 160
Cdd:cd03255 99 ALENVELPLLLAGVPKKERRerAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgk 177
|
170 180
....*....|....*....|....*.
gi 556426975 161 --MLWLEHFLQNWSGSFVLVSHDRQL 184
Cdd:cd03255 178 evMELLRELNKEAGTTIVVVTHDPEL 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-190 |
4.60e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 92.79 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVdtAFGTL--FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL---------- 68
Cdd:COG0411 1 SDPLLEVRGLTK--RFGGLvaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 69 --MARVEQHLpdAIFP-LTMLD----AVLAQL-------------PLAERDSLRWKAETLLAGMGFTPQdMALQSATLSG 128
Cdd:COG0411 79 lgIARTFQNP--RLFPeLTVLEnvlvAAHARLgrgllaallrlprARREEREARERAEELLERVGLADR-ADEPAGNLSY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 129 GQHTRLLLARALIHDPDLLLLDEPS---NHLDLPTMLWLEHFLQNWSG-SFVLVSHDrqlLDAVTN 190
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHD---MDLVMG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-200 |
8.36e-21 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 91.03 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL---MARVEQHL-----PDAIFP-LTMLDAVL- 90
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdRKAARQSLgycpqFDALFDeLTVREHLRf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 -AQL---PLAERDSLrwkAETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDlPTM---LW 163
Cdd:cd03263 99 yARLkglPKSEIKEE---VELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PASrraIW 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 556426975 164 --LEHFLQNwsGSFVLVSHDRQLLDAVTNGSWILRDKTL 200
Cdd:cd03263 174 dlILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-188 |
1.34e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 96.06 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHlpDAIFPLTMLD 87
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrqidpaslrrqIGVVLQD--VFLFSGTIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AVLAQLPLAERDSLRWKAEtlLAG---------MGFtpqDMAL--QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:COG2274 568 NITLGDPDATDEEIIEAAR--LAGlhdfiealpMGY---DTVVgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190
....*....|....*....|....*....|....*.
gi 556426975 157 DLPT----MLWLEHFLQNWsgSFVLVSHDRQLLDAV 188
Cdd:COG2274 643 DAETeaiiLENLRRLLKGR--TVIIIAHRLSTIRLA 676
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-186 |
1.49e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 90.49 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSL----RVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmarveQHL 76
Cdd:COG1136 1 MSPLLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-----SSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 77 PDA------------IF------P-LT-----MLDAVLAQLPLAERdslRWKAETLLAGMGFTPQdMALQSATLSGGQHT 132
Cdd:COG1136 76 SERelarlrrrhigfVFqffnllPeLTalenvALPLLLAGVSRKER---RERARELLERVGLGDR-LDHRPSQLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 133 RLLLARALIHDPDLLLLDEPSNHLDLPT----MLWLEHFLQNWSGSFVLVSHDRQLLD 186
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELAA 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-184 |
3.05e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 90.63 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL--------------MARVEQHLPDAIFPL 83
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldrkqrrafrrdVQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 84 TMLDAVLAQlPLAERDSL-----RWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDL 158
Cdd:TIGR02769 105 MTVRQIIGE-PLRHLTSLdeseqKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190
....*....|....*....|....*....|
gi 556426975 159 ---PTMLWLEHFLQNWSG-SFVLVSHDRQL 184
Cdd:TIGR02769 184 vlqAVILELLRKLQQAFGtAYLFITHDLRL 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-190 |
3.63e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 89.80 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVdtAFGTL--FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL------------MA 70
Cdd:cd03219 1 LEVRGLTK--RFGGLvaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglppheiarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 71 RVEQHLpdAIFP-LTMLD----AVLAQLPLA--------ERDSLRWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLA 137
Cdd:cd03219 79 RTFQIP--RLFPeLTVLEnvmvAAQARTGSGlllararrEEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 138 RALIHDPDLLLLDEPS---NHLDLPTMLWLEHFLQNWSGSFVLVSHDrqlLDAVTN 190
Cdd:cd03219 156 RALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHD---MDVVMS 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-184 |
7.60e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 8 QSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMA--------------RVE 73
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiqMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 74 QHLPDAIFPLTMLDAVLAQ-----LPLAERDSLRwKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLL 148
Cdd:PRK10419 96 QDSISAVNPRKTVREIIREplrhlLSLDKAERLA-RASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556426975 149 LDEPSNHLDL---PTMLWLEHFLQNWSG-SFVLVSHDRQL 184
Cdd:PRK10419 175 LDEAVSNLDLvlqAGVIRLLKKLQQQFGtACLFITHDLRL 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-189 |
1.12e-19 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 93.01 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHLpdAIFPLTMLDAV 89
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqidpadlrrnIGYVPQDP--RLFYGTLRDNI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQLPLAERDSLRWKAEtlLAGMG-FT---PQDMALQ----SATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTM 161
Cdd:TIGR03375 560 ALGAPYADDEEILRAAE--LAGVTeFVrrhPDGLDMQigerGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSE 637
|
170 180 190
....*....|....*....|....*....|
gi 556426975 162 LWLEHFLQNWSG--SFVLVSHDRQLLDAVT 189
Cdd:TIGR03375 638 ERFKDRLKRWLAgkTLVLVTHRTSLLDLVD 667
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-182 |
1.53e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVdtAFGTLF--DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHcLMARVE----- 73
Cdd:COG3842 2 AMPALELENVSK--RYGDVTalDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-DVTGLPpekrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 74 -----QHlpDAIFP-LTMLDAV-----LAQLPLAERDSlrwKAETLLA--GMGftpqDMALQS-ATLSGGQHTRLLLARA 139
Cdd:COG3842 79 vgmvfQD--YALFPhLTVAENVafglrMRGVPKAEIRA---RVAELLElvGLE----GLADRYpHQLSGGQQQRVALARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556426975 140 LIHDPDLLLLDEPSNHLDLPT---M-LWLEHFLQNWSGSFVLVSHDR 182
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLreeMrEELRRLQRELGITFIYVTHDQ 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-182 |
1.77e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.82 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVE----------QHLpdAIFP-LTML 86
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprerrvgfvfQHY--ALFPhMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 DAV---LAQLPLAERDSLRwKAETLLAGMGftpqdmaLQS------ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG1118 94 ENIafgLRVRPPSKAEIRA-RVEELLELVQ-------LEGladrypSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190
....*....|....*....|....*....|.
gi 556426975 158 ------LptMLWLEHFLQNWSGSFVLVSHDR 182
Cdd:COG1118 166 akvrkeL--RRWLRRLHDELGGTTVFVTHDQ 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-196 |
1.87e-19 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 91.74 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 17 GTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHlpDAIFPLTM 85
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsdldpaswrrqIAWVPQN--PYLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 LDAVLAQLPLAERDSLRWKAEtlLAGM-GFTPQ-----DMAL--QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG4988 428 RENLRLGRPDASDEELEAALE--AAGLdEFVAAlpdglDTPLgeGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556426975 158 LPTMLWLEHFLQNWSGS--FVLVSHDrqlLDAVTNGSWILR 196
Cdd:COG4988 506 AETEAEILQALRRLAKGrtVILITHR---LALLAQADRILV 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
296-489 |
2.38e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 85.73 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPP-LFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLI---WQQFADESAESGLKIHpRVSPGYYDQTL 371
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSF-SIEPGESLAIIGPSGSGKSTLARLIlglLRPTSGRVRLDGADIS-QWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 372 NQLPDDATLLDalepfapdpqnrkmalisagfpwsrhG---QKIstLSGGERSRLLfvgltLAR--Y---SLLMLDEPTN 443
Cdd:cd03246 79 GYLPQDDELFS--------------------------GsiaENI--LSGGQRQRLG-----LARalYgnpRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556426975 444 HLDMEGKEALAQTLQQFEGG---VLLVSHDRQLIsQSCNRFWLIEEGKL 489
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-181 |
4.10e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.22 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM------ARVEQHlpDAIFP-LTMLDAV-----L 90
Cdd:COG4525 26 VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgadrGVVFQK--DALLPwLNVLDNVafglrL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 AQLPLAERdslRWKAETLLAGMGFtpQDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT---MlwLEH 166
Cdd:COG4525 104 RGVPKAER---RARAEELLALVGL--ADFARRRiWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTreqM--QEL 176
|
170
....*....|....*...
gi 556426975 167 FLQNWSGS---FVLVSHD 181
Cdd:COG4525 177 LLDVWQRTgkgVFLITHS 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-197 |
4.20e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 84.40 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmaRVEQHLPdaifpltmldavlaqlplaeRDS 100
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK----EVSFASP--------------------RDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 101 LRwkaetllAGMGFTPQdmalqsatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNW--SG-SFVL 177
Cdd:cd03216 73 RR-------AGIAMVYQ--------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIF 137
|
170 180
....*....|....*....|....
gi 556426975 178 VSH----DRQLLDAVTngswILRD 197
Cdd:cd03216 138 ISHrldeVFEIADRVT----VLRD 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-157 |
6.72e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.29 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHcLMARVEQHLPDAIfpltmldAVLAQLPLAE 97
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV-PVSDLEKALSSLI-------SVLNQRPYLF 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 98 RDSLRwkaetllagmgftpQDMALQsatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03247 88 DTTLR--------------NNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-160 |
9.70e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 89.34 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG-------HCLMARVEQHLP-DA-IFPLTMLDAVL 90
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldQDEVRRRVSVCAqDAhLFDTTVRENLR 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 91 AQLPLAERDSLRWKAETllAGMGFTPQD--------MALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT 160
Cdd:TIGR02868 431 LARPDATDEELWAALER--VGLADWLRAlpdgldtvLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-181 |
1.10e-18 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain] Cd Length: 178 Bit Score: 83.78 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarveqhlpdaifplTMLDAVLAQLPLAE 97
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG------------------EDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 98 RDSlrwkaetllaGMGFtpQDMALQSA---------TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFL 168
Cdd:cd03229 76 RRI----------GMVF--QDFALFPHltvlenialGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALL 143
|
170
....*....|....*..
gi 556426975 169 ----QNWSGSFVLVSHD 181
Cdd:cd03229 144 kslqAQLGITVVLVTHD 160
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-183 |
2.37e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). 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: 213263 [Multi-domain] Cd Length: 239 Bit Score: 84.70 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR---------VEQHLpdAIFP-LTMLDAV- 89
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvqernvgfVFQHY--ALFRhMTVFDNVa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 --LAQLPLAER---DSLRWKAETLLAGMGFTpqdmALQS---ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD---- 157
Cdd:cd03296 97 fgLRVKPRSERppeAEIRAKVHELLKLVQLD----WLADrypAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDakvr 172
|
170 180
....*....|....*....|....*...
gi 556426975 158 --LPTmlWLEHFLQNWSGSFVLVSHDRQ 183
Cdd:cd03296 173 keLRR--WLRRLHDELHVTTVFVTHDQE 198
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-183 |
3.47e-18 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. 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: 213267 [Multi-domain] Cd Length: 232 Bit Score: 83.83 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 11 RVDTAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL---------MARVEQHLpdA 79
Cdd:cd03300 5 NVSKFYGgfVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlpphkrpVNTVFQNY--A 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 80 IFP-LTMLDAV-----LAQLPLAERDslRWKAETL-LAGMGFTPQDMALQsatLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:cd03300 83 LFPhLTVFENIafglrLKKLPKAEIK--ERVAEALdLVQLEGYANRKPSQ---LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 556426975 153 SNHLDLP----TMLWLEHFLQNWSGSFVLVSHDRQ 183
Cdd:cd03300 158 LGALDLKlrkdMQLELKRLQKELGITFVFVTHDQE 192
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-181 |
4.05e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.92 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHlpdaifpLTMLDAVLAQ-------L 93
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF-------LRRIGVVFGQktqlwwdL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 94 PLAERDSL----------RWKA--ETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTM 161
Cdd:cd03267 111 PVIDSFYLlaaiydlppaRFKKrlDELSELLDLEEL-LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180
....*....|....*....|....
gi 556426975 162 LWLEHFLQNWS----GSFVLVSHD 181
Cdd:cd03267 190 ENIRNFLKEYNrergTTVLLTSHY 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-185 |
4.53e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 87.34 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPD---------AIFPLTMLDAVLA 91
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDqiawvpqhpFLFAGTIAENIRL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 92 QLPLAERDSLRwKAETLLAGMGFT---PQDMALQ----SATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT-MLW 163
Cdd:TIGR02857 419 ARPDASDAEIR-EALERAGLDEFVaalPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETeAEV 497
|
170 180
....*....|....*....|...
gi 556426975 164 LEHFLQNWSG-SFVLVSHDRQLL 185
Cdd:TIGR02857 498 LEALRALAQGrTVLLVTHRLALA 520
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
297-488 |
1.02e-17 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 82.13 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 297 EMENLSVPPAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRL-----------IWQQFADESAESGLKIHPRVspG 365
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLlngllgptsgeVLVDGKDLTKLSLKELRRKV--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 366 YydqtLNQLPDD----ATLLD----ALEPFAPDP---QNRKMALISAGFPWSRHGQKISTLSGGERSRLLFVGLTLARYS 434
Cdd:cd03225 79 L----VFQNPDDqffgPTVEEevafGLENLGLPEeeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 435 LLMLDEPTNHLDMEGKEALAQTLQQF--EG-GVLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-180 |
1.27e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 81.49 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 17 GTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarveQHLPDAIFPL----TMLDAVLAQ 92
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG--------KSYQKNIEALrrigALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 93 LPLAERDSLRWKA-----------ETL-LAGMGFTPQDMAlqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT 160
Cdd:cd03268 85 PNLTARENLRLLArllgirkkridEVLdVVGLKDSAKKKV---KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180
....*....|....*....|...
gi 556426975 161 MLWLEHFLQNWS---GSFVLVSH 180
Cdd:cd03268 162 IKELRELILSLRdqgITVLISSH 184
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
15-161 |
1.60e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 81.42 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 15 AFGTL--FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------------MARVEQHLpdA 79
Cdd:cd03262 9 SFGDFhvLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkkninelrqkVGMVFQQF--N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 80 IFP-LTMLDAV-LAQ-----LPLAERDSlrwKAETLLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:cd03262 87 LFPhLTVLENItLAPikvkgMSKAEAEE---RALELLEKVGLADKADAY-PAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
....*....
gi 556426975 153 SNHLDlPTM 161
Cdd:cd03262 163 TSALD-PEL 170
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-181 |
1.64e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; 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: 213262 [Multi-domain] Cd Length: 242 Bit Score: 81.96 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMA----RVEQHLPDAI-----FP-LTMLD--A 88
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpvELRRKIGYVIqqiglFPhMTVEEniA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VLAQLPLAERDSLRWKAETLLAGMGFTPQDMALQ-SATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWL-EH 166
Cdd:cd03295 98 LVPKLLKWPKEKIRERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqEE 177
|
170
....*....|....*...
gi 556426975 167 F--LQNWSG-SFVLVSHD 181
Cdd:cd03295 178 FkrLQQELGkTIVFVTHD 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-183 |
2.19e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.12 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmarveQHLPDAIFPLTMLDAVLAQLP------ 94
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPYQRPINMMFQSYALFPhmtveq 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 95 -----LAE----RDSLRWKAETLLAGMGFtpQDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD--LPTML 162
Cdd:PRK11607 111 niafgLKQdklpKAEIASRVNEMLGLVHM--QEFAKRKPhQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRM 188
|
170 180
....*....|....*....|...
gi 556426975 163 WLE--HFLQNWSGSFVLVSHDRQ 183
Cdd:PRK11607 189 QLEvvDILERVGVTCVMVTHDQE 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
21-157 |
3.63e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 81.26 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL--------------MARVEQH--LPDaifPLT 84
Cdd:COG3638 20 DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgralrrlrrrIGMIFQQfnLVP---RLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAVLA--------------QLPLAERDslrwKAETLLA--GMGftpqDMALQSA-TLSGGQHTRLLLARALIHDPDLL 147
Cdd:COG3638 97 VLTNVLAgrlgrtstwrsllgLFPPEDRE----RALEALErvGLA----DKAYQRAdQLSGGQQQRVAIARALVQEPKLI 168
|
170
....*....|
gi 556426975 148 LLDEPSNHLD 157
Cdd:COG3638 169 LADEPVASLD 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-181 |
3.99e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.01 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 12 VDTAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL--MARVE-QHLP--------- 77
Cdd:cd03261 6 LTKSFGgrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsgLSEAElYRLRrrmgmlfqs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 DAIF-PLTMLDAVlaQLPLAE-----RDSLRWKAETLLAGMGFTPQDmALQSATLSGGQHTRLLLARALIHDPDLLLLDE 151
Cdd:cd03261 86 GALFdSLTVFENV--AFPLREhtrlsEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 556426975 152 PSNHLDLPTMLWLEHFLQNWSGSF----VLVSHD 181
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELgltsIMVTHD 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-181 |
4.06e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVaLAGHCLMARVEQHLPdaifpLTMLDAVLaqLP--- 94
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTR-----LMFQDARL--LPwkk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 95 ------LAERDSLRWKAETLLAGMGFtpQDMALQ-SATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT---M--- 161
Cdd:PRK11247 98 vidnvgLGLKGQWRDAALQALAAVGL--ADRANEwPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrieMqdl 175
|
170 180
....*....|....*....|...
gi 556426975 162 ---LWLEHFLqnwsgSFVLVSHD 181
Cdd:PRK11247 176 iesLWQQHGF-----TVLLVTHD 193
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
21-157 |
5.62e-17 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 81.74 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMA---RVEQ---HLPDAiFPLtMLD------- 87
Cdd:TIGR03522 19 DEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQnpkEVQRnigYLPEH-NPL-YLDmyvreyl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AVLAQLPLAERDSLRWKAETLLAGMGFTPQDMALQSAtLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:TIGR03522 97 QFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQ-LSKGYRQRVGLAQALIHDPKVLILDEPTTGLD 165
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-190 |
5.89e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLP-DA 79
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYlDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 80 IFPLTMLDAVLAQLPLAERDSL----RWKAETLLagmgftpqDMALQSatLSGGQHTRLLLARALIHDPDLLLLDEPSNH 155
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEDILpalkRVQAGHLI--------DAPMQK--LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 556426975 156 LDLPTMLWLEHF---LQNWSGSFVL-VSHDRQLLDAVTN 190
Cdd:PRK09544 151 VDVNGQVALYDLidqLRRELDCAVLmVSHDLHLVMAKTD 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-157 |
6.13e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 79.72 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG---HCLMARVEQHL-----PDAIFP-LTMLDAVL- 90
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEARRRLgfvsdSTGLYDrLTARENLEy 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 91 -AQLPLAERDSLRWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03266 102 fAGLYGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
298-506 |
7.24e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 83.83 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 298 MENLSVPPAPGLPPLFNIEMARLkSGDRVAIVGRNGCGKSSLMRL---IWQQFADESaesglkihpRVSPGYYDQTLNQL 374
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFF-PGAKIGVLGLNGAGKSTLLRImagVDKDFNGEA---------RPQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 375 PD-DATL-------------LDALEPF--------APDP--------QNRKMALISAGFPWSRHGQ-------------- 410
Cdd:TIGR03719 77 PQlDPTKtvrenveegvaeiKDALDRFneisakyaEPDAdfdklaaeQAELQEIIDAADAWDLDSQleiamdalrcppwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 411 -KISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDRQLISQSCNrfWLIE---- 485
Cdd:TIGR03719 157 aDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILEldrg 234
|
250 260
....*....|....*....|....*.
gi 556426975 486 -----EGKLSEWHDAEAvfERLRESA 506
Cdd:TIGR03719 235 rgipwEGNYSSWLEQKQ--KRLEQEE 258
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
296-504 |
9.06e-17 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 79.68 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRL-----------IWqqFADE--SAESGLKIHPRV 362
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSL-SIEKGEFVAIIGPNGSGKSTLLRLlngllkptsgeVL--VDGKdiTKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 363 spGYydqtLNQLPDD----ATLLD----ALEPFAPDPQNRKM----ALISAGFpWSRHGQKISTLSGGERSRLLFVGLtL 430
Cdd:COG1122 78 --GL----VFQNPDDqlfaPTVEEdvafGPENLGLPREEIRErveeALELVGL-EHLADRPPHELSGGQKQRVAIAGV-L 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 431 A-RYSLLMLDEPTNHLDMEGKEALAQTLQQF--EG-GVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFERLRE 504
Cdd:COG1122 150 AmEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
319-489 |
9.81e-17 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 78.25 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFadeSAESGlKIHprvspgYYDQTLNQLPDD------ATLLDALE-----PF 387
Cdd:cd03214 21 SIEAGEIVGILGPNGAGKSTLLKTLAGLL---KPSSG-EIL------LDGKDLASLSPKelarkiAYVPQALEllglaHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 388 ApdpqnrkmalisagfpwsrhGQKISTLSGGERSRLLfvgltLARY-----SLLMLDEPTNHLDMEGKEALAQTLQQF-- 460
Cdd:cd03214 91 A--------------------DRPFNELSGGERQRVL-----LARAlaqepPILLLDEPTSHLDIAHQIELLELLRRLar 145
|
170 180 190
....*....|....*....|....*....|.
gi 556426975 461 EGG--VLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03214 146 ERGktVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-157 |
1.10e-16 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. 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: 213223 [Multi-domain] Cd Length: 241 Bit Score: 79.53 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA------IF-------PLTMLD 87
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqigmIFqqfnlieRLSVLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AVLAQLpLAERDSLR------WKAETLLA-------GMgftpQDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:cd03256 98 NVLSGR-LGRRSTWRslfglfPKEEKQRAlaalervGL----LDKAYQRAdQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
....
gi 556426975 154 NHLD 157
Cdd:cd03256 173 ASLD 176
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-187 |
1.44e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.94 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARVEQH----------LPDaifp 82
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkrreIPYLRRRigvvfqdfrlLPD---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 83 LTMLDAVLaqLPL----AERDSLRWKAETLLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDl 158
Cdd:COG2884 94 RTVYENVA--LPLrvtgKSRKEIRRRVREVLDLVGLSDKAKAL-PHELSGGEQQRVAIARALVNRPELLLADEPTGNLD- 169
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 159 PTMLW--LEHFLQ-NWSGSFVLV-SHDRQLLDA 187
Cdd:COG2884 170 PETSWeiMELLEEiNRRGTTVLIaTHDLELVDR 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-192 |
1.62e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSP---AAGTVALAGHCLmarveQHLP---- 77
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-----TALPaeqr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 --------DAIFP-LTMLD----AVLAQLPLAERdslRWKAETLLAGMGFTpqDMALQ-SATLSGGQHTRLLLARALIHD 143
Cdd:COG4136 77 rigilfqdDLLFPhLSVGEnlafALPPTIGRAQR---RARVEQALEEAGLA--GFADRdPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556426975 144 PDLLLLDEPSNHLDLPTMLWLEHF----LQNWSGSFVLVSHDRQllDAVTNGS 192
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE--DAPAAGR 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
296-491 |
1.73e-16 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 82.96 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPPLF-NIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwQQFadESAESGL---------KIHPRV--- 362
Cdd:COG2274 474 IELENVSFRYPGDSPPVLdNISL-TIKPGERVAIVGRSGSGKSTLLKLL-LGL--YEPTSGRilidgidlrQIDPASlrr 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 363 SPGYYDQ-------TL-------NQLPDDATLLDALE-----PFApdpQNRKMAL---ISAGfpwsrhGqkiSTLSGGER 420
Cdd:COG2274 550 QIGVVLQdvflfsgTIrenitlgDPDATDEEIIEAARlaglhDFI---EALPMGYdtvVGEG------G---SNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 421 SRLLfvgltLAR--Y---SLLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHDRQLIsQSCNRFWLIEEGKLSE 491
Cdd:COG2274 618 QRLA-----IARalLrnpRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-181 |
2.06e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 78.87 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 12 VDTAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLpDAI--------- 80
Cdd:COG1127 11 LTKSFGdrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL-YELrrrigmlfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 81 ---------------FPLTMldavLAQLPLAERDSLrwkAETLLAGMGFtPQDMALQSATLSGGQHTRLLLARALIHDPD 145
Cdd:COG1127 90 ggalfdsltvfenvaFPLRE----HTDLSEAEIREL---VLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556426975 146 LLLLDEPSNHLDlPTM------LWLEhfLQNWSG-SFVLVSHD 181
Cdd:COG1127 162 ILLYDEPTAGLD-PITsavideLIRE--LRDELGlTSVVVTHD 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-157 |
4.30e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 77.61 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDG-----TDSPAAGTVALAGH-------------CLMARVEQHLPdaIFPLT 84
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKdiydldvdvlelrRRVGMVFQKPN--PFPGS 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 85 MLDAVLAQLPL---AERDSLRWKAETLLAGMGFTPQ-DMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03260 97 IYDNVAYGLRLhgiKLKEELDERVEEALRKAALWDEvKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
296-488 |
4.41e-16 |
|
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: 76.27 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSV--PPAPGlPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaesglkihprvsPGYYDqtlnq 373
Cdd:cd03228 1 IEFKNVSFsyPGRPK-PVLKDVSL-TIKPGEKVAIVGPSGSGKSTLLKLL--------------------LRLYD----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 374 lPDDATLL---DALEPFAPDPQNRKMALISagfpwsrhgQKI----ST-----LSGGERSRllfvgLTLARY-----SLL 436
Cdd:cd03228 54 -PTSGEILidgVDLRDLDLESLRKNIAYVP---------QDPflfsGTireniLSGGQRQR-----IAIARAllrdpPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556426975 437 MLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHDRQLIsQSCNRFWLIEEGK 488
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
312-489 |
5.65e-16 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter 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: 213197 [Multi-domain] Cd Length: 173 Bit Score: 75.90 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 312 LFNIEMArLKSGDRVAIVGRNGCGKSSLMRLIWQQ----------FADESAESGLKIHPRVspGYYDQTlNQLPDDATLL 381
Cdd:cd03230 16 LDDISLT-VEKGEIYGLLGPNGAGKTTLIKIILGLlkpdsgeikvLGKDIKKEPEEVKRRI--GYLPEE-PSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 382 DALEpfapdpqnrkmalisagfpwsrhgqkistLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF- 460
Cdd:cd03230 92 ENLK-----------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELk 142
|
170 180 190
....*....|....*....|....*....|.
gi 556426975 461 -EGG-VLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03230 143 kEGKtILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-158 |
7.77e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARVEQHL 76
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspweLARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 77 PDAI---FPLTMLDAV-LAQLPLAERDSLRWK-AETLLAGMGFtpQDMALQS-ATLSGGQHTRLLLARAL--IHDPD--- 145
Cdd:COG4559 81 PQHSslaFPFTVEEVVaLGRAPHGSSAAQDRQiVREALALVGL--AHLAGRSyQTLSGGEQQRVQLARVLaqLWEPVdgg 158
|
170
....*....|....*
gi 556426975 146 --LLLLDEPSNHLDL 158
Cdd:COG4559 159 prWLFLDEPTSALDL 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-181 |
8.76e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 76.74 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmaRVEQHLPD--------AIFP-LTM------ 85
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK----QITEPGPDrmvvfqnySLLPwLTVrenial 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 -LDAVLAQLPLAERDSLrwkAETLLAGMGFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWL 164
Cdd:TIGR01184 78 aVDRVLPDLSKSERRAI---VEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|.
gi 556426975 165 -EHFLQNWSGS---FVLVSHD 181
Cdd:TIGR01184 154 qEELMQIWEEHrvtVLMVTHD 174
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-158 |
8.78e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 3 TLLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARVEQH 75
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwspaeLARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 76 LPDAI---FPLTMLDAV-LAQLPLAERDSlrwKAETLLagmgftpqDMALQSA-----------TLSGGQHTRLLLARAL 140
Cdd:PRK13548 81 LPQHSslsFPFTVEEVVaMGRAPHGLSRA---EDDALV--------AAALAQVdlahlagrdypQLSGGEQQRVQLARVL 149
|
170 180
....*....|....*....|....
gi 556426975 141 I------HDPDLLLLDEPSNHLDL 158
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDL 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-153 |
9.44e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). 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.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 76.32 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL------------MARVEQHlpDAIFP-LTM 85
Cdd:cd03224 16 LFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglppheraragIGYVPEG--RRIFPeLTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 86 LDAVLAQLPLAERDSLRWKAETLLAgMgFtP--QDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLERVYE-L-F-PrlKERRKQLAgTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-157 |
1.12e-15 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. 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: 213225 [Multi-domain] Cd Length: 233 Bit Score: 76.47 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA------IF-------PLTMLD 87
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKArrrigmIFqhfnllsSRTVFE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 88 AV-----LAQLPLAERDSlrwKAETLLAGMGFTPQDMAlQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03258 102 NValpleIAGVPKAEIEE---RVLELLELVGLEDKADA-YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
296-469 |
1.28e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.50 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLI---WQqfadesaesglkihprvspgYYDQTLN 372
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSF-EIKPGDRLLITGPSGTGKSSLFRALaglWP--------------------WGSGRIG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 373 QLPDDATLLDALEPFAPdPQNRKMALIsagFPWSRhgqkisTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEA 452
Cdd:cd03223 60 MPEGEDLLFLPQRPYLP-LGTLREQLI---YPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170
....*....|....*..
gi 556426975 453 LAQTLQQFEGGVLLVSH 469
Cdd:cd03223 130 LYQLLKELGITVISVGH 146
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-157 |
1.31e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 76.25 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR----------VEQHLP-DAIfpLTMLDAV 89
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREprevrrrigiVFQDLSvDDE--LTGWENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 90 LAQLPLA--ERDSLRWKAETLLAGMGFTpqDMA-LQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03265 95 YIHARLYgvPGAERRERIDELLDFVGLL--EAAdRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-157 |
1.74e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHL-------------PD------ 78
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrvgvvpqfdnldPDftvren 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 79 -----AIFPLTMLDAVLAQLPLAERDSLRWKAETllagmgftpqdmalQSATLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:PRK13537 101 llvfgRYFGLSAAAARALVPPLLEFAKLENKADA--------------KVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
....
gi 556426975 154 NHLD 157
Cdd:PRK13537 167 TGLD 170
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-158 |
1.79e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 12 VDTAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARveqhlpDAifplTMLDAV 89
Cdd:PRK09536 9 LSVEFGdtTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL------SA----RAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQLPLAERDSLRWKAETLLAgMGFTPQ-----------DMALQSA---------------TLSGGQHTRLLLARALIHD 143
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVE-MGRTPHrsrfdtwtetdRAAVERAmertgvaqfadrpvtSLSGGERQRVLLARALAQA 157
|
170
....*....|....*
gi 556426975 144 PDLLLLDEPSNHLDL 158
Cdd:PRK09536 158 TPVLLLDEPTASLDI 172
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-184 |
1.90e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----MARVE------------QH-LPDaifpLT 84
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssAAKAElrnqklgfiyqfHHlLPD----FT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAVlaQLPL----AERDSLRWKAETLLAGMGFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT 160
Cdd:PRK11629 104 ALENV--AMPLligkKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180
....*....|....*....|....*...
gi 556426975 161 MLWLEHFLQNWS----GSFVLVSHDRQL 184
Cdd:PRK11629 181 ADSIFQLLGELNrlqgTAFLVVTHDLQL 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
15-157 |
2.00e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain] Cd Length: 210 Bit Score: 75.39 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 15 AFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQH---LPD--AIFP-LTML 86
Cdd:cd03269 9 RFGrvTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLPEerGLYPkMKVI 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 87 DAV--LAQLP-LAERDSLRWkAETLLAGMGFTP-QDMALQsaTLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03269 89 DQLvyLAQLKgLKKEEARRR-IDEWLERLELSEyANKRVE--ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-157 |
2.89e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.45 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 12 VDTAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHlPD--------AIF 81
Cdd:PRK11432 12 ITKRFGsnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDicmvfqsyALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 82 P-----------LTMLDavlaqLPLAERDSlRWKaETL----LAGMG--FTPQdmalqsatLSGGQHTRLLLARALIHDP 144
Cdd:PRK11432 91 PhmslgenvgygLKMLG-----VPKEERKQ-RVK-EALelvdLAGFEdrYVDQ--------ISGGQQQRVALARALILKP 155
|
170
....*....|...
gi 556426975 145 DLLLLDEPSNHLD 157
Cdd:PRK11432 156 KVLLFDEPLSNLD 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-183 |
3.29e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmarveQHLPD------------AIFP-LT 84
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPAenrhvntvfqsyALFPhMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAV-----LAQLPLAE-----RDSLRWkaeTLLAGMG-FTPQDmalqsatLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:PRK09452 103 VFENVafglrMQKTPAAEitprvMEALRM---VQLEEFAqRKPHQ-------LSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 556426975 154 NHLDLP---TM-LWLEHfLQNWSG-SFVLVSHDRQ 183
Cdd:PRK09452 173 SALDYKlrkQMqNELKA-LQRKLGiTFVFVTHDQE 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-157 |
4.96e-15 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain] Cd Length: 211 Bit Score: 74.15 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 17 GTLFDSLSFTLKKGdRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQhlpdaifpltmLDAVLAQLPLA 96
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-----------LRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 97 ERDSLRWKAETLLAGMGF---TPQ-------DMALQS-----------ATLSGGQHTRLLLARALIHDPDLLLLDEPSNH 155
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWlkgIPSkevkarvDEVLELvnlgdrakkkiGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
..
gi 556426975 156 LD 157
Cdd:cd03264 161 LD 162
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-157 |
9.10e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.88 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmaRVEQHLP----------------------D 78
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG-----RDVTDLPpkdrniamvfqsyalyphmtvyE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 79 AI-FPLTMldavlAQLPLAERDS-LRWKAETL-LAGMgftpqdmaLQS--ATLSGGQHTRLLLARALIHDPDLLLLDEP- 152
Cdd:COG3839 95 NIaFPLKL-----RKVPKAEIDRrVREAAELLgLEDL--------LDRkpKQLSGGQRQRVALGRALVREPKVFLLDEPl 161
|
....*
gi 556426975 153 SNhLD 157
Cdd:COG3839 162 SN-LD 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-502 |
1.00e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.76 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDS--PAAGT----VALAGHCLM----ARVEQHLPD-------------- 78
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRiiyhVALCEKCGYverpSKVGEPCPVcggtlepeevdfwn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 79 -------------AI-----FPL----TMLDAVLAQLPLAE---RDSLRwKAETLLAGMGFTPQDMALqSATLSGGQHTR 133
Cdd:TIGR03269 99 lsdklrrrirkriAImlqrtFALygddTVLDNVLEALEEIGyegKEAVG-RAVDLIEMVQLSHRITHI-ARDLSGGEKQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 134 LLLARALIHDPDLLLLDEPSNHLDLPTMLW----LEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRDKTLHYFALPCTA 209
Cdd:TIGR03269 177 VVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 210 ARKALEAKDESDAQRHKAEQKEIDRVtasakrlatwgkvydnEDLARKAKQMEKQVerlkesqtaltagsqwtltlrgda 289
Cdd:TIGR03269 257 VAVFMEGVSEVEKECEVEVGEPIIKV----------------RNVSKRYISVDRGV------------------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 290 LRAdrlleMENLSvppapglpplFNIemarlKSGDRVAIVGRNGCGKSSLMRLI-----------WQQFADE---SAESG 355
Cdd:TIGR03269 297 VKA-----VDNVS----------LEV-----KEGEIFGIVGTSGAGKTTLSKIIagvleptsgevNVRVGDEwvdMTKPG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 356 LKIHPRVSP--GYYDQTLNQLPDDA---TLLDALEPFAPDPQNRKMALI---SAGFPwSRHGQKI-----STLSGGERSR 422
Cdd:TIGR03269 357 PDGRGRAKRyiGILHQEYDLYPHRTvldNLTEAIGLELPDELARMKAVItlkMVGFD-EEKAEEIldkypDELSEGERHR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 423 LLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAV 498
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
....
gi 556426975 499 FERL 502
Cdd:TIGR03269 516 VEEL 519
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
295-537 |
1.03e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 76.87 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSVPPAPGLPP-LFNIEMaRLKSGDRVAIVGRNGCGKS----SLMRL----------IWQQFADESAESGLKIH 359
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPaVDGVSL-TIAPGETVALVGESGSGKStlalALMGLlphggrisgeVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 360 PRVS--PGYYDQTLNQLPDDATLLDALEPFAPDPQNRK----MALISAGFPwSRHGQKISTLSGGERSRLLFVGLTLARY 433
Cdd:COG1123 83 RRIGmvFQDPMTQLNPVTVGDQIAEALENLGLSRAEARarvlELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 434 SLLMLDEPTNHLDMEGKE---ALAQTLQQFEG-GVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFERLRESAgla 509
Cdd:COG1123 162 DLLIADEPTTALDVTTQAeilDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA--- 238
|
250 260
....*....|....*....|....*...
gi 556426975 510 tsTAPVIDTAAVQPSPYDDLLERLVALE 537
Cdd:COG1123 239 --AVPRLGAARGRAAPAAAAAEPLLEVR 264
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-153 |
1.11e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.48 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM-----ARVEQ---HLP--DAIFP-LTMLD 87
Cdd:COG0410 19 LHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglpphRIARLgigYVPegRRIFPsLTVEE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 -AVLAQLPLAERDSLRWKAETLLAgmgFTP--QDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:COG0410 98 nLLLGAYARRDRAEVRADLERVYE---LFPrlKERRRQRAgTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-152 |
1.11e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.46 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 3 TLLTAQSLRVDTAFgtlfDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVeqhlpdaifP 82
Cdd:cd03215 3 PVLEVRGLSVKGAV----RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS---------P 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 83 LTMLDAVLAQLPlAERdslrwKAETLLAGMGfTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:cd03215 70 RDAIRAGIAYVP-EDR-----KREGLVLDLS-VAENIAL-SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-157 |
1.68e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.39 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmARVEQHLPDAIFPLT 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAVLAQLPLAErdSLRW----------KAETLLAGMGFTpqDMA-LQSATLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:TIGR01189 80 HLPGLKPELSALE--NLHFwaaihggaqrTIEDALAAVGLT--GFEdLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....
gi 556426975 154 NHLD 157
Cdd:TIGR01189 156 TALD 159
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
24-157 |
1.94e-14 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 73.10 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL--------------MARVEQHLpDAIFPLTMLDAV 89
Cdd:TIGR02315 22 NLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkklrklrrrIGMIFQHY-NLIERLTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 L--------------AQLPLAERDslrwKAETLLAGMGFTpqDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:TIGR02315 101 LhgrlgykptwrsllGRFSEEDKE----RALSALERVGLA--DKAYQRAdQLSGGQQQRVAIARALAQQPDLILADEPIA 174
|
...
gi 556426975 155 HLD 157
Cdd:TIGR02315 175 SLD 177
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-158 |
2.10e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 3 TLLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAIfp 82
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 83 ltmldAVLAQLPLA-ERDSLRwkaetLLAGMGFTP----------QDMAL-QSA---------------TLSGGQHTRLL 135
Cdd:PRK11231 79 -----ALLPQHHLTpEGITVR-----ELVAYGRSPwlslwgrlsaEDNARvNQAmeqtrinhladrrltDLSGGQRQRAF 148
|
170 180
....*....|....*....|...
gi 556426975 136 LARALIHDPDLLLLDEPSNHLDL 158
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-181 |
2.24e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 73.64 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA--------------IFPLTML 86
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLrkkvglvfqfpehqLFEETVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 DAV---LAQLPLAERDSLRwKAETLLAGMGFtPQDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDlP--- 159
Cdd:TIGR04521 102 KDIafgPKNLGLSEEEAEE-RVKEALELVGL-DEEYLERSpFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD-Pkgr 178
|
170 180
....*....|....*....|....
gi 556426975 160 -TMLWLEHFLQNWSG-SFVLVSHD 181
Cdd:TIGR04521 179 kEILDLFKRLHKEKGlTVILVTHS 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-180 |
2.26e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 72.50 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAI---------FPLTMLDAVLAQL 93
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVslvgqepvlFARSLQDNIAYGL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 94 PLAERDSLRWKAETLLAGmGFTPQ-------DMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEH 166
Cdd:cd03248 113 QSCSFECVKEAAQKAHAH-SFISElasgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ 191
|
170
....*....|....*.
gi 556426975 167 FLQNW--SGSFVLVSH 180
Cdd:cd03248 192 ALYDWpeRRTVLVIAH 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-157 |
2.27e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 72.47 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTV-------------ALAGHCLMAR------VEQHLpDAI 80
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaqASPREILALRrrtigyVSQFL-RVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 81 FPLTMLDAVlAQlPLAE----RDSLRWKAETLLAGMGFtPQDM-ALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNH 155
Cdd:COG4778 106 PRVSALDVV-AE-PLLErgvdREEARARARELLARLNL-PERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
..
gi 556426975 156 LD 157
Cdd:COG4778 183 LD 184
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
319-489 |
2.28e-14 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 71.90 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIwQQFADESAES----GLKIHPRV---SPGYYDQTLN-QLPDDATLLDALE--PFA 388
Cdd:cd03226 22 DLYAGEIIALTGKNGAGKTTLAKIL-AGLIKESSGSillnGKPIKAKErrkSIGYVMQDVDyQLFTDSVREELLLglKEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 389 PDPQNRK---MALISAGFPWSRHGQkisTLSGGERSRLLfVGLTLAR-YSLLMLDEPTNHLDMEGKEALAQ---TLQQFE 461
Cdd:cd03226 101 DAGNEQAetvLKDLDLYALKERHPL---SLSGGQKQRLA-IAAALLSgKDLLIFDEPTSGLDYKNMERVGElirELAAQG 176
|
170 180
....*....|....*....|....*...
gi 556426975 462 GGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03226 177 KAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-191 |
3.02e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQ---------HLP---DAIFPLTML 86
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqdllylgHQPgikTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 DAVLAQLPLAERDSLrWKAetlLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLE- 165
Cdd:PRK13538 96 RFYQRLHGPGDDEAL-WEA---LAQVGLAGFEDVP-VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEa 170
|
170 180
....*....|....*....|....*...
gi 556426975 166 HFLQNWS--GSFVLVSHdrQLLDAVTNG 191
Cdd:PRK13538 171 LLAQHAEqgGMVILTTH--QDLPVASDK 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-157 |
3.21e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG-----HCLMARVEQHLPDAIFPLTMLDAVLAQLPL 95
Cdd:PRK13536 58 NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpaRARLARARIGVVPQFDNLDLEFTVRENLLV 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 96 AERdSLRWKAETLLAGMGFTPQDMALQS------ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13536 138 FGR-YFGMSTREIEAVIPSLLEFARLESkadarvSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-184 |
3.41e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 27 LKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA-------IFPLTMLDAVL-----AQLP 94
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvgfVFQSFMLIPTLnalenVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 95 L-----AERDSlRWKAETLLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFL- 168
Cdd:PRK10584 113 AllrgeSSRQS-RNGAKALLEQLGLGKRLDHL-PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLf 190
|
170
....*....|....*....
gi 556426975 169 ---QNWSGSFVLVSHDRQL 184
Cdd:PRK10584 191 slnREHGTTLILVTHDLQL 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-152 |
3.55e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 72.19 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALaGHCLMARVEQH---------LPD--AIF-PLTMLDA 88
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-DGQDITKLPMHkrarlgigyLPQeaSIFrKLTVEEN 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 89 VLAQLPLAERDSLRW--KAETLLAGMGFTPqdMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:cd03218 96 ILAVLEIRGLSKKEReeKLEELLEEFHITH--LRKSKAsSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-183 |
4.25e-14 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 73.68 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 35 LLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmARVEQHLPD--------AIFPLTMLDAVLA------QLPLAERDS 100
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLRHinmvfqsyALFPHMTVEENVAfglkmrKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 101 lRWKAETLLAGMgftpQDMALQSAT-LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD--LPTMLWLE-HFLQNWSG-SF 175
Cdd:TIGR01187 80 -RVLEALRLVQL----EEFADRKPHqLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQLElKTIQEQLGiTF 154
|
....*...
gi 556426975 176 VLVSHDRQ 183
Cdd:TIGR01187 155 VFVTHDQE 162
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-183 |
4.27e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH---CLMAR------VEQHLpdAIFP-LTMLDAV--- 89
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsRLHARdrkvgfVFQHY--ALFRhMTVFDNIafg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQLPLAERDS---LRWKAETLLagmgftpqDMALQS-------ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLP 159
Cdd:PRK10851 99 LTVLPRRERPNaaaIKAKVTQLL--------EMVQLAhladrypAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180
....*....|....*....|....*...
gi 556426975 160 TML----WLEHFLQNWSGSFVLVSHDRQ 183
Cdd:PRK10851 171 VRKelrrWLRQLHEELKFTSVFVTHDQE 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
319-489 |
4.70e-14 |
|
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: 71.47 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFadeSAESGL---------KIHP---RVSPGYYDQ-------TL-------N 372
Cdd:cd03245 26 TIRAGEKVAIIGRVGSGKSTLLKLLAGLY---KPTSGSvlldgtdirQLDPadlRRNIGYVPQdvtlfygTLrdnitlgA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 373 QLPDDATLLDALE-----PFAPD-PQNRKMALisagfpwsrhGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLD 446
Cdd:cd03245 103 PLADDERILRAAElagvtDFVNKhPNGLDLQI----------GERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556426975 447 MEGKEALAQTLQQFEGG--VLLVSHdRQLISQSCNRFWLIEEGKL 489
Cdd:cd03245 173 MNSEERLKERLRQLLGDktLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
297-480 |
4.73e-14 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 71.41 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 297 EMENLSVPpAPGLPPLFNIEmARLKSGDRVAIVGRNGCGKSSLMRLIWQQ----------FADESAESGLKIhprvspGY 366
Cdd:cd03235 1 EVEDLTVS-YGGHPVLEDVS-FEVKPGEFLAIVGPNGAGKSTLLKAILGLlkptsgsirvFGKPLEKERKRI------GY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 367 YDQTLNQLPD-DATLLDALepfapdpqnrKMALISAGFPWSRHGQK---------------------ISTLSGGERSRLL 424
Cdd:cd03235 73 VPQRRSIDRDfPISVRDVV----------LMGLYGHKGLFRRLSKAdkakvdealervglseladrqIGELSGGQQQRVL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 425 FVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF--EG-GVLLVSHDRQLISQSCNR 480
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFDR 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-157 |
5.19e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarvEQHLPDAIFPLTML---DAVLAQLP 94
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVAEACHYLghrNAMKPALT 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556426975 95 LAE--------RDSLRWKAETLLAGMGFtpQDMA-LQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13539 90 VAEnlefwaafLGGEELDIAAALEAVGL--APLAhLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-181 |
5.46e-14 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 71.13 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL---------MARVEQHLpdAIFP-LTMLD 87
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdrdIAMVFQNY--ALYPhMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AV-----LAQLPLAERDS-LRWKAETLLAGmgftpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD---- 157
Cdd:cd03301 92 NIafglkLRKVPKDEIDErVREVAELLQIE-----HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklr 166
|
170 180
....*....|....*....|....
gi 556426975 158 LPTMLWLEHFLQNWSGSFVLVSHD 181
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-187 |
5.88e-14 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 71.28 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARVEQH----------LPDaifpL 83
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgraIPYLRRKigvvfqdfrlLPD----R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 84 TMLDAVLAQLPLAE--RDSLRWKAETLLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTM 161
Cdd:cd03292 94 NVYENVAFALEVTGvpPREIRKRVPAALELVGLSHKHRAL-PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180
....*....|....*....|....*....
gi 556426975 162 LWLEHFLQ--NWSGSFVLVS-HDRQLLDA 187
Cdd:cd03292 173 WEIMNLLKkiNKAGTTVVVAtHAKELVDT 201
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
319-489 |
6.18e-14 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 71.81 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIwqqFADESAESGLKIHPRVSPGYYDQTLNQ----------LPDDATLLDALEPFA 388
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRML---AGLLKPDSGSILIDGEDVRKEPREARRqigvlpdergLYDRLTVRENIRYFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 389 -----PDPQNRK---MALISAGFPWSRHgQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF 460
Cdd:COG4555 100 elyglFDEELKKrieELIELLGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL 178
|
170 180 190
....*....|....*....|....*....|..
gi 556426975 461 ---EGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:COG4555 179 kkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-157 |
6.75e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 70.27 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAA--GTVALAGH--------CLMARVEQHlpdaifpltmlD 87
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRpldkrsfrKIIGYVPQD-----------D 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AVLAQLPLAErdSLRWKAEtllagmgftpqdmaLQSatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03213 92 ILHPTLTVRE--TLMFAAK--------------LRG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-181 |
8.11e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain] Cd Length: 269 Bit Score: 71.91 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL---------------MARVEQHLpdAIFP-LTMLD 87
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrkelrelrrkkISMVFQSF--ALLPhRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AV-----LAQLPLAERdslRWKAETLLAGMGFTPQDMALQSAtLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDlPT-- 160
Cdd:cd03294 122 NVafgleVQGVPRAER---EERAAEALELVGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLir 196
|
170 180
....*....|....*....|....*.
gi 556426975 161 --MlwLEHFLQ---NWSGSFVLVSHD 181
Cdd:cd03294 197 reM--QDELLRlqaELQKTIVFITHD 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
295-504 |
9.49e-14 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 71.23 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSVPpAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkIHP-------------R 361
Cdd:COG1120 1 MLEAENLSVG-YGGRPVLDDVSL-SLPPGEVTALLGPNGSGKSTLLRAL----------AGL-LKPssgevlldgrdlaS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 362 VSP-------GYYDQTlNQLPDDATLLDA--------LEPFA-PDPQNRKM---ALISAGFPWSRHgQKISTLSGGERSR 422
Cdd:COG1120 68 LSRrelarriAYVPQE-PPAPFGLTVRELvalgryphLGLFGrPSAEDREAveeALERTGLEHLAD-RPVDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 423 LLfvgltLARY-----SLLMLDEPTNHLDMEGKEALAQTLQQF---EG-GVLLVSHDRQLISQSCNRFWLIEEGKLSEWH 493
Cdd:COG1120 146 VL-----IARAlaqepPLLLLDEPTSHLDLAHQLEVLELLRRLareRGrTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
250
....*....|...
gi 556426975 494 DAEAVF--ERLRE 504
Cdd:COG1120 221 PPEEVLtpELLEE 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-185 |
1.07e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 70.64 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG--HCLMArveqhLPDAIFP-LT-----MLDAVLA 91
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLG-----LGGGFNPeLTgreniYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 92 QLPLAERDSLRwkAETL-LAGMGftpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEpsnhldlptmlWL----EH 166
Cdd:cd03220 113 GLSRKEIDEKI--DEIIeFSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE-----------VLavgdAA 176
|
170 180
....*....|....*....|....*....
gi 556426975 167 F----------LQNWSGSFVLVSHDRQLL 185
Cdd:cd03220 177 FqekcqrrlreLLKQGKTVILVSHDPSSI 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-157 |
1.18e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------------------MARVEQHLpda 79
Cdd:COG4161 18 LFD-INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsekairllrqkvgMVFQQYNL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 80 iFP-LTMLD----AVLAQLPLAERDSlRWKAETLLAGMGFTpqDMA----LQsatLSGGQHTRLLLARALIHDPDLLLLD 150
Cdd:COG4161 94 -WPhLTVMEnlieAPCKVLGLSKEQA-REKAMKLLARLRLT--DKAdrfpLH---LSGGQQQRVAIARALMMEPQVLLFD 166
|
....*..
gi 556426975 151 EPSNHLD 157
Cdd:COG4161 167 EPTAALD 173
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-157 |
1.37e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.83 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmARVEQHLPDAIFPLT 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 MLDAVLAQLPLAErdSLRWKA--------ETLLAGMGFTP-QDMALqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNH 155
Cdd:cd03231 80 HAPGIKTTLSVLE--NLRFWHadhsdeqvEEALARVGLNGfEDRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
..
gi 556426975 156 LD 157
Cdd:cd03231 156 LD 157
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
15-161 |
1.46e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.41 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 15 AFGTL--FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR-------------VEQH--Lp 77
Cdd:COG1126 10 SFGDLevLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkdinklrrkvgmVFQQfnL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 daiFP-LTMLDAV-LAQ-----LPLAERDSlrwKAETLLA--GMGftpqDMALQS-ATLSGGQHTRLLLARALIHDPDLL 147
Cdd:COG1126 89 ---FPhLTVLENVtLAPikvkkMSKAEAEE---RAMELLErvGLA----DKADAYpAQLSGGQQQRVAIARALAMEPKVM 158
|
170
....*....|....
gi 556426975 148 LLDEPSNHLDlPTM 161
Cdd:COG1126 159 LFDEPTSALD-PEL 171
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-160 |
1.49e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.30 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFG-TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQH--LP---- 77
Cdd:COG4178 363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpyLPlgtl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 -DAI--------FPLTMLDAVL--AQLP-LAER--DSLRWkaetllagmgftpqdmalqSATLSGGQHTRLLLARALIHD 143
Cdd:COG4178 443 rEALlypataeaFSDAELREALeaVGLGhLAERldEEADW-------------------DQVLSLGEQQRLAFARLLLHK 503
|
170
....*....|....*..
gi 556426975 144 PDLLLLDEPSNHLDLPT 160
Cdd:COG4178 504 PDWLFLDEATSALDEEN 520
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-213 |
1.58e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDG--TDSPAAGTVALAG---------HCL---- 68
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGdvtlngeplAAIdapr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 69 MARVEQHLPDA---IFPLTMLDAV-LAQLPLAERD--------SLRWKAetlLAGMGFTPQDmALQSATLSGGQHTRLLL 136
Cdd:PRK13547 81 LARLRAVLPQAaqpAFAFSAREIVlLGRYPHARRAgalthrdgEIAWQA---LALAGATALV-GRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 137 ARAL---------IHDPDLLLLDEPSNHLDLptmlwlehflqnwsgsfvlvSHDRQLLDAVTNgswILRDKTLHYFAL-- 205
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDL--------------------AHQHRLLDTVRR---LARDWNLGVLAIvh 213
|
....*....
gi 556426975 206 -PCTAARKA 213
Cdd:PRK13547 214 dPNLAARHA 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-489 |
1.85e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.09 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGL--------------------KIHPRVspGYYDQTLNqLPDDAT 379
Cdd:COG1131 23 VEPGEIFGLLGPNGAGKTTTIRML----------LGLlrptsgevrvlgedvardpaEVRRRI--GYVPQEPA-LYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 380 LLDALEPFA-----PDPQNRKMA---LISAGFpWSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKE 451
Cdd:COG1131 90 VRENLRFFArlyglPRKEARERIdelLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556426975 452 ALAQTLQQF--EG-GVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:COG1131 169 ELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-185 |
1.88e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmaRVeqhlpdaifpltmldavlaqLPLAE-- 97
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----RV--------------------SALLElg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 98 ---------RDSLRwkaetlLAG--MGFTPQDMA-----------LQSA------TLSGGQHTRLLLARALIHDPDLLLL 149
Cdd:COG1134 97 agfhpeltgRENIY------LNGrlLGLSRKEIDekfdeivefaeLGDFidqpvkTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556426975 150 DEpsnhldlptmlWL----EHF----------LQNWSGSFVLVSHDRQLL 185
Cdd:COG1134 171 DE-----------VLavgdAAFqkkclarireLRESGRTVIFVSHSMGAV 209
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-157 |
2.11e-13 |
|
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: 69.88 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH-----------CLMARVEQHlPdAIFPLTMLDA 88
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrSQIGLVSQE-P-VLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VL-----AQLPLAER-----------DSLRWKAETLLAGMGFTpqdmalqsatLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:cd03249 97 IRygkpdATDEEVEEaakkanihdfiMSLPDGYDTLVGERGSQ----------LSGGQKQRIAIARALLRNPKILLLDEA 166
|
....*
gi 556426975 153 SNHLD 157
Cdd:cd03249 167 TSALD 171
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-181 |
2.37e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.15 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMA----------------------------RV 72
Cdd:PRK11308 32 DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeaqkllrqkiqivfqnpygslnprkKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 73 EQHLPDaifPLtmldAVLAQLPLAERdslRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:PRK11308 112 GQILEE---PL----LINTSLSAAER---REKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 153 SNHLDLPT---MLWLEHFLQNWSG-SFVLVSHD 181
Cdd:PRK11308 182 VSALDVSVqaqVLNLMMDLQQELGlSYVFISHD 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-181 |
2.58e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM------ARVEQHlp 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaerGVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 DAIFP-LTMLDAVLAQLPLA--ERDSLRWKAETLLAGMGFTPQDmALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:PRK11248 79 EGLLPwRNVQDNVAFGLQLAgvEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|.
gi 556426975 155 HLDLPTMLWL-EHFLQNWSGS---FVLVSHD 181
Cdd:PRK11248 158 ALDAFTREQMqTLLLKLWQETgkqVLLITHD 188
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-203 |
2.61e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 72.38 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARVEQHLPDAI--FPLTMLDAVLAQL 93
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLkqwdretFGKHIGYLPQDVelFPGTVAENIARFG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 94 PLAERDSLRWKAEtlLAG-----MGFtPQ----DMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD----LPT 160
Cdd:TIGR01842 417 ENADPEKIIEAAK--LAGvheliLRL-PDgydtVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDeegeQAL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556426975 161 MLWLEHfLQNWSGSFVLVSHDRQLLDAVtNGSWILRDKTLHYF 203
Cdd:TIGR01842 494 ANAIKA-LKARGITVVVITHRPSLLGCV-DKILVLQDGRIARF 534
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-187 |
3.07e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAFG--------TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDG--TDSPAAGTVALaghclma 70
Cdd:COG2401 19 SVLDLSERVAIVLEAFGvelrvverYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 71 rveqhlPDAIFP--LTMLDAVLAQLPLAErdslrwkAETLLAGMGF-TPQDMALQSATLSGGQHTRLLLARALIHDPDLL 147
Cdd:COG2401 92 ------PDNQFGreASLIDAIGRKGDFKD-------AVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556426975 148 LLDEPSNHLDLPTMLWLEHFLQNWS----GSFVLVSHDRQLLDA 187
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLArragITLVVATHHYDVIDD 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-470 |
3.20e-13 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 68.66 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHP--RVSPGYYDQTL-----NQLPDDATLLDALE------ 385
Cdd:COG4133 24 TLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirDAREDYRRRLAylghaDGLKPELTVRENLRfwaaly 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 386 PFAPDPQNRKMALISAGFPWSRHgQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF--EGG 463
Cdd:COG4133 104 GLRADREAIDEALEAVGLAGLAD-LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlaRGG 182
|
....*...
gi 556426975 464 -VLLVSHD 470
Cdd:COG4133 183 aVLLTTHQ 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
16-157 |
3.85e-13 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. 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: 213265 [Multi-domain] Cd Length: 211 Bit Score: 68.67 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 16 FGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarVE-QHLPDAIFPLTML---DAVLA 91
Cdd:cd03298 10 YGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING------VDvTAAPPADRPVSMLfqeNNLFA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 92 QLPLAERDSL------------RWKAETLLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03298 84 HLTVEQNVGLglspglkltaedRQAIEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-180 |
4.09e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.78 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA---------IFPLTMLDAVL 90
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAisvvsqrvhLFSATLRDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 AQLPLAERDSL-----RWKAETLLAGMGftPQDMALQSA--TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT--- 160
Cdd:PRK11160 436 LAAPNASDEALievlqQVGLEKLLEDDK--GLNAWLGEGgrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerq 513
|
170 180
....*....|....*....|.
gi 556426975 161 -MLWLEHFLQNwsGSFVLVSH 180
Cdd:PRK11160 514 iLELLAEHAQN--KTVLMITH 532
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-197 |
5.19e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.37 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVAL-----------AGHCLMARVEQ-----HLPDAIFP-L 83
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGRGRAKRyigilHQEYDLYPhR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 84 TMLDAVLAQLPLAERDSL-RWKAETLLAGMGFTpQDMALQ-----SATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:TIGR03269 381 TVLDNLTEAIGLELPDELaRMKAVITLKMVGFD-EEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556426975 158 LPTMLWLEHFLQN----WSGSFVLVSHDRQLLDAVTNGSWILRD 197
Cdd:TIGR03269 460 PITKVDVTHSILKareeMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-183 |
5.69e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 70.53 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM-ARVEQHLP---------- 77
Cdd:TIGR02142 2 SARFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdSRKGIFLPpekrrigyvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 78 -DA-IFP-LTMLDAVLAQLPLAERDSLRWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:TIGR02142 82 qEArLFPhLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 155 HLDLPTMLWLEHFLQNWSGSF----VLVSHDRQ 183
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFgipiLYVSHSLQ 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-181 |
5.80e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 68.63 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 11 RVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarvEQHLPDAIF--PLTML-- 86
Cdd:COG3840 6 DLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG-------QDLTALPPAerPVSMLfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 D-------AVLAQLPLAERDSLRW------KAETLLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:COG3840 79 EnnlfphlTVAQNIGLGLRPGLKLtaeqraQVEQALERVGLAGLLDRL-PGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 154 NHLDlPT----MLWLEHFLQNWSGSFVL-VSHD 181
Cdd:COG3840 158 SALD-PAlrqeMLDLVDELCRERGLTVLmVTHD 189
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-188 |
7.94e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 70.93 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 22 SLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL----MARVEQH---LPDAI--FPLT-------M 85
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdREELGRHigyLPQDVelFDGTiaeniarF 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 LDA----VLAqlplAERdslrwkaetlLAGMgftpQDMALQ------------SATLSGGQHTRLLLARALIHDPDLLLL 149
Cdd:COG4618 430 GDAdpekVVA----AAK----------LAGV----HEMILRlpdgydtrigegGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556426975 150 DEPSNHLDLPTMLWLEHFLQNWS---GSFVLVSHDRQLLDAV 188
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLLAAV 533
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
265-473 |
8.36e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 265 VERLKESQTALTAGSQWTLTLRGDALRADRLLEMENLSVppapGLP---PLFNIEMARLKSGDRVAIVGRNGCGKSSLMR 341
Cdd:COG4178 332 VDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTL----RTPdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLLR 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 342 LI---WqqfadeSAESGlKIHprvspgyydqtlnqLPDDA--------------TLLDALE-PFAPDPQNR---KMALIS 400
Cdd:COG4178 408 AIaglW------PYGSG-RIA--------------RPAGArvlflpqrpylplgTLREALLyPATAEAFSDaelREALEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 401 AGFP-----------WSRhgqkisTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVS- 468
Cdd:COG4178 467 VGLGhlaerldeeadWDQ------VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISv 540
|
250
....*....|....
gi 556426975 469 ---------HDRQL 473
Cdd:COG4178 541 ghrstlaafHDRVL 554
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-488 |
9.48e-13 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 68.19 E-value: 9.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLI----WQQFADE--------SAESGLKIHPRVspGYYDQTL-NQLPDDATLLDA-- 383
Cdd:COG1119 25 TVKPGEHWAILGPNGAGKSTLLSLItgdlPPTYGNDvrlfgerrGGEDVWELRKRI--GLVSPALqLRFPRDETVLDVvl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 384 ------LEPF-APDPQNRKMA---LISAGFpWSRHGQKISTLSGGERSRLLfvgltLARY-----SLLMLDEPTNHLDME 448
Cdd:COG1119 103 sgffdsIGLYrEPTDEQRERArelLELLGL-AHLADRPFGTLSQGEQRRVL-----IARAlvkdpELLILDEPTAGLDLG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556426975 449 GKEALAQTLQQF--EGG--VLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:COG1119 177 ARELLLALLDKLaaEGAptLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-157 |
9.58e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------------------MARVEQHLpda 79
Cdd:PRK11124 18 LFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsdkairelrrnvgMVFQQYNL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 80 iFP-LTMLD----AVLAQLPLAERDSLRwKAETLLAGMGFTP--QDMALQsatLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:PRK11124 94 -WPhLTVQQnlieAPCRVLGLSKDQALA-RAEKLLERLRLKPyaDRFPLH---LSGGQQQRVAIARALMMEPQVLLFDEP 168
|
....*
gi 556426975 153 SNHLD 157
Cdd:PRK11124 169 TAALD 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
320-443 |
1.21e-12 |
|
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: 65.75 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRL-----------IWQQFADESAESGLKIHPRVspGYYDQTLNQLPD---DATLLDALE 385
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLiagllsptegtILLDGQDLTDDERKSLRKEI--GYVFQDPQLFPRltvRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 386 PFAPDPQNRK------MALISAGFPWSRH-GQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTN 443
Cdd:pfam00005 86 LKGLSKREKDaraeeaLEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-152 |
1.29e-12 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 68.93 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRV--DTAFGTLF--DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSP---AAGTVALAGHCLMarveqHL 76
Cdd:COG0444 1 LLEVRNLKVyfPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL-----KL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 77 PDA------------IF--PLTMLDAVL---AQL--PL-----AERDSLRWKAETLLAGMGFTPQDMALQS--ATLSGGQ 130
Cdd:COG0444 76 SEKelrkirgreiqmIFqdPMTSLNPVMtvgDQIaePLrihggLSKAEARERAIELLERVGLPDPERRLDRypHELSGGM 155
|
170 180
....*....|....*....|..
gi 556426975 131 HTRLLLARALIHDPDLLLLDEP 152
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEP 177
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
296-491 |
1.54e-12 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 70.18 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIwQQFADESAES----GLKIHpRVSPGYYDQTL 371
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-LRFLDPQSGSitlgGVDLR-DLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 372 NQLPDDA-----TLLDALEPFAPDPQNRKM--ALISAGF-PWSRH---------GQKISTLSGGERSRLLFVGLTLARYS 434
Cdd:COG4987 412 AVVPQRPhlfdtTLRENLRLARPDATDEELwaALERVGLgDWLAAlpdgldtwlGEGGRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 435 LLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHDRQLISQsCNRFWLIEEGKLSE 491
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLER-MDRILVLEDGRIVE 549
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-198 |
1.54e-12 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213266 [Multi-domain] Cd Length: 235 Bit Score: 67.36 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL---------MARVEQHLpdAIFP-LTMLDAVL 90
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItnlppekrdISYVPQNY--ALFPhMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 AQLPLAERDSLRWKAETL-LAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQ 169
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLeIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 170 NWSGSF---VL-VSHDrqLLDAvtngsWILRDK 198
Cdd:cd03299 174 KIRKEFgvtVLhVTHD--FEEA-----WALADK 199
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-157 |
1.68e-12 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 67.51 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHClMARVEQHLPDAIFPLTMLDAVLAQLPLAERDS 100
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD-LALADPAWLRRQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 101 L--------RWKAETLLAG---------MGFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03252 98 LadpgmsmeRVIEAAKLAGahdfiselpEGYD-TIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-152 |
1.70e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.66 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmARVE----------------QHLpdAIFP-LTML 86
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG----EPVRfrsprdaqaagiaiihQEL--NLVPnLSVA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556426975 87 DAVLAQLPLAERDSLRWK-----AETLLAGMGFT--PQDMAlqsATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:COG1129 98 ENIFLGREPRRGGLIDWRamrrrARELLARLGLDidPDTPV---GDLSVAQQQLVEIARALSRDARVLILDEP 167
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-160 |
2.55e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 69.77 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHcLMARVEQH--------LPDA--IFPLTMLDAVL 90
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF-SLKDIDRHtlrqfinyLPQEpyIFSGSILENLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 AQL-PLAERDSLrWKA----------ETLLAGMGftpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLP 159
Cdd:TIGR01193 570 LGAkENVSQDEI-WAAceiaeikddiENMPLGYQ---TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
.
gi 556426975 160 T 160
Cdd:TIGR01193 646 T 646
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-170 |
2.61e-12 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR 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: 213218 [Multi-domain] Cd Length: 234 Bit Score: 66.87 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH--------CL---MARVEQhlpDA-IFPLTMLDA 88
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaSLrrqIGLVSQ---DVfLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VLAQLPLAERDSLRWKAETLLAgMGF---TPQ----DMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTm 161
Cdd:cd03251 96 IAYGRPGATREEVEEAARAANA-HEFimeLPEgydtVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES- 173
|
....*....
gi 556426975 162 lwlEHFLQN 170
Cdd:cd03251 174 ---ERLVQA 179
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
313-489 |
3.12e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213264 [Multi-domain] Cd Length: 214 Bit Score: 66.16 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 313 FNIEMARLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLKihpRVSPGYYDQtlnqlpDDATLLDALEPFAPDPQ 392
Cdd:cd03297 13 FTLKIDFDLNEEVTGIFGASGAGKSTLLRCI----------AGLE---KPDGGTIVL------NGTVLFDSRKKINLPPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 393 NRKMALI---SAGFP-----------WSRH----------------------GQKISTLSGGERSRLLFVGLTLARYSLL 436
Cdd:cd03297 74 QRKIGLVfqqYALFPhlnvrenlafgLKRKrnredrisvdelldllgldhllNRYPAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 437 MLDEPTNHLDMEGKEA----LAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03297 154 LLDEPFSALDRALRLQllpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-489 |
3.49e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 65.70 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 321 KSGDRVAIVGRNGCGKSSLMRLI-------------WQQFADESAESGLKIHPRV-SPGYYDqtlNQLPDDATLLDALEP 386
Cdd:cd03268 24 KKGEIYGFLGPNGAGKTTTMKIIlglikpdsgeitfDGKSYQKNIEALRRIGALIeAPGFYP---NLTARENLRLLARLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 387 FAPDpQNRKMALISAGFPWSRHgQKISTLSGGERSRLlfvGLTLA---RYSLLMLDEPTNHLDMEG-KE--ALAQTLQQF 460
Cdd:cd03268 101 GIRK-KRIDEVLDVVGLKDSAK-KKVKGFSLGMKQRL---GIALAllgNPDLLILDEPTNGLDPDGiKElrELILSLRDQ 175
|
170 180
....*....|....*....|....*....
gi 556426975 461 EGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03268 176 GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-157 |
4.35e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGT-LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTdSPAAGTVALAGHCL----MARVEQHL--- 76
Cdd:PRK11174 350 IEAEDLEILSPDGKtLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELreldPESWRKHLswv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 77 ---PdAIFPLTMLDAVLAQLPLAERDSLrWKA----------ETLLAGMGFTPQDmalQSATLSGGQHTRLLLARALIHD 143
Cdd:PRK11174 429 gqnP-QLPHGTLRDNVLLGNPDASDEQL-QQAlenawvseflPLLPQGLDTPIGD---QAAGLSVGQAQRLALARALLQP 503
|
170
....*....|....
gi 556426975 144 PDLLLLDEPSNHLD 157
Cdd:PRK11174 504 CQLLLLDEPTASLD 517
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-157 |
4.69e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.06 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQH---LPD--AIFP-LTMLDAV--LAQ 92
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigyLPEerGLYPkMKVGEQLvyLAR 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 93 LPLAERDSLRWKAETLLAGMGFTP-QDMALQsaTLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG4152 98 LKGLSKAEAKRRADEWLERLGLGDrANKKVE--ELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
296-470 |
5.10e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.54 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKihpRVSPGYYDQT----- 370
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSL-DLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD---GVPVSSLDQDevrrr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 ---LNQLPD--DATLLDALEPFAPDPQNRKM--ALISAGF-PWSRH---------GQKISTLSGGERSRLLFVGLTLARY 433
Cdd:TIGR02868 411 vsvCAQDAHlfDTTVRENLRLARPDATDEELwaALERVGLaDWLRAlpdgldtvlGEGGARLSGGERQRLALARALLADA 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 556426975 434 SLLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHD 470
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHH 529
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
296-492 |
6.90e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 64.74 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPP-LFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWqQFADesAESGlKIH------PRVSPGYYD 368
Cdd:cd03369 7 IEVENLSVRYAPDLPPvLKNVSF-KVKAGEKIGIVGRTGAGKSTLILALF-RFLE--AEEG-KIEidgidiSTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 369 QTLNQLPDDATLLDA-----LEPFA--PDPQNRKMALISAGfpwsrhGqkiSTLSGGERSRLLFVGLTLARYSLLMLDEP 441
Cdd:cd03369 82 SSLTIIPQDPTLFSGtirsnLDPFDeySDEEIYGALRVSEG------G---LNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556426975 442 TNHLDMEGKEALAQTL-QQFEGG-VLLVSHDRQLISqSCNRFWLIEEGKLSEW 492
Cdd:cd03369 153 TASIDYATDALIQKTIrEEFTNStILTIAHRLRTII-DYDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-181 |
9.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.01 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAI---------FPLTML--DAV 89
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLrkkvslvfqFPEAQLfeNTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQL---PL---AERDSLRWKAETLLAGMGFtPQDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDlP--- 159
Cdd:PRK13641 104 LKDVefgPKnfgFSEDEAKEKALKWLKKVGL-SEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD-Pegr 181
|
170 180
....*....|....*....|...
gi 556426975 160 -TMLWLEHFLQNWSGSFVLVSHD 181
Cdd:PRK13641 182 kEMMQLFKDYQKAGHTVILVTHN 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
319-475 |
1.07e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHPrvspgyydqtlNQLPDDATLLDALepFAPDPQNRKMAL 398
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPD-----------NQFGREASLIDAI--GRKGDFKDAVEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 399 ISA-----GFPWSRhgqKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLD----MEGKEALAQTLQQFEGGVLLVSH 469
Cdd:COG2401 119 LNAvglsdAVLWLR---RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITLVVATH 195
|
....*.
gi 556426975 470 DRQLIS 475
Cdd:COG2401 196 HYDVID 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-152 |
1.07e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMarveqHLP--------------DA-IF-PLTMLD 87
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-----HLPmhkrarlgigylpqEAsIFrKLTVED 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 88 AVLAQLPLAERDSLRW--KAETLLAGMGFTPqdMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:COG1137 98 NILAVLELRKLSKKEReeRLEELLEEFGITH--LRKSKAySLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
261-507 |
1.08e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 67.48 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 261 MEKQVERLKESQTALTAGSQWTLTLrgdalradrllemENLSVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLM 340
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPSIEL-------------EDVSFSYPGGRPALDGLSL-TIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 341 RLIwQQFADesAESG-LKIhprvspgyYDQTLNQLPDDA-----------------TLLDALEPFAPDPQNRKM--ALIS 400
Cdd:COG4988 381 NLL-LGFLP--PYSGsILI--------NGVDLSDLDPASwrrqiawvpqnpylfagTIRENLRLGRPDASDEELeaALEA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 401 AGFpW-----------SRHGQKISTLSGGERSRLlfvglTLAR-----YSLLMLDEPTNHLDMEGKEALAQTLQQFEGG- 463
Cdd:COG4988 450 AGL-DefvaalpdgldTPLGEGGRGLSGGQAQRL-----ALARallrdAPLLLLDEPTAHLDAETEAEILQALRRLAKGr 523
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556426975 464 -VLLVSHDRQLISQsCNRFWLIEEGKLSEwhdaEAVFERLRESAG 507
Cdd:COG4988 524 tVILITHRLALLAQ-ADRILVLDDGRIVE----QGTHEELLAKNG 563
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-190 |
1.16e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-MAR-----------------------VEQHLPD 78
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInLVRdkdgqlkvadknqlrllrtrltmVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 79 AIFpLTMLDAVLAQ----LPLAERDSlRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:PRK10619 104 WSH-MTVLENVMEApiqvLGLSKQEA-RERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 556426975 155 HLD---LPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTN 190
Cdd:PRK10619 182 ALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSS 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-181 |
1.18e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHL-----------PDAIFPLTMLDAV 89
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpDDQVFSSTVWDDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 lAQLPL---AERDSLRWKAETLLAGMGFtpQDMALQSAT-LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD------LP 159
Cdd:PRK13647 102 -AFGPVnmgLDKDEVERRVEEALKAVRM--WDFRDKPPYhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgqetLM 178
|
170 180
....*....|....*....|..
gi 556426975 160 TMLWLehfLQNWSGSFVLVSHD 181
Cdd:PRK13647 179 EILDR---LHNQGKTVIVATHD 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-181 |
1.22e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARVEQHLPDaifpltmldavl 90
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskaFARKVAYLPQ------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 aQLPLAERDSLR---------W-------------KAETLLAGMGFTPQDMALQSaTLSGGQHTRLLLARALIHDPDLLL 148
Cdd:PRK10575 93 -QLPAAEGMTVRelvaigrypWhgalgrfgaadreKVEEAISLVGLKPLAHRLVD-SLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 556426975 149 LDEPSNHLDLP---TMLWLEHFLQNWSGSFVL-VSHD 181
Cdd:PRK10575 171 LDEPTSALDIAhqvDVLALVHRLSQERGLTVIaVLHD 207
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-181 |
1.29e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.74 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 26 TLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDaiFPLTMLDAVLAQLPLAERDSlRWKA 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD--YEGTVRDLLSSITKDFYTHP-YFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 106 ETLlagmgfTP----QDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLW----LEHF-LQNWSGSFV 176
Cdd:cd03237 98 EIA------KPlqieQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMaskvIRRFaENNEKTAFV 171
|
....*
gi 556426975 177 lVSHD 181
Cdd:cd03237 172 -VEHD 175
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-152 |
1.31e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 16 FG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR---------------------- 71
Cdd:NF033858 276 FGdfTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiatrrrvgymsqafslygelt 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 72 VEQHLpdaifpltMLDAVLAQLPLAERDSlrwKAETLLAGMGFTPQDMALqSATLSGGQHTRLLLARALIHDPDLLLLDE 151
Cdd:NF033858 356 VRQNL--------ELHARLFHLPAAEIAA---RVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
.
gi 556426975 152 P 152
Cdd:NF033858 424 P 424
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-157 |
1.38e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.91 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMarveqHLPDA-----------IF--PLTMLD 87
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT-----GLSGRelrplrrrmqmVFqdPYASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 ------AVLAQlPL-----AERDSLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:COG4608 110 prmtvgDIIAE-PLrihglASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
.
gi 556426975 157 D 157
Cdd:COG4608 189 D 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-157 |
1.39e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.11 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH--------CLMAR---VEQhlpDA-IFPLTMLD 87
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleSLRRQigvVPQ---DTfLFSGTIRE 432
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 88 AVLAQLPLAERDSLRWKAETLLAG---MGFtPQ--DMAL--QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG1132 433 NIRYGRPDATDEEVEEAAKAAQAHefiEAL-PDgyDTVVgeRGVNLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-187 |
1.49e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.94 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHlpdAIFPLTMLDAVLAqLPlae 97
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR---PYLPLGTLREQLI-YP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 98 rdslrWkaetllagmgftpqdmalqSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSFVL 177
Cdd:cd03223 88 -----W-------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVIS 143
|
170
....*....|
gi 556426975 178 VSHdRQLLDA 187
Cdd:cd03223 144 VGH-RPSLWK 152
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-152 |
1.71e-11 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 64.08 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 22 SLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA----------IFP-LTM---LD 87
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgiayvpqgreIFPrLTVeenLL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 88 AVLAQLPLAERDslrwkaetllagmgfTPQDM-----ALQS------ATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:TIGR03410 98 TGLAALPRRSRK---------------IPDEIyelfpVLKEmlgrrgGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-190 |
1.79e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQhlpDAIFPLTMLDAVLAQLPLAEr 98
Cdd:PRK13643 22 LFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQ---KEIKPVRKKVGVVFQFPESQ- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 99 dslrWKAETLLAGMGFTPQDMALQSA-------------------------TLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:PRK13643 97 ----LFEETVLKDVAFGPQNFGIPKEkaekiaaeklemvgladefwekspfELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556426975 154 NHLDLPT---MLWLEHFLQNWSGSFVLVSHdrqLLDAVTN 190
Cdd:PRK13643 173 AGLDPKArieMMQLFESIHQSGQTVVLVTH---LMDDVAD 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-180 |
2.14e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarveqhlpdaifPLTMLD--------AVLA 91
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV---------------PLVQYDhhylhrqvALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 92 QLPLAERDSLRwkaETLLAGMGFTPQDMALQSAT-------------------------LSGGQHTRLLLARALIHDPDL 146
Cdd:TIGR00958 562 QEPVLFSGSVR---ENIAYGLTDTPDEEIMAAAKaanahdfimefpngydtevgekgsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190
....*....|....*....|....*....|....*...
gi 556426975 147 LLLDEPSNHLDLPTmlwlEHFLQNW----SGSFVLVSH 180
Cdd:TIGR00958 639 LILDEATSALDAEC----EQLLQESrsraSRTVLLIAH 672
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-152 |
2.43e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 16 FGTLF--DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL------------MARVEQHLpdAIF 81
Cdd:PRK11300 15 FGGLLavNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgVVRTFQHV--RLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 82 -PLTMLDAVL-AQ--------------LPL---AERDSLRWkAETLLAGMGFTpqDMALQSA-TLSGGQHTRLLLARALI 141
Cdd:PRK11300 93 rEMTVIENLLvAQhqqlktglfsgllkTPAfrrAESEALDR-AATWLERVGLL--EHANRQAgNLAYGQQRRLEIARCMV 169
|
170
....*....|.
gi 556426975 142 HDPDLLLLDEP 152
Cdd:PRK11300 170 TQPEILMLDEP 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
327-489 |
2.86e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain] Cd Length: 211 Bit Score: 62.98 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 327 AIVGRNGCGKSSLMRLIWQQFADESA----------ESGLKIHPRVspGYYDQTLNqLPDDATLLDALEPFA-----PDP 391
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPSSGtiridgqdvlKQPQKLRRRI--GYLPQEFG-VYPNFTVREFLDYIAwlkgiPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 392 QNRKMA--LISAGFPWSRHGQKISTLSGGERSRllfVGLTLA---RYSLLMLDEPTNHLDMEGKEALAQTLQQFEGG--V 464
Cdd:cd03264 106 EVKARVdeVLELVNLGDRAKKKIGSLSGGMRRR---VGIAQAlvgDPSILIVDEPTAGLDPEERIRFRNLLSELGEDriV 182
|
170 180
....*....|....*....|....*
gi 556426975 465 LLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03264 183 ILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-181 |
3.10e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 65.12 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM-ARVEQHLP-----------DA-IFP-LTmldaV 89
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdSARGIFLPphrrrigyvfqEArLFPhLS----V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 laqlplaerdslrwkAETLLAGMGFTPQDMALQS------------------ATLSGGQHTRLLLARALIHDPDLLLLDE 151
Cdd:COG4148 95 ---------------RGNLLYGRKRAPRAERRISfdevvellgighlldrrpATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 556426975 152 PSNHLDLPTMLWLEHFLQNWSGSF----VLVSHD 181
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELdipiLYVSHS 193
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
312-489 |
3.50e-11 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 62.89 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 312 LFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLKihpRVSPGYY---DQTLNQLPDDATL-------- 380
Cdd:cd03255 20 LKGVSL-SIEKGEFVAIVGPSGSGKSTLLNIL----------GGLD---RPTSGEVrvdGTDISKLSEKELAafrrrhig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 381 -----------LDALEpfapdpqNRKMALISAGFPWS-----------------RHGQKISTLSGGERSRllfvgLTLAR 432
Cdd:cd03255 86 fvfqsfnllpdLTALE-------NVELPLLLAGVPKKerreraeellervglgdRLNHYPSELSGGQQQR-----VAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 433 Y-----SLLMLDEPTNHLDMEGKEALAQTLQQF--EGG--VLLVSHDRQLISQsCNRFWLIEEGKL 489
Cdd:cd03255 154 AlandpKIILADEPTGNLDSETGKEVMELLRELnkEAGttIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-181 |
3.63e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDaifpltmLDAVLAQ-------L 93
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-------IGVVFGQrsqlwwdL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 94 PLaeRDSLRWKA-----------ETL--LAGMgftpqdMALQS------ATLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:COG4586 112 PA--IDSFRLLKaiyripdaeykKRLdeLVEL------LDLGElldtpvRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190
....*....|....*....|....*....|.
gi 556426975 155 HLDLPTMLWLEHFL----QNWSGSFVLVSHD 181
Cdd:COG4586 184 GLDVVSKEAIREFLkeynRERGTTILLTSHD 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-184 |
3.94e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAFG----TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------M 69
Cdd:PRK10535 1 MTALLELKDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 70 ARVEQHLPDAIFP----LTMLD--------AVLAQLPLAERdslRWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLA 137
Cdd:PRK10535 81 AQLRREHFGFIFQryhlLSHLTaaqnvevpAVYAGLERKQR---LLRAQELLQRLGLEDR-VEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556426975 138 RALIHDPDLLLLDEPSNHLD----LPTMLWLeHFLQNWSGSFVLVSHDRQL 184
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDshsgEEVMAIL-HQLRDRGHTVIIVTHDPQV 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-181 |
4.07e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.96 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAG-----TVALAGHCLM---------A 70
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFnyrdvlefrR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 71 RVEQ--HLPDAiFPLTMLDAVLAQL---PLAERDSLRWKAETLLAGMGF---TPQDMALQSATLSGGQHTRLLLARALIH 142
Cdd:PRK14271 102 RVGMlfQRPNP-FPMSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556426975 143 DPDLLLLDEPSNHLDLPTMLWLEHFLQNWSG--SFVLVSHD 181
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-157 |
4.97e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA------IF--PLTMLDA---- 88
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdiqmIFqdPLASLNPrmti 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 89 --VLAQ-----LPLAERDSLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK15079 118 geIIAEplrtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-500 |
5.16e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 2 STLLTAQSLRVdtAFG------TLFDSLSFTLKKGDRIGLLGDNGCGKS-TLLKVLDGTDSPAA----GTVALAGHCLMA 70
Cdd:PRK15134 3 QPLLAIENLSV--AFRqqqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 71 RVEQHLPDA-------IF--------PLTMLDAVLAQLPLAERDSLRWKAETLL------AGMGFTPQDMALQSATLSGG 129
Cdd:PRK15134 81 ASEQTLRGVrgnkiamIFqepmvslnPLHTLEKQLYEVLSLHRGMRREAARGEIlncldrVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 130 QHTRLLLARALIHDPDLLLLDEPSNHLDLPT----MLWLEHFLQNWSGSFVLVSHD----RQLLDAVT---NGSWILRDK 198
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVqaqiLQLLRELQQELNMGLLFITHNlsivRKLADRVAvmqNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 199 TLHYFALPCTA-ARKALEAKDESDAqrhkaeqkeidrvtasakrlatwgkvydnedlarkakqmekqverlkesqtalta 277
Cdd:PRK15134 241 AATLFSAPTHPyTQKLLNSEPSGDP------------------------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 278 gsqwtLTLRGDAlraDRLLEMENLSV--PPAPGL--------PPLFNIEMArLKSGDRVAIVGRNGCGKSS----LMRLI 343
Cdd:PRK15134 266 -----VPLPEPA---SPLLDVEQLQVafPIRKGIlkrtvdhnVVVKNISFT-LRPGETLGLVGESGSGKSTtglaLLRLI 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 344 WQQ----------------------------FADESA------------ESGLKIHPRvspgyydqTLNQLPDDATLLDA 383
Cdd:PRK15134 337 NSQgeiwfdgqplhnlnrrqllpvrhriqvvFQDPNSslnprlnvlqiiEEGLRVHQP--------TLSAAQREQQVIAV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 384 LEPFAPDPQNRKMalisagFPwsrhgqkiSTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKE---ALAQTLQQ- 459
Cdd:PRK15134 409 MEEVGLDPETRHR------YP--------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAqilALLKSLQQk 474
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 556426975 460 FEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFE 500
Cdd:PRK15134 475 HQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-179 |
6.32e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 62.29 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAA---GTVALAGHCL--------MARVEQHlpDAIFP-LTMLDAVL 90
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRkpdqfqkcVAYVRQD--DILLPgLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 --AQLPL------------AERDSLRWKAETLLAGMGFTpqdmalqsaTLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:cd03234 104 ytAILRLprkssdairkkrVEDVLLRDLALTRIGGNLVK---------GISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*
gi 556426975 157 DLPTMLWLEHFLQNW--SGSFVLVS 179
Cdd:cd03234 175 DSFTALNLVSTLSQLarRNRIVILT 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
296-489 |
6.40e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 62.04 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqFADESAESGL---------KIHPRVSPgY 366
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINI-SISAGEFVFLVGPSGAGKSTLLKLI---YKEELPTSGTirvngqdvsDLRGRAIP-Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 367 YDQTLNQLPDDATLLDALEPF-----------APDPQNRK---MALISAGFPwSRHGQKISTLSGGERSRLlfvglTLAR 432
Cdd:cd03292 76 LRRKIGVVFQDFRLLPDRNVYenvafalevtgVPPREIRKrvpAALELVGLS-HKHRALPAELSGGEQQRV-----AIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 433 Y-----SLLMLDEPTNHLDMEGKEALAQTLQQFEGG---VLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03292 150 AivnspTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-491 |
6.75e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG-------HCLMAR-----VEQHLpDAIFPLTMLDA 88
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldHKLAAQlgigiIYQEL-SVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 V---------LAQLPLAERDSLRWKAETLLAGMGFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL--- 156
Cdd:PRK09700 101 LyigrhltkkVCGVNIIDWREMRVRAAMMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnk 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 157 DLPTMLWLEHFLQNWSGSFVLVSHD----RQLLDAVTngswILRDKTlhyfaLPCTAARKALEAKD------ESDAQ-RH 225
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKlaeiRRICDRYT----VMKDGS-----SVCSGMVSDVSNDDivrlmvGRELQnRF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 226 KAEQKEIDRVTASAkrlatwgkVYDNEDLARKAKQMEKQVE-RLKESQTALTAGsqwtltLRGdalrADRLLEMENL--S 302
Cdd:PRK09700 251 NAMKENVSNLAHET--------VFEVRNVTSRDRKKVRDISfSVCRGEILGFAG------LVG----SGRTELMNCLfgV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 303 VPPAPGLPPLFNIEMARLKSGDRVaivgRNGCGKSSLMRLIWQQFADESAESGLKIHPRVSPGYYDQTLNqLPDDATlld 382
Cdd:PRK09700 313 DKRAGGEIRLNGKDISPRSPLDAV----KKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMG-LFHEVD--- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 383 alEPFAPDPQNRKMALISAGFpwsrhGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF-- 460
Cdd:PRK09700 385 --EQRTAENQRELLALKCHSV-----NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLad 457
|
490 500 510
....*....|....*....|....*....|..
gi 556426975 461 EG-GVLLVSHDRQLISQSCNRFWLIEEGKLSE 491
Cdd:PRK09700 458 DGkVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-157 |
7.58e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 64.71 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 3 TLLTAQSLRVDtaF---GTLF----------DSLSFTLKKGDRIGLLGDNGCGKSTL----LKVLdgtdsPAAGTVALAG 65
Cdd:COG4172 274 PLLEARDLKVW--FpikRGLFrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 66 HCLMARVEQHLPDA------IF--PLTMLD-------------AVLA-QLPLAERDSlrwKAETLLAGMGFTPQDMALQS 123
Cdd:COG4172 347 QDLDGLSRRALRPLrrrmqvVFqdPFGSLSprmtvgqiiaeglRVHGpGLSAAERRA---RVAEALEEVGLDPAARHRYP 423
|
170 180 190
....*....|....*....|....*....|....
gi 556426975 124 ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-181 |
7.74e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTdSPAAGTVALAGHCL-------MARVEQHLPDAIFPLTMLdAVLAQLPL 95
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLsdwsaaeLARHRAYLSQQQSPPFAM-PVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 96 AERDSLRwkAETLLAGMGFTPQDMALQS------ATLSGGQHTRLLLARAL--IH---DPD--LLLLDEPSNHLD----L 158
Cdd:COG4138 93 HQPAGAS--SEAVEQLLAQLAEALGLEDklsrplTQLSGGEWQRVRLAAVLlqVWptiNPEgqLLLLDEPMNSLDvaqqA 170
|
170 180
....*....|....*....|...
gi 556426975 159 PTMLWLEHFLQNwSGSFVLVSHD 181
Cdd:COG4138 171 ALDRLLRELCQQ-GITVVMSSHD 192
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-157 |
7.90e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.20 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL----------------MARVEQHLpdaIFPLTML 86
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlknrevpflrrqigMIFQDHHL---LMDRTVY 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 87 DAVlaQLPL----AERDSLRWKAETLLAGMGF--TPQDMALQsatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK10908 98 DNV--AIPLiiagASGDDIRRRVSAALDKVGLldKAKNFPIQ---LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-158 |
1.13e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAIFPL-----TMLDAVLAQ 92
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLaqnatTPGDITVQE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 93 LPLAERDS-----LRWKAE------TLLAGMGFTpqDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDL 158
Cdd:PRK10253 101 LVARGRYPhqplfTRWRKEdeeavtKAMQATGIT--HLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-157 |
1.25e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.34 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHlPDAIF-PLTMLDA 88
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvwdvrrqVGMVFQN-PDNQFvGATVQDD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 89 VLAQLPL--AERDSL--RWKAETLLAGMgftpQDMALQS-ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13635 103 VAFGLENigVPREEMveRVDQALRQVGM----EDFLNREpHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-196 |
1.26e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 34 GLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------------MARVEQHLPDAIFpLTMLDAVLA----QLPLA 96
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllalrqqVATVFQDPEQQIF-YTDIDSDIAfslrNLGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 97 ERDSLRW--KAETLLAGMGFTPQDMalqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD---LPTMLWLEHFLQNW 171
Cdd:PRK13638 110 EAEITRRvdEALTLVDAQHFRHQPI----QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagRTQMIAIIRRIVAQ 185
|
170 180
....*....|....*....|....*
gi 556426975 172 SGSFVLVSHDRQLLDAVTNGSWILR 196
Cdd:PRK13638 186 GNHVIISSHDIDLIYEISDAVYVLR 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-160 |
1.27e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.57 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmaRVEQHLPDA-IFPLTMLDAVLAQLPLaerDSL 101
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISFSSQFSwIMPGTIKENIIFGVSY---DEY 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 102 RWKA--------ETLLAgmgFTPQD---MALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT 160
Cdd:cd03291 128 RYKSvvkacqleEDITK---FPEKDntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-157 |
1.51e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 26 TLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTValaghclMARVE-----QHL-PDaiFPLTmLDAVLAQLPLAERD 99
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------DPELKisykpQYIkPD--YDGT-VEDLLRSITDDLGS 430
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 100 SLrWKAEtLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13409 431 SY-YKSE-IIKPLQLERL-LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-157 |
1.84e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.26 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 11 RVDTAFG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLK-------------VLDGTD--SPAAGTVALAGHCLMARVE 73
Cdd:PRK09493 6 NVSKHFGptQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKvnDPKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 74 QHLpdaiFP-LTMLDAVL---AQLPLAERDSLRWKAETLLAGMGFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLL 149
Cdd:PRK09493 86 FYL----FPhLTALENVMfgpLRVRGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
....*...
gi 556426975 150 DEPSNHLD 157
Cdd:PRK09493 161 DEPTSALD 168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-156 |
1.95e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH---------CLMARV-----EQHL-PDaifpLTM 85
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVaiiyqELHLvPE----MTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 86 LDAV-LAQLP----LAERDSLRWKAETLLAGMG--FTPQdmaLQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:PRK11288 97 AENLyLGQLPhkggIVNRRLLNYEAREQLEHLGvdIDPD---TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-157 |
1.98e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarvEQH--LPDAIFPLTML---DAVLAQLPLAER 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-------QDHttTPPSRRPVSMLfqeNNLFSHLTVAQN 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 99 DSL------------RWKAETLLAGMGFTPQDMALQSAtLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK10771 92 IGLglnpglklnaaqREKLHAIARQMGIEDLLARLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-181 |
2.95e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTA-----QSLRVDTAfgTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLD-----GTDSPAAGTVALAGHCLMA 70
Cdd:PRK14258 1 MSKLIPAikvnnLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmnelESEVRVEGRVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 71 R----------VEQHLPDA-IFPLTMLDAV------LAQLPLAERDSL---RWKAETLLAGMGFTPQDMALQsatLSGGQ 130
Cdd:PRK14258 79 RrvnlnrlrrqVSMVHPKPnLFPMSVYDNVaygvkiVGWRPKLEIDDIvesALKDADLWDEIKHKIHKSALD---LSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 131 HTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNW----SGSFVLVSHD 181
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHN 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-160 |
2.98e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.39 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmaRVeQHLPDA--IFPLTMLDAVLAQLPLAE-RD 99
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----RI-SFSPQTswIMPGTIKDNIIFGLSYDEyRY 518
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 100 SLRWKAETLLAGMGFTPQD----MALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT 160
Cdd:TIGR01271 519 TSVIKACQLEEDIALFPEKdktvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
295-491 |
3.33e-10 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 60.21 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSV--PPAPGLPP-LFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWQQfadESAESG-LKIHPRVSPGYYDQT 370
Cdd:cd03257 1 LLEVKNLSVsfPTGGGSVKaLDDVSF-SIKKGETLGLVGESGSGKSTLARAILGL---LKPTSGsIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 LN----------QLPDDA-----TLLDAL-EPF-------APDPQNRKMALISAGFPWSRH--GQKISTLSGGERSRLLF 425
Cdd:cd03257 77 RKirrkeiqmvfQDPMSSlnprmTIGEQIaEPLrihgklsKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 426 VGLTLARYSLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSE 491
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLkklqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
318-475 |
5.05e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.17 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 318 ARLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAEsgLKIHPRVSPGYYDQTLnQLPDD--ATLLDALEpfapdpqnrk 395
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT--VRRAGGARVAYVPQRS-EVPDSlpLTVRDLVA---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 396 MALISAGFPWSRH---------------------GQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALA 454
Cdd:NF040873 80 MGRWARRGLWRRLtrddraavddalervgladlaGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180
....*....|....*....|....
gi 556426975 455 QTLQQFEG---GVLLVSHDRQLIS 475
Cdd:NF040873 160 ALLAEEHArgaTVVVVTHDLELVR 183
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
319-505 |
5.39e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGL--------KIHPRVSP------GYY-DQT------LNqlpdd 377
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLI----------AGIleptsgrvEVNGRVSAllelgaGFHpELTgreniyLN----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 378 ATLLDalepFAPDPQNRKMALIsAGFpwSRHG----QKISTLSGGERSRLLFvGLTLA-RYSLLMLDeptnhldmegkEA 452
Cdd:COG1134 113 GRLLG----LSRKEIDEKFDEI-VEF--AELGdfidQPVKTYSSGMRARLAF-AVATAvDPDILLVD-----------EV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 453 LA-----------QTLQQF--EGG-VLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFERLRES 505
Cdd:COG1134 174 LAvgdaafqkkclARIRELreSGRtVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-181 |
6.92e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAI---------FPLTML--DAV 89
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVrkrigmvfqFPESQLfeDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQLPLAER------DSLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD----LP 159
Cdd:PRK13646 104 EREIIFGPKnfkmnlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskRQ 183
|
170 180
....*....|....*....|..
gi 556426975 160 TMLWLEHFLQNWSGSFVLVSHD 181
Cdd:PRK13646 184 VMRLLKSLQTDENKTIILVSHD 205
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-200 |
7.07e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAIFPLTML---DAVLAQL-- 93
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLfqsGALFTDMnv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 94 ------PLAE---------RDSLRWKAETL-LAGMGftpqdmALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK11831 102 fdnvayPLREhtqlpapllHSTVMMKLEAVgLRGAA------KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556426975 158 LPTMLWLEHFLQNWSGSF----VLVSHDRQLLDAVTNGSWILRDKTL 200
Cdd:PRK11831 176 PITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-488 |
7.53e-10 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. 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: 213196 [Multi-domain] Cd Length: 178 Bit Score: 58.35 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkihprVSPGYYDQTLnqlpdDATLLDALEPFAPdPQNRKMALI 399
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCI----------AGL-----EEPDSGSILI-----DGEDLTDLEDELP-PLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 400 ---SAGFPWSRHGQKIS-TLSGGERSRllfVGLtlARY-----SLLMLDEPTNHLDMEGK---EALAQTLQQFEG-GVLL 466
Cdd:cd03229 82 fqdFALFPHLTVLENIAlGLSGGQQQR---VAL--ARAlamdpDVLLLDEPTSALDPITRrevRALLKSLQAQLGiTVVL 156
|
170 180
....*....|....*....|..
gi 556426975 467 VSHDRQLISQSCNRFWLIEEGK 488
Cdd:cd03229 157 VTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-185 |
8.09e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 58.63 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 11 RVDTAFGTLFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHClmarveqhlpdaifpltmldAVL 90
Cdd:cd03250 13 GEQETSFTLKD-INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--------------------AYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 AQLPLAERDSLRwkaETLLAGMGFTPQ-------------DMAL-----------QSATLSGGQHTRLLLARALIHDPDL 146
Cdd:cd03250 72 SQEPWIQNGTIR---ENILFGKPFDEEryekvikacalepDLEIlpdgdlteigeKGINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556426975 147 LLLDEPSNHLDLPTMLWL-EH-FLQNWSGS--FVLVSHDRQLL 185
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIfENcILGLLLNNktRILVTHQLQLL 191
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
320-489 |
8.81e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 59.08 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQfadESAESG-LKIHPRVSPgyydqtlnqlpddatLLDA---LEPFAPDPQN-R 394
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGI---YPPDSGtVTVRGRVSS---------------LLGLgggFNPELTGRENiY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 395 KMALISaGFPWSRHGQK-----------------ISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL 457
Cdd:cd03220 107 LNGRLL-GLSRKEIDEKideiiefselgdfidlpVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190
....*....|....*....|....*....|....*
gi 556426975 458 QQF---EGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03220 186 RELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-157 |
1.12e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 59.33 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH-----------CLMARVEQhlpDaifPL--- 83
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeykraKYIGRVFQ---D---PMmgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 84 --TMldAVLAQLPLA----ERDSLRW---KAET-----LLA--GMGFtPQDMALQSATLSGGQHTRLLLARALIHDPDLL 147
Cdd:COG1101 94 apSM--TIEENLALAyrrgKRRGLRRgltKKRRelfreLLAtlGLGL-ENRLDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170
....*....|
gi 556426975 148 LLDEPSNHLD 157
Cdd:COG1101 171 LLDEHTAALD 180
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-157 |
1.15e-09 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 60.89 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHLpdAIFPLTMLDAV 89
Cdd:TIGR02203 349 DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLadytlaslrrqVALVSQDV--VLFNDTIANNI 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 90 ----LAQLPLAE-RDSLR-WKAETLLAGM--GFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:TIGR02203 427 aygrTEQADRAEiERALAaAYAQDFVDKLplGLD-TPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-157 |
1.20e-09 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 58.33 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarvEQHLPDAIF--PLTML---DAVLAQLPLAER 98
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND-------QSHTGLAPYqrPVSMLfqeNNLFAHLTVRQN 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 99 DSL------------RWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:TIGR01277 91 IGLglhpglklnaeqQEKVVDAAQQVGIADY-LDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-163 |
1.32e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.57 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQ------HLP--DAIFPLTM------L 86
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDvhqnmgYCPqfDAIDDLLTgrehlyL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 87 DAVLAQLPLAERDSL-RWKAETLlaGMGFTPQDMAlqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT--MLW 163
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVaNWSIQSL--GLSLYADRLA---GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQArrMLW 2110
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-180 |
1.42e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.77 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVdtAFGT--LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDG-----TDSPAAGTVALAGHC--------LM 69
Cdd:PRK14247 4 IEIRDLKV--SFGQveVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDifkmdvieLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 70 ARVEQ--HLPDAIFPLTMLDAVLAQLPLAE--------RDSLRWKAETllAGMGFTPQD-MALQSATLSGGQHTRLLLAR 138
Cdd:PRK14247 82 RRVQMvfQIPNPIPNLSIFENVALGLKLNRlvkskkelQERVRWALEK--AQLWDEVKDrLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556426975 139 ALIHDPDLLLLDEPSNHLDLPTMLWLEH-FLQ-NWSGSFVLVSH 180
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESlFLElKKDMTIVLVTH 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-152 |
1.68e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 3 TLLTAQSLRVdtafGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARveqHLPDAI-- 80
Cdd:COG1129 255 VVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR---SPRDAIra 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 81 --------------FP---------LTMLDAvLAQLPLAERDSLRWKAETLLAGMGFTPQDMALQSATLSGG--QhtRLL 135
Cdd:COG1129 328 giayvpedrkgeglVLdlsirenitLASLDR-LSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGnqQ--KVV 404
|
170
....*....|....*..
gi 556426975 136 LARALIHDPDLLLLDEP 152
Cdd:COG1129 405 LAKWLATDPKVLILDEP 421
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
321-489 |
2.29e-09 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 57.18 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 321 KSGDRVAIVGRNGCGKSSLMRLIWQQFADESAE-----SGLKIHPRVSP---GYYDQtlnqlpDDaTLLDALEPfapdpq 392
Cdd:cd03213 33 KPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSgevliNGRPLDKRSFRkiiGYVPQ------DD-ILHPTLTV------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 393 nRKMALISAgfpwsrhgqKISTLSGGERSRLLfVGLTL-ARYSLLMLDEPTNHLDMEGKEALAQTLQQF-EGG--VLLVS 468
Cdd:cd03213 100 -RETLMFAA---------KLRGLSGGERKRVS-IALELvSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGrtIICSI 168
|
170 180
....*....|....*....|..
gi 556426975 469 HD-RQLISQSCNRFWLIEEGKL 489
Cdd:cd03213 169 HQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-156 |
2.39e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 22 SLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMarveqHLPDA---------------IFP-LTM 85
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-----RLTPAkahqlgiylvpqeplLFPnLSV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 86 LDAVLAQLPLAERDSLRWKAetLLAGMGfTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:PRK15439 104 KENILFGLPKRQASMQKMKQ--LLAALG-CQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-157 |
2.45e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.06 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVL---DGTDSPAAGTVALAGHCLMAR--------VEQHlpDAIFP-LTM 85
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDAKemraisayVQQD--DLFIPtLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 LDAVL--AQLPLAERDSLRWKAE---TLLAGMGFTP-QDMALQSAT----LSGGQHTRLLLARALIHDPDLLLLDEPSNH 155
Cdd:TIGR00955 117 REHLMfqAHLRMPRRVTKKEKRErvdEVLQALGLRKcANTRIGVPGrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
..
gi 556426975 156 LD 157
Cdd:TIGR00955 197 LD 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
13-201 |
2.50e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.02 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 13 DTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTdSPAAGTVALAGHCL-------MARVEQHLPDAIFPLTM 85
Cdd:PRK03695 5 DVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeawsaaeLARHRAYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 86 LDA----VLAQLPLAERDSLRWKAETLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIH-DPD------LLLLDEPSN 154
Cdd:PRK03695 84 MPVfqylTLHQPDKTRTEAVASALNEVAEALGLDDK-LGRSVNQLSGGEWQRVRLAAVVLQvWPDinpagqLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556426975 155 HLDLPTMLWLEHFLQNWS---GSFVLVSHD--RQLLDAvtNGSWILRDKTLH 201
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCqqgIAVVMSSHDlnHTLRHA--DRVWLLKQGKLL 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-157 |
2.88e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGT---DSPAAGTVALAGHCLMA------- 70
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQRegrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 71 -RVEQHLPDAIFP-------LTMLDAVL----AQLPLAeRDSLRW-----KAETLLA----GMG-FTPQdmalQSATLSG 128
Cdd:PRK09984 81 iRKSRANTGYIFQqfnlvnrLSVLENVLigalGSTPFW-RTCFSWftreqKQRALQAltrvGMVhFAHQ----RVSTLSG 155
|
170 180
....*....|....*....|....*....
gi 556426975 129 GQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-157 |
3.37e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG-----HCLMAR---- 71
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 72 -----------VEQHLPDAifpLTMldAVLAQLPLAER---------DSLRWKAETLLAGMGFTPQDMALQSATLSGGQH 131
Cdd:PRK11701 83 rrrllrtewgfVHQHPRDG---LRM--QVSAGGNIGERlmavgarhyGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQ 157
|
170 180
....*....|....*....|....*.
gi 556426975 132 TRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
319-525 |
3.75e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIwqqfADESAESGLKIHPRVSPgyydqtLNQLPDDATLL--DA-LEPFAPDPQNRK 395
Cdd:PRK11247 34 HIPAGQFVAVVGRSGCGKSTLLRLL----AGLETPSAGELLAGTAP------LAEAREDTRLMfqDArLLPWKKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 396 M------------ALISAGFPwSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLD----MEGKEALAQTLQQ 459
Cdd:PRK11247 104 LglkgqwrdaalqALAAVGLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQ 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 460 FEGGVLLVSHDrqlISQS---CNRFWLIEEGKLSEWHDAEAVFERLRESAGLATSTAPVIDTAAVQPSP 525
Cdd:PRK11247 183 HGFTVLLVTHD---VSEAvamADRVLLIEEGKIGLDLTVDLPRPRRRGSARLAELEAEVLQRVMSRGES 248
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-157 |
4.41e-09 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. 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: 213221 [Multi-domain] Cd Length: 229 Bit Score: 56.85 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG-----------HCLMARVEQHlpDAIFPLTMLDAVLA 91
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslRSMIGVVLQD--TFLFSGTIMENIRL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 92 QLPLAERDslRWKAETLLAGMG----FTPQD----MALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:cd03254 100 GRPNATDE--EVIEAAKEAGAHdfimKLPNGydtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-491 |
4.55e-09 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 56.17 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIwqqFADESAESGLKIHPRVSPGYYDQT-------LNQLPD--DATLLDALepfapd 390
Cdd:cd03247 25 LKQGEKIALLGRSGSGKSTLLQLL---TGDLKPQQGEITLDGVPVSDLEKAlsslisvLNQRPYlfDTTLRNNL------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 391 pqnrkmalisagfpwsrhGQKistLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF--EGGVLLVS 468
Cdd:cd03247 96 ------------------GRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWIT 154
|
170 180
....*....|....*....|...
gi 556426975 469 HDRQLISQScNRFWLIEEGKLSE 491
Cdd:cd03247 155 HHLTGIEHM-DKILFLENGKIIM 176
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
320-474 |
4.73e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAEsgLKIHPRVSPGYYDQTLNQlpdDATLLDALEPFAPDPQNRKMALI 399
Cdd:PRK09544 27 LKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--IKRNGKLRIGYVPQKLYL---DTTLPLTVNRFLRLRPGTKKEDI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 400 SAGFPWSRHG----QKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEAL----AQTLQQFEGGVLLVSHDR 471
Cdd:PRK09544 102 LPALKRVQAGhlidAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHDL 181
|
...
gi 556426975 472 QLI 474
Cdd:PRK09544 182 HLV 184
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-158 |
4.91e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 22 SLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM--------ARVEQHLPDAIFPLT-------ML 86
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyrsQRIRMIFQDPSTSLNprqrisqIL 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 87 DAVL---AQLPLAERDSlrwKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDL 158
Cdd:PRK15112 111 DFPLrlnTDLEPEQREK---QIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-157 |
5.07e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.39 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH--------CLMAR-----VEQHLPDAIFPLTMLD 87
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksLLEVRktvgiVFQNPDDQLFAPTVEE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 88 AVL---AQLPLAERDSLRWKAETLLA-GM-GF---TPQDmalqsatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13639 99 DVAfgpLNLGLSKEEVEKRVKEALKAvGMeGFenkPPHH-------LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-188 |
5.82e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.00 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 5 LTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDS--PAAGTVALAGHclmarveqhlpdaifp 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 83 ltmldaVLAQLPLAERdslrwkaetllAGMGFTpqdMALQS-----------------ATLSGGQHTRLLLARALIHDPD 145
Cdd:cd03217 65 ------DITDLPPEER-----------ARLGIF---LAFQYppeipgvknadflryvnEGFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556426975 146 LLLLDEPSNHLDLPTMLWLEHFLQNWSG---SFVLVSHDRQLLDAV 188
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYI 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
319-491 |
7.04e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 56.73 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIH--PRVSPGYYDQTLNQLPDDATLLD-------ALEPFAP 389
Cdd:cd03252 24 RIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlALADPAWLRRQVGVVLQENVLFNrsirdniALADPGM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 390 DPQNRKMALISAG-------FPWSRH---GQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQ 459
Cdd:cd03252 104 SMERVIEAAKLAGahdfiseLPEGYDtivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHD 183
|
170 180 190
....*....|....*....|....*....|....
gi 556426975 460 FEGG--VLLVSHdRQLISQSCNRFWLIEEGKLSE 491
Cdd:cd03252 184 ICAGrtVIIIAH-RLSTVKNADRIIVMEKGRIVE 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-157 |
7.12e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 26 TLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAghclmARVE---QHL-PDaiFPLTmLDAVLAQLPLAERDSL 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----LKISykpQYIsPD--YDGT-VEEFLRSANTDDFGSS 433
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 102 RWKAEtLLAGMGFTPQdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG1245 434 YYKTE-IIKPLGLEKL-LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-157 |
7.68e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLD--GTDSP---AAGTVALAGHCLMAR---- 71
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPrtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 72 ----------VEQHLPdaiFPLTMLDAVLAQLPLA---ERDSLRWKAETLLAGMGF--TPQDMALQSAT-LSGGQHTRLL 135
Cdd:PRK14239 82 vdlrkeigmvFQQPNP---FPMSIYENVVYGLRLKgikDKQVLDEAVEKSLKGASIwdEVKDRLHDSALgLSGGQQQRVC 158
|
170 180
....*....|....*....|..
gi 556426975 136 LARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALD 180
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-152 |
7.77e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGdRI-GLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmARVEQHLP-DAI----------F----PLT 84
Cdd:COG3845 22 DDVSLTVRPG-EIhALLGENGAGKSTLMKILYGLYQPDSGEILIDG----KPVRIRSPrDAIalgigmvhqhFmlvpNLT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 85 MLDAVL-----AQLPLAERDSLRWKAETLLAGMGFT--PQDMAlqsATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:COG3845 97 VAENIVlglepTKGGRLDRKAARARIRELSERYGLDvdPDAKV---EDLSVGEQQRVEILKALYRGARILILDEP 168
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-157 |
8.87e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.30 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVAL------------AGHCLMARVEQHLPDA-----I 80
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsQQKGLIRQLRQHVGFVfqnfnL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 81 FP-LTMLDAVLaQLPL----AERDSLRWKAETLLAGMGFTPQDMALQSaTLSGGQHTRLLLARALIHDPDLLLLDEPSNH 155
Cdd:PRK11264 97 FPhRTVLENII-EGPVivkgEPKEEATARARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
..
gi 556426975 156 LD 157
Cdd:PRK11264 175 LD 176
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
21-157 |
9.01e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.40 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLM---------AR-----VEQHlpdaiFPL--- 83
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalserelraARrkigmIFQH-----FNLlss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 84 -TMLDAV-----LAQLPLAERDSlrwKAETLLAGMGFT------PqdmalqsATLSGGQHTRLLLARALIHDPDLLLLDE 151
Cdd:COG1135 97 rTVAENValpleIAGVPKAEIRK---RVAELLELVGLSdkadayP-------SQLSGGQKQRVGIARALANNPKVLLCDE 166
|
....*.
gi 556426975 152 PSNHLD 157
Cdd:COG1135 167 ATSALD 172
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-160 |
1.00e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHL---------PDAIFPLTMLDAVL---- 90
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLvayvpqseeVDWSFPVLVEDVVMmgry 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556426975 91 AQLPLAERDSLRWKA--ETLLAGMGFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPT 160
Cdd:PRK15056 107 GHMGWLRRAKKRDRQivTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-157 |
1.05e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclMARVEQHLpdAIFPLTMLDAVLAQLPLAE-R 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQA--WIQNDSLRENILFGKALNEkY 729
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556426975 99 DSLRWKAETLLAGMGFTPQ----DMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSgdrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
328-509 |
1.27e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 328 IVGRNGCGKSSL-MRL-----------IWQQFA-DESAESGLKIHPRVSpgyydqTLNQLPDDA---TLLDALEPF---- 387
Cdd:PRK13638 32 LVGANGCGKSTLfMNLsgllrpqkgavLWQGKPlDYSKRGLLALRQQVA------TVFQDPEQQifyTDIDSDIAFslrn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 388 ---APDPQNRK----MALISA-GFpwsRHgQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQ 459
Cdd:PRK13638 106 lgvPEAEITRRvdeaLTLVDAqHF---RH-QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 460 FEGG---VLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFER--LRESAGLA 509
Cdd:PRK13638 182 IVAQgnhVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACteAMEQAGLT 236
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
24-157 |
1.30e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 55.96 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL------------------------MARVEQHlpda 79
Cdd:COG4598 28 SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpadrrqlqrirtrLGMVFQS---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 80 iFPL----TMLDAVLA------QLPLAErdsLRWKAETLLAGMG------FTPqdmalqsATLSGGQHTRLLLARALIHD 143
Cdd:COG4598 104 -FNLwshmTVLENVIEapvhvlGRPKAE---AIERAEALLAKVGladkrdAYP-------AHLSGGQQQRAAIARALAME 172
|
170
....*....|....
gi 556426975 144 PDLLLLDEPSNHLD 157
Cdd:COG4598 173 PEVMLFDEPTSALD 186
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
296-474 |
1.36e-08 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 57.30 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPpAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIwQQFADESAES----GLKIHPRVSPGYYDQT- 370
Cdd:TIGR02857 322 LEFSGVSVA-YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL-LGFVDPTEGSiavnGVPLADADADSWRDQIa 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 -LNQLPD--DATLLDAL---EPFAPDPQNRKmALISAGF-------PWSRH---GQKISTLSGGERSRLLFVGLTLARYS 434
Cdd:TIGR02857 400 wVPQHPFlfAGTIAENIrlaRPDASDAEIRE-ALERAGLdefvaalPQGLDtpiGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556426975 435 LLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHDRQLI 474
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALA 520
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-186 |
1.51e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.67 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVA--------LAGHCLMARVEQH 75
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedislLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 76 LPD--AIFP-LTMLDAVLAQLPLAE---RDSLRWKAETLLAGMGFTPQDMALQSAtLSGGQHTRLLLARALIHDPDLLLL 149
Cdd:PRK10895 83 LPQeaSIFRrLSVYDNLMAVLQIRDdlsAEQREDRANELMEEFHIEHLRDSMGQS-LSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556426975 150 DEPSNHLDLPTMLWLEHFLQNW--SGSFVLVS-HD-RQLLD 186
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLrdSGLGVLITdHNvRETLA 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-168 |
1.75e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHClMARVEQ--------H 75
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRsrfmaylgH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 76 LPDAIFPLTMLDAVLAQLPLAERDSLRWKAETL-LAGMGFTPQDMALQsatLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:PRK13543 90 LPGLKADLSTLENLHFLCGLHGRRAKQMPGSALaIVGLAGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170
....*....|....
gi 556426975 155 HLDLPTMLWLEHFL 168
Cdd:PRK13543 167 NLDLEGITLVNRMI 180
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
296-500 |
2.00e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLP----PLFNIEMaRLKSGDRVAIVGRNGCGKSSLMR--------------LIWQQFADESAESGLK 357
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkGLDNISF-ELEEGSFVALVGHTGSGKSTLMQhfnallkpssgtitIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 358 -IHPRVSPGYydqtlnQLPD----DATLLDALEpFAP------DPQNRKMA---LISAGFPWSRHGQKISTLSGGERSRL 423
Cdd:PRK13641 82 kLRKKVSLVF------QFPEaqlfENTVLKDVE-FGPknfgfsEDEAKEKAlkwLKKVGLSEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 424 LFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGG---VLLVSHDRQLISQSCNRFWLIEEGKLSEwHDA-EAVF 499
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIK-HASpKEIF 233
|
.
gi 556426975 500 E 500
Cdd:PRK13641 234 S 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-157 |
2.24e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 56.62 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVdtAFGTLF------DSLSFTLKKGDRIGLLGDNGCGKS----TLLKVLDGTDSPAAGTVALAGHCLMa 70
Cdd:COG4172 3 SMPLLSVEDLSV--AFGQGGgtveavKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 71 rveqHLPDA------------IF--PLTMLDAVL---AQlpLAE---------RDSLRWKAETLLAGMGFtPQDMALQSA 124
Cdd:COG4172 80 ----GLSERelrrirgnriamIFqePMTSLNPLHtigKQ--IAEvlrlhrglsGAAARARALELLERVGI-PDPERRLDA 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 556426975 125 ---TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
326-500 |
2.58e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.87 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 326 VAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHPRvspgyydqtlnqlpDDATLLDALEpfapdpqnrkmALISAGFPW 405
Cdd:cd03238 24 VVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSR--------------NKLIFIDQLQ-----------FLIDVGLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 406 SRHGQKISTLSGGERSRL-----LFVGLTlarYSLLMLDEPTNHLDMEGKEALaqtLQQFEG------GVLLVSHDRQLI 474
Cdd:cd03238 79 LTLGQKLSTLSGGELQRVklaseLFSEPP---GTLFILDEPSTGLHQQDINQL---LEVIKGlidlgnTVILIEHNLDVL 152
|
170 180
....*....|....*....|....*.
gi 556426975 475 SQSCnrfWLIEEGKLSEWHDAEAVFE 500
Cdd:cd03238 153 SSAD---WIIDFGPGSGKSGGKVVFS 175
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-183 |
2.61e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 34 GLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAI---------------FP-LTMLDAVLAQLP--- 94
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIklrkevgmvfqqpnpFPhLSIYDNIAYPLKshg 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 95 LAERDSLRWKAETLLAGMGFTPQ---DMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNW 171
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKEvydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170
....*....|....
gi 556426975 172 SG--SFVLVSHDRQ 183
Cdd:PRK14246 200 KNeiAIVIVSHNPQ 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
296-488 |
2.63e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). 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.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 54.75 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVppapG---LPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLI------WQ---QFADESAeSGLKIHPRVS 363
Cdd:cd03224 1 LEVENLNA----GygkSQILFGVSL-TVPEGEIVALLGRNGAGKTTLLKTImgllppRSgsiRFDGRDI-TGLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 364 PG--YYDQTLNQLPD---DATLLDALEPFAPDPQNRKMALISAGFP--WSRHGQKISTLSGGERsRLLFVGLTL-ARYSL 435
Cdd:cd03224 75 AGigYVPEGRRIFPEltvEENLLLGAYARRRAKRKARLERVYELFPrlKERRKQLAGTLSGGEQ-QMLAIARALmSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 436 LMLDEPTnhldmegkEALA-----------QTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:cd03224 154 LLLDEPS--------EGLApkiveeifeaiRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-190 |
2.94e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.73 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 27 LKKGDRIGLLGDNGCGKSTLLKVLDGTDSPaagtvalaghclmarveqhlpdaifpltmldavlaqlplaERDSLRWKAE 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIP----------------------------------------NGDNDEWDGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 107 TLLagmgFTPQDMalqsaTLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTML----WLEHFLQNWSGSFVLVSHDR 182
Cdd:cd03222 62 TPV----YKPQYI-----DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLnaarAIRRLSEEGKKTALVVEHDL 132
|
....*...
gi 556426975 183 QLLDAVTN 190
Cdd:cd03222 133 AVLDYLSD 140
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-157 |
3.15e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMA----RVEQHLP-----DAIFPLTMLDA 88
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeIYRQQVSycaqtPTLFGDTVYDN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 89 VLaqLPLAER----DSLRWKAEtlLAGMGFtPQDMALQSAT-LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK10247 101 LI--FPWQIRnqqpDPAIFLDD--LERFAL-PDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
323-489 |
3.40e-08 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 54.82 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 323 GDRVAIVGRNGCGKSSLMRLIWQQFADESAE---SGLKIH--PRVSPGYYDQTLNQLPDDATLLDALEP----------- 386
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLAGALRPDAGTvdlAGVDLHglSRRARARRVALVEQDSDTAVPLTVRDVvalgriphrsl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 387 FAPDPQ------NRKMALISAGFPWSRhgqKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF 460
Cdd:TIGR03873 107 WAGDSPhdaavvDRALARTELSHLADR---DMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVREL 183
|
170 180 190
....*....|....*....|....*....|..
gi 556426975 461 EGG---VLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:TIGR03873 184 AATgvtVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
320-489 |
3.54e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQqfaDESAESGlkihpRVSpgYYDQTLNQLPDD--ATLLDALepfapdPQNrkmA 397
Cdd:PRK13548 25 LRPGEVVAILGPNGAGKSTLLRALSG---ELSPDSG-----EVR--LNGRPLADWSPAelARRRAVL------PQH---S 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 398 LISAGF-----------PWSRHGQK---------------------ISTLSGGERSRLlfvglTLAR-----------YS 434
Cdd:PRK13548 86 SLSFPFtveevvamgraPHGLSRAEddalvaaalaqvdlahlagrdYPQLSGGEQQRV-----QLARvlaqlwepdgpPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 435 LLMLDEPTNHLDMEGKEALAQTLQQF----EGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-153 |
3.93e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.50 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarveQHLPDAIFPLTMLDAVlAQLPLAERDSLR 102
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG--------KDITDWQTAKIMREAV-AIVPEGRRVFSR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 103 WKAETLLAGMGFTPQDMALQ--------------------SATLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:PRK11614 95 MTVEENLAMGGFFAERDQFQerikwvyelfprlherriqrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-157 |
4.06e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQ-HLPdaifPLTMLDAVLAQLP--- 94
Cdd:PRK13634 23 LYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkKLK----PLRKKVGIVFQFPehq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 95 ------------------LAERDSLRwKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:PRK13634 98 lfeetvekdicfgpmnfgVSEEDAKQ-KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
.
gi 556426975 157 D 157
Cdd:PRK13634 177 D 177
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-157 |
4.53e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 2 STLLTAQSLRVDTAFGT-LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL------------ 68
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmklre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 69 -MARVEQHLPDAIFPLTMLD-----AVLAQLPlaeRDSLRWKAETLLAGMGFTPQDMALQSAtLSGGQHTRLLLARALIH 142
Cdd:PRK13636 83 sVGMVFQDPDNQLFSASVYQdvsfgAVNLKLP---EDEVRKRVDNALKRTGIEHLKDKPTHC-LSFGQKKRVAIAGVLVM 158
|
170
....*....|....*
gi 556426975 143 DPDLLLLDEPSNHLD 157
Cdd:PRK13636 159 EPKVLVLDEPTAGLD 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
21-157 |
5.03e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDA------IF------------- 81
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqigmIFqhfnllssrtvfd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 82 ----PLTmldavLAQLPLAERDSlrwKAETLLAGMGFTpqDMALQ-SATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:PRK11153 102 nvalPLE-----LAGTPKAEIKA---RVTELLELVGLS--DKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
|
.
gi 556426975 157 D 157
Cdd:PRK11153 172 D 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-157 |
5.07e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 10 LRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVeqhlpdaifPLTMLDAV 89
Cdd:PRK15439 269 LTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---------TAQRLARG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 LAQLP-------LAERDSLRWKAETLLAG-MGF---TPQDMAL----------------QSA-TLSGGQHTRLLLARALI 141
Cdd:PRK15439 340 LVYLPedrqssgLYLDAPLAWNVCALTHNrRGFwikPARENAVleryrralnikfnhaeQAArTLSGGNQQKVLIAKCLE 419
|
170
....*....|....*.
gi 556426975 142 HDPDLLLLDEPSNHLD 157
Cdd:PRK15439 420 ASPQLLIVDEPTRGVD 435
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
314-474 |
5.22e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 314 NIEMARLKSGDRVAIVGRNGCGKSSLMRLIwqqfADE-SAESGlKIHPRVSPGYYDQTLNqlPD-DATLLDALEPFAPDP 391
Cdd:COG1245 357 EVEGGEIREGEVLGIVGPNGIGKTTFAKIL----AGVlKPDEG-EVDEDLKISYKPQYIS--PDyDGTVEEFLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 392 QNRKMALISAGFPWSRH---GQKISTLSGGERSRLLfVGLTLARYS-LLMLDEPTNHLDMEGKEALAQTLQQF----EGG 463
Cdd:COG1245 430 FGSSYYKTEIIKPLGLEkllDKNVKDLSGGELQRVA-IAACLSRDAdLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKT 508
|
170
....*....|.
gi 556426975 464 VLLVSHDRQLI 474
Cdd:COG1245 509 AMVVDHDIYLI 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
292-504 |
5.89e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 292 ADRLLEMENLSVppAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMR------------------------------ 341
Cdd:PLN03073 174 AIKDIHMENFSI--SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddtta 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 342 --------------------LIWQQ----FADESAESGLKIHPRVSPGYYDQTLNQLPDDATLLDAlepfapDPQNRKMA 397
Cdd:PLN03073 252 lqcvlntdiertqlleeeaqLVAQQreleFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDA------YTAEARAA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 398 LISAGFPWSRHGQ--KISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDRQLIS 475
Cdd:PLN03073 326 SILAGLSFTPEMQvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLN 405
|
250 260
....*....|....*....|....*....
gi 556426975 476 QSCNRFWLIEEGKLSEWHDAEAVFERLRE 504
Cdd:PLN03073 406 TVVTDILHLHGQKLVTYKGDYDTFERTRE 434
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-157 |
6.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.22 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 22 SLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhclmarVEQHLPDAIFPLTMLDAVLAQLPlaerdSL 101
Cdd:PRK13644 20 NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG------IDTGDFSKLQGIRKLVGIVFQNP-----ET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 102 RWKAETLLAGMGFTPQ-------------DMAL-----------QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13644 89 QFVGRTVEEDLAFGPEnlclppieirkrvDRALaeiglekyrhrSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
295-499 |
6.62e-08 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. 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: 213225 [Multi-domain] Cd Length: 233 Bit Score: 53.74 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSV---PPAPGLPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkihprvspgyydqtl 371
Cdd:cd03258 1 MIELKNVSKvfgDTGGKVTALKDVSLS-VPKGEIFGIIGRSGAGKSTLIRCI----------NGL--------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 372 nQLPD------DATLLDALEPFAPDPQNRKMALISAGFP--WSR------------------------------------ 407
Cdd:cd03258 55 -ERPTsgsvlvDGTDLTLLSGKELRKARRRIGMIFQHFNllSSRtvfenvalpleiagvpkaeieervlellelvgledk 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 408 HGQKISTLSGGERSRllfVGLtlARY-----SLLMLDEPTNHLDMEGKEA----LAQTLQQFEGGVLLVSHDRQLISQSC 478
Cdd:cd03258 134 ADAYPAQLSGGQKQR---VGI--ARAlannpKVLLCDEATSALDPETTQSilalLRDINRELGLTIVLITHEMEVVKRIC 208
|
250 260
....*....|....*....|.
gi 556426975 479 NRFWLIEEGKLSEWHDAEAVF 499
Cdd:cd03258 209 DRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-160 |
7.40e-08 |
|
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: 53.39 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarveqhlpDaIFPLTMldavlaqlplaer 98
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ-----------D-IREVTL------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 99 DSLRwkaetllAGMGFTPQDMALQSAT-----------------------------------------------LSGGQH 131
Cdd:cd03253 71 DSLR-------RAIGVVPQDTVLFNDTigynirygrpdatdeevieaakaaqihdkimrfpdgydtivgerglkLSGGEK 143
|
170 180
....*....|....*....|....*....
gi 556426975 132 TRLLLARALIHDPDLLLLDEPSNHLDLPT 160
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHT 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
319-492 |
7.58e-08 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain] Cd Length: 213 Bit Score: 52.91 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkIHP---RVSPGyyDQTLNQLP----------DDATL----- 380
Cdd:cd03259 22 TVEPGEFLALLGPSGCGKTTLLRLI----------AGL-ERPdsgEILID--GRDVTGVPperrnigmvfQDYALfphlt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 381 --------LDALEPFAPDPQNRKMALIsAGFPWSRHGQ-KISTLSGGERSRllfVGL--TLARY-SLLMLDEPTNHLDME 448
Cdd:cd03259 89 vaeniafgLKLRGVPKAEIRARVRELL-ELVGLEGLLNrYPHELSGGQQQR---VALarALAREpSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556426975 449 GKEAL----AQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEW 492
Cdd:cd03259 165 LREELreelKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-152 |
7.67e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTV-ALAGHclMArvEQHLPDAIFP----------------L 83
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGD--MA--DARHRRAVCPriaympqglgknlyptL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 84 TM---LD--AVLAQLPLAERdslRWKAETLLAGMGFTP-QDMAlqSATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:NF033858 94 SVfenLDffGRLFGQDAAER---RRRIDELLRATGLAPfADRP--AGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
296-481 |
8.68e-08 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 52.05 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPpAPGLPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkiHPrvspgyydqtlnqlP 375
Cdd:cd03216 1 LELRGITKR-FGGVKALDGVSLS-VRRGEVHALLGENGAGKSTLMKIL----------SGL--YK--------------P 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 376 DDATLLDALEPFAPDpqNRKMALisagfpwsRHGqkIST---LSGGERSRLLfVGLTLARYS-LLMLDEPTNHLDMEGKE 451
Cdd:cd03216 53 DSGEILVDGKEVSFA--SPRDAR--------RAG--IAMvyqLSVGERQMVE-IARALARNArLLILDEPTAALTPAEVE 119
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 452 ALAQTLQQF--EG-GVLLVSHDRQLISQSCNRF 481
Cdd:cd03216 120 RLFKVIRRLraQGvAVIFISHRLDEVFEIADRV 152
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-157 |
8.76e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVE----------QHlpDAIF-PLTMLDAV 89
Cdd:TIGR01257 947 DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDavrqslgmcpQH--NILFhHLTVAEHI 1024
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 L--AQLPLAERDSLRWKAETLLAGMGFTPQDMAlQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:TIGR01257 1025 LfyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-488 |
8.87e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain] Cd Length: 210 Bit Score: 52.67 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAE-----SGLKIHPRVSPGYydqtlnqLPD------DATLLDALEPFA 388
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEvlfdgKPLDIAARNRIGY-------LPEerglypKMKVIDQLVYLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 389 pdpQNRKMAlISAGFPWSRH-----------GQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL 457
Cdd:cd03269 96 ---QLKGLK-KEEARRRIDEwlerlelseyaNKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190
....*....|....*....|....*....|....
gi 556426975 458 QQFEGG---VLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:cd03269 172 RELARAgktVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
35-157 |
9.70e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.50 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 35 LLGDNGCGKSTLLKVL------------------DGTD--SPAAGTVALAGHCLMarVEQHL-PdaiFPLTMLDAVLAQL 93
Cdd:COG1117 42 LIGPSGCGKSTLLRCLnrmndlipgarvegeillDGEDiyDPDVDVVELRRRVGM--VFQKPnP---FPKSIYDNVAYGL 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 94 PLAE---RDSLRWKAETLLagmgftpQDMAL---------QSAT-LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:COG1117 117 RLHGiksKSELDEIVEESL-------RKAALwdevkdrlkKSALgLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
296-491 |
1.20e-07 |
|
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: 53.00 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWqQFADESAES----GLKIHprvspgyyDQTL 371
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSF-TIPAGKKVAIVGPSGSGKSTILRLLF-RFYDVSSGSilidGQDIR--------EVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 372 NQL-------PDDATLLDAL--------EPFAPDPQNRKMALISA------GFPW---SRHGQKISTLSGGERSRLLFVG 427
Cdd:cd03253 71 DSLrraigvvPQDTVLFNDTigynirygRPDATDEEVIEAAKAAQihdkimRFPDgydTIVGERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 428 LTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHDRQLISqSCNRFWLIEEGKLSE 491
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRLSTIV-NADKIIVLKDGRIVE 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-190 |
1.41e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.21 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMArveQHLPDAIFPLTMLDAVLAQLPLAEr 98
Cdd:PRK13649 23 LFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS---TSKNKDIKQIRKKVGLVFQFPESQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 99 dslrWKAETLLAGMGFTPQD----------MALQSAT---------------LSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:PRK13649 98 ----LFEETVLKDVAFGPQNfgvsqeeaeaLAREKLAlvgiseslfeknpfeLSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556426975 154 NHLDlPT----MLWLEHFLQNWSGSFVLVSHdrqLLDAVTN 190
Cdd:PRK13649 174 AGLD-PKgrkeLMTLFKKLHQSGMTIVLVTH---LMDDVAN 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
318-528 |
1.56e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.69 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 318 ARLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAE---SGLKIHPRvSPGYYDQTLNQLPDDATL-------------- 380
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTvlvAGDDVEAL-SARAASRRVASVPQDTSLsfefdvrqvvemgr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 381 ---LDALEPFAPDPQ---NRKMALIS-AGFPwsrhGQKISTLSGGERSRLLfvgltLAR-----YSLLMLDEPTNHLDME 448
Cdd:PRK09536 103 tphRSRFDTWTETDRaavERAMERTGvAQFA----DRPVTSLSGGERQRVL-----LARalaqaTPVLLLDEPTASLDIN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 449 GKE---ALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVF--ERLRESAG--LATSTAPVIDTAAV 521
Cdd:PRK09536 174 HQVrtlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLtaDTLRAAFDarTAVGTDPATGAPTV 253
|
....*..
gi 556426975 522 QPSPYDD 528
Cdd:PRK09536 254 TPLPDPD 260
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
230-474 |
1.80e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.98 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 230 KEIDRVTASAKRLATWGKVYDNEDLARKAKQMEKQVERLKESQTA--LTAGsqwtltlRGDALRADRLLEMEN--LSVPP 305
Cdd:TIGR00954 391 RDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNsnLVPG-------RGIVEYQDNGIKFENipLVTPN 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 306 APGLPPLFNIEmarLKSGDRVAIVGRNGCGKSSLMRL---IWQQFA---DESAESGL-----------------KIHPRV 362
Cdd:TIGR00954 464 GDVLIESLSFE---VPSGNNLLICGPNGCGKSSLFRIlgeLWPVYGgrlTKPAKGKLfyvpqrpymtlgtlrdqIIYPDS 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 363 S-----PGYYDQTLNQLPDDATLLDALEpfapdpqnRKMALiSAGFPWSrhgqkiSTLSGGERSRLLFVGLTLARYSLLM 437
Cdd:TIGR00954 541 SedmkrRGLSDKDLEQILDNVQLTHILE--------REGGW-SAVQDWM------DVLSGGEKQRIAMARLFYHKPQFAI 605
|
250 260 270
....*....|....*....|....*....|....*....
gi 556426975 438 LDEPTN--HLDMEGKeaLAQTLQQFEGGVLLVSHDRQLI 474
Cdd:TIGR00954 606 LDECTSavSVDVEGY--MYRLCREFGITLFSVSHRKSLW 642
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-157 |
1.81e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.88 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMAR-----------VEQHLPDAIFPltmldav 89
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevrkfvglVFQNPDDQIFS------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 laqlPLAERDslrwkaetllagMGFTPQDMALQSAT------------------------LSGGQHTRLLLARALIHDPD 145
Cdd:PRK13652 94 ----PTVEQD------------IAFGPINLGLDEETvahrvssalhmlgleelrdrvphhLSGGEKKRVAIAGVIAMEPQ 157
|
170
....*....|..
gi 556426975 146 LLLLDEPSNHLD 157
Cdd:PRK13652 158 VLVLDEPTAGLD 169
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
295-491 |
2.79e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSVP-PAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLI---WQQFADESAESGLKIHprvspGYYDQT 370
Cdd:PRK11160 338 SLTLNNVSFTyPDQPQPVLKGLSL-QIKAGEKVALLGRTGCGKSTLLQLLtraWDPQQGEILLNGQPIA-----DYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 L-------NQLPD--DATLLDALEPFAPDPQNRKMA----------LISAGFP---WSRHGQKisTLSGGERSRllfvgL 428
Cdd:PRK11160 412 LrqaisvvSQRVHlfSATLRDNLLLAAPNASDEALIevlqqvglekLLEDDKGlnaWLGEGGR--QLSGGEQRR-----L 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 429 TLARY-----SLLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHDRQLISQsCNRFWLIEEGKLSE 491
Cdd:PRK11160 485 GIARAllhdaPLLLLDEPTEGLDAETERQILELLAEHAQNktVLMITHRLTGLEQ-FDRICVMDNGQIIE 553
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-158 |
3.68e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 51.62 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-------MARV------EQHLPDAI------- 80
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsreLAKRlailrqENHINSRLtvrelva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 81 ---FP-----LT-----MLDAVLAQL---PLAER--DslrwkaetllagmgftpqdmalqsaTLSGGQHTRLLLARALIH 142
Cdd:COG4604 98 fgrFPyskgrLTaedreIIDEAIAYLdleDLADRylD-------------------------ELSGGQRQRAFIAMVLAQ 152
|
170
....*....|....*.
gi 556426975 143 DPDLLLLDEPSNHLDL 158
Cdd:COG4604 153 DTDYVLLDEPLNNLDM 168
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-160 |
4.04e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGH---------------------CLMAR-VEQHL-- 76
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrniavvfqdaGLFNRsIEDNIrv 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 77 --PDAIFPLTMLDAVLAQ-LPLAERDSLRWkaETLLAGMGftpqdmalqsATLSGGQHTRLLLARALIHDPDLLLLDEPS 153
Cdd:PRK13657 432 grPDATDEEMRAAAERAQaHDFIERKPDGY--DTVVGERG----------RQLSGGERQRLAIARALLKDPPILILDEAT 499
|
....*..
gi 556426975 154 NHLDLPT 160
Cdd:PRK13657 500 SALDVET 506
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-186 |
4.56e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 28 KKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTV-----------ALAGHCLMARVEQHLPDAIFPlTMLDAVLAQLP-- 94
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVKV-IVKPQYVDLIPka 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 95 -------LAERDSLRWKAETLLAGMGFTP-QDMALQSatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLP---TMLW 163
Cdd:cd03236 103 vkgkvgeLLKKKDERGKLDELVDQLELRHvLDRNIDQ--LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAAR 180
|
170 180
....*....|....*....|...
gi 556426975 164 LEHFLQNWSGSFVLVSHDRQLLD 186
Cdd:cd03236 181 LIRELAEDDNYVLVVEHDLAVLD 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
319-489 |
4.74e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHPRVspgyydqTLNQLP---DDATLLDALEPFAPDPQNRK 395
Cdd:PRK13547 23 RIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDV-------TLNGEPlaaIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 396 MA-----LISAG-FPWSRH-------------------------GQKISTLSGGERSRLLFV-----------GLTLARY 433
Cdd:PRK13547 96 FAfsareIVLLGrYPHARRagalthrdgeiawqalalagatalvGRDVTTLSGGELARVQFArvlaqlwpphdAAQPPRY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 434 slLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:PRK13547 176 --LLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-197 |
4.85e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 16 FG--TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAA--GTVALAGHCLMAR------------VEQHLpdA 79
Cdd:TIGR02633 11 FGgvKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASnirdteragiviIHQEL--T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 80 IFP-LTMLDAVLA----QLP--LAERDSLRWKAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:TIGR02633 89 LVPeLSVAENIFLgneiTLPggRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556426975 153 SNHL---DLPTMLWLEHFLQNWSGSFVLVSHDRQLLDAVTNGSWILRD 197
Cdd:TIGR02633 169 SSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
314-491 |
5.20e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 51.25 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 314 NIEMARLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLkihPRVSPGYYDQTLNqlPD-----DATLLDALEPFA 388
Cdd:cd03237 16 EVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIK--ADyegtvRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 389 PDPQNRK-----MALISAgfpwsrHGQKISTLSGGERSRLLfVGLTLAR-YSLLMLDEPTNHLDMEGKEALAQTLQQF-- 460
Cdd:cd03237 91 THPYFKTeiakpLQIEQI------LDREVPELSGGELQRVA-IAACLSKdADIYLLDEPSAYLDVEQRLMASKVIRRFae 163
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 461 --EGGVLLVSHDRQLISQSCNRFwLIEEGKLSE 491
Cdd:cd03237 164 nnEKTAFVVEHDIIMIDYLADRL-IVFEGEPSV 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
323-478 |
5.79e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.14 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 323 GDRVAIVGRNGCGKSSLMRL-----------IW------QQFADESAES--GLKIHPRVSPGyyDQTLNQLpddatLLDA 383
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTlsrlmtpahghVWldgehiQHYASKEVARriGLLAQNATTPG--DITVQEL-----VARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 384 LEPFAP--------DPQNRKMALISAGFPwSRHGQKISTLSGGERSRlLFVGLTLAR-YSLLMLDEPTNHLDMEGKEALA 454
Cdd:PRK10253 106 RYPHQPlftrwrkeDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQR-AWIAMVLAQeTAIMLLDEPTTWLDISHQIDLL 183
|
170 180
....*....|....*....|....*...
gi 556426975 455 QTLQQF--EGGVLL--VSHDrqlISQSC 478
Cdd:PRK10253 184 ELLSELnrEKGYTLaaVLHD---LNQAC 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-157 |
6.62e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 3 TLLTAQSLRVDTAFGTL-FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----MARVEQ-- 74
Cdd:COG3845 256 VVLEVENLSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRLgv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 75 -HLPD------AIFPLTMLD-AVL---AQLPLAERDSLRWK-----AETLLAGMGFTPQDMALQSATLSGG--QhtRLLL 136
Cdd:COG3845 336 aYIPEdrlgrgLVPDMSVAEnLILgryRRPPFSRGGFLDRKairafAEELIEEFDVRTPGPDTPARSLSGGnqQ--KVIL 413
|
170 180
....*....|....*....|.
gi 556426975 137 ARALIHDPDLLLLDEPSNHLD 157
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLD 434
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-157 |
6.67e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHlPDAIF-PLTMLDA 88
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwdirhkIGMVFQN-PDNQFvGATVEDD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 89 VLAQL-----PLAERDSlRWKAETLLAGMgftpQDMAL-QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13650 103 VAFGLenkgiPHEEMKE-RVNEALELVGM----QDFKErEPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
312-496 |
6.81e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.48 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 312 LFNIEMArLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHP--RVSPGYYDQTLN---QLPD--DATLLDAL 384
Cdd:PRK10247 23 LNNISFS-LRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDisTLKPEIYRQQVSycaQTPTlfGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 385 E-PF-----APDPQNRKMALISAGFPWSRHGQKISTLSGGERSRllfvgLTLARY-----SLLMLDEPTNHLDMEGK--- 450
Cdd:PRK10247 102 IfPWqirnqQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQR-----ISLIRNlqfmpKVLLLDEITSALDESNKhnv 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556426975 451 -EALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGklSEWHDAE 496
Cdd:PRK10247 177 nEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA--GEMQEAR 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
294-506 |
6.89e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 294 RLLEMENLSVPPAPGLPPLFNIEMARlksGDRVAIVGRNGCGKS------------SLMRLIWQQFADesaesGLKIHPR 361
Cdd:PRK10418 3 QQIELRNIALQAAQPLVHGVSLTLQR---GRVLALVGGSGSGKSltcaaalgilpaGVRQTAGRVLLD-----GKPVAPC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 362 VSPGYYDQTLNQLP-------------------------DDATLLDALEPFAPDPQNRKMALisagFPWSrhgqkistLS 416
Cdd:PRK10418 75 ALRGRKIATIMQNPrsafnplhtmhtharetclalgkpaDDATLTAALEAVGLENAARVLKL----YPFE--------MS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 417 GGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGK----EALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEW 492
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQarilDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
250
....*....|....
gi 556426975 493 HDAEAVFERLRESA 506
Cdd:PRK10418 223 GDVETLFNAPKHAV 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-511 |
6.98e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSVPPAPGLPPLFNIEMARLKSGDRVAIVGRNGCGKSSLMRLIWQ-----------------QFADESAESGLK 357
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRivelekgrimiddcdvaKFGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 358 IHPRvSPGYYDQTL--NQLP----DDATLLDALE-----------PFAPDPQnrkmalISAGfpwsrhGQKISTlsgGER 420
Cdd:PLN03232 1314 IIPQ-SPVLFSGTVrfNIDPfsehNDADLWEALErahikdvidrnPFGLDAE------VSEG------GENFSV---GQR 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 421 SRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL-QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAE--- 496
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIrEEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQell 1457
|
250
....*....|....*....
gi 556426975 497 ----AVFERLRESAGLATS 511
Cdd:PLN03232 1458 srdtSAFFRMVHSTGPANA 1476
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-151 |
7.76e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.72 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLmarVEQHLPD------AIFPltmlDAVL-AQLPL 95
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAyrqlfsAVFS----DFHLfDRLLG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 96 AERDSLRWKAETLLagmgftpQDMALQSAT-----------LSGGQHTRLLLARALIHDPDLLLLDE 151
Cdd:COG4615 424 LDGEADPARARELL-------ERLELDHKVsvedgrfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-508 |
9.37e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.77 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQqFAdeSAESGLKIH----PRVSPGYYDQTLN------QLPDdATLLDAL---E 385
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNALLG-FL--PYQGSLKINgielRELDPESWRKHLSwvgqnpQLPH-GTLRDNVllgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 386 PFAPDPQnRKMALISAG---FPwSRHGQKISTLSGgERSRLLFVG----LTLAR-----YSLLMLDEPTNHLDMEGKEAL 453
Cdd:PRK11174 448 PDASDEQ-LQQALENAWvseFL-PLLPQGLDTPIG-DQAAGLSVGqaqrLALARallqpCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 454 AQTLQQFEGG--VLLVSHDRQLISQsCNRFWLIEEGKLSEWHDaeavFERLRESAGL 508
Cdd:PRK11174 525 MQALNAASRRqtTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGD----YAELSQAGGL 576
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
296-474 |
9.40e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.45 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPApGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGlkiHP--RVSPG---YYDQT 370
Cdd:cd03217 1 LEIKDLHVSVG-GKEILKGVNL-TIKKGEVHALMGPNGSGKSTLAKTI----------MG---HPkyEVTEGeilFKGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 LNQLPddatlldalepfapdPQNRKMALISAGF--PWSRHGQKISTL--------SGGERSRLLFVGLTLARYSLLMLDE 440
Cdd:cd03217 66 ITDLP---------------PEERARLGIFLAFqyPPEIPGVKNADFlryvnegfSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|....*..
gi 556426975 441 PTNHLDMEGKEALAQTLQQF--EG-GVLLVSHDRQLI 474
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLreEGkSVLIITHYQRLL 167
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-160 |
9.56e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 20 FDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHL----------PDAIF-PLTMLDA 88
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrkigmvfqnPDNQFvGATVEDD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 89 V---LAQLPLAERDSLRWKAETLLA--GMGFTPQdmalQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDlPT 160
Cdd:PRK13642 103 VafgMENQGIPREEMIKRVDEALLAvnMLDFKTR----EPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD-PT 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-157 |
1.05e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEqhlPDAIFPLTML-------DAVLAQLPLA 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP---RDAIRAGIMLcpedrkaEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 97 E-------RDSLRWK-----------AETLLAGMGF-TP---QDMalqsATLSGGQHTRLLLARALIHDPDLLLLDEPSN 154
Cdd:PRK11288 350 DninisarRHHLRAGclinnrweaenADRFIRSLNIkTPsreQLI----MNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
...
gi 556426975 155 HLD 157
Cdd:PRK11288 426 GID 428
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-157 |
1.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.52 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 13 DTAFgTLfDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL----MARVEQHL------PDAIFP 82
Cdd:PRK13648 20 DASF-TL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLRKHIgivfqnPDNQFV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 83 LTMLDAVLA---QLPLAERDSLRWKAETLLAGMGFTPQ-DMALQSatLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13648 98 GSIVKYDVAfglENHAVPYDEMHRRVSEALKQVDMLERaDYEPNA--LSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-180 |
1.12e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.23 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 35 LLGDNGCGKSTLLKVLD-----GTDSPAAGTVALAGHCLMA------RVEQHL------PDAIFPLTMLDAVLAQLPL-- 95
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRNIYSpdvdpiEVRREVgmvfqyPNPFPHLTIYDNVAIGVKLng 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 96 -----AERDS-LRW--KAETLLAGMGFTPQDMAlqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHF 167
Cdd:PRK14267 115 lvkskKELDErVEWalKKAALWDEVKDRLNDYP---SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170
....*....|....*
gi 556426975 168 LQNWSGSF--VLVSH 180
Cdd:PRK14267 192 LFELKKEYtiVLVTH 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
320-473 |
1.12e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.81 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHP--RVSP-----------GYYDQTLNQLPDDATLLDALEP 386
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmsKLSSaakaelrnqklGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 387 F-----APD-PQNRKMALISAGFPWSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF 460
Cdd:PRK11629 112 LligkkKPAeINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
170
....*....|....*..
gi 556426975 461 E----GGVLLVSHDRQL 473
Cdd:PRK11629 192 NrlqgTAFLVVTHDLQL 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-157 |
1.15e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.37 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHL----------PD 78
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrkkigiifqnPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 79 AIF-PLTMLDAVLAQLP--LAERDSLRWKAETLL--AGMG----FTPQDmalqsatLSGGQHTRLLLARALIHDPDLLLL 149
Cdd:PRK13632 94 NQFiGATVEDDIAFGLEnkKVPPKKMKDIIDDLAkkVGMEdyldKEPQN-------LSGGQKQRVAIASVLALNPEIIIF 166
|
....*...
gi 556426975 150 DEPSNHLD 157
Cdd:PRK13632 167 DESTSMLD 174
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-184 |
1.24e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.29 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQH-------------LPDAIFPLT- 84
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtlrdqiiYPDSSEDMKr 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 --MLDAVLAQ-LPLAERDSLrwkaetLLAGMGFTPqdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTM 161
Cdd:TIGR00954 547 rgLSDKDLEQiLDNVQLTHI------LEREGGWSA--VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
170 180
....*....|....*....|...
gi 556426975 162 LWLEHFLQNWSGSFVLVSHDRQL 184
Cdd:TIGR00954 619 GYMYRLCREFGITLFSVSHRKSL 641
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
319-489 |
1.45e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.01 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAesglKIHprvspgYYDQTLNQLPDD--ATLLDALEPFAPDPQNRKM 396
Cdd:PRK11231 24 SLPTGKITALIGPNGCGKSTLLKCFARLLTPQSG----TVF------LGDKPISMLSSRqlARRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 397 -ALISAGFP-----WSRHGQK---------------------ISTLSGGERSRLlFVGLTLARYS-LLMLDEPTNHLDME 448
Cdd:PRK11231 94 rELVAYGRSpwlslWGRLSAEdnarvnqameqtrinhladrrLTDLSGGQRQRA-FLAMVLAQDTpVVLLDEPTTYLDIN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556426975 449 GK---EALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:PRK11231 173 HQvelMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-182 |
1.48e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKV---LDGTDspaaGTVALAGHCLMARVEQH-------LPDAIFPLT--- 84
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAllrLLSTE----GEIQIDGVSWNSVTLQTwrkafgvIPQKVFIFSgtf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 --MLDAvLAQLP------LAERDSLRWKAETLLAGMGFTPQDmalQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:TIGR01271 1309 rkNLDP-YEQWSdeeiwkVAEEVGLKSVIEQFPDKLDFVLVD---GGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180
....*....|....*....|....*..
gi 556426975 157 DLPTMLWLEHFL-QNWSGSFVLVSHDR 182
Cdd:TIGR01271 1385 DPVTLQIIRKTLkQSFSNCTVILSEHR 1411
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
36-183 |
1.56e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.78 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 36 LGDNGCGKSTLLKVLDGTDS-----PAAGTVALAGHCLMAR-------------VEQHlPDAiFPLTMLD--AVLAQL-- 93
Cdd:PRK14243 42 IGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPdvdpvevrrrigmVFQK-PNP-FPKSIYDniAYGARIng 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 94 ------PLAERdSLRWkaetllAGMGFTPQDMALQSA-TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEH 166
Cdd:PRK14243 120 ykgdmdELVER-SLRQ------AALWDEVKDKLKQSGlSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEE 192
|
170
....*....|....*....
gi 556426975 167 FLQNWSGSF--VLVSHDRQ 183
Cdd:PRK14243 193 LMHELKEQYtiIIVTHNMQ 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-174 |
1.65e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALA-GHCLM----------------------ARVEQH 75
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKdinlkwwrskigvvsqdpllfsNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 76 LPDAIFPLTMLDAVLAQLP---------LAERDSLRWKAETLLAGMGFTPQDMAL------------------------- 121
Cdd:PTZ00265 480 IKYSLYSLKDLEALSNYYNedgndsqenKNKRNSCRAKCAGDLNDMSNTTDSNELiemrknyqtikdsevvdvskkvlih 559
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 122 ----------------QSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGS 174
Cdd:PTZ00265 560 dfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
291-488 |
2.08e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.46 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 291 RADRLLEMENLSVPPAPGLPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMR-------------LIWQQFADESAESGLK 357
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININ-IKKGEVTAILGGNGAGKSTLFQnlngilkpssgriLFDGKPIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 358 IHPRVSPGYYDQTlNQLPDDATLLD----ALEPFAPDPQNRKM---ALISAGFPWSRHgQKISTLSGGERSRLLFVGLTL 430
Cdd:PRK13636 80 LRESVGMVFQDPD-NQLFSASVYQDvsfgAVNLKLPEDEVRKRvdnALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556426975 431 ARYSLLMLDEPTNHLDMEG----KEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGvseiMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-156 |
2.34e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGT-----------------------DSPAAGTVALagHCLMARVEQ-HL 76
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegeiifegeelqasnirDTERAGIAII--HQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 77 PDAIFpltmLDAVLAQLPLAERDSLRWKAETLLAGMGFTpQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:PRK13549 100 LENIF----LGNEITPGGIMDYDAMYLRAQKLLAQLKLD-INPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
124-180 |
2.41e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 2.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 124 ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTMLWLEHFLQNWSGSF----VLVSH 180
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREInipiLYVSH 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-487 |
2.49e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMR-LIWQQFADESAESGLKI----------------HPRVSPGYYDQTLNqLPDDATLLD 382
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRhLSGLITGDKSAGSHIELlgrtvqregrlardirKSRANTGYIFQQFN-LVNRLSVLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 383 ---------------ALEPFAPDPQNRKM-ALISAGFPWSRHgQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLD 446
Cdd:PRK09984 106 nvligalgstpfwrtCFSWFTREQKQRALqALTRVGMVHFAH-QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556426975 447 MEGKEALAQTLQ---QFEGGVLLVS-HDRQLISQSCNRFWLIEEG 487
Cdd:PRK09984 185 PESARIVMDTLRdinQNDGITVVVTlHQVDYALRYCERIVALRQG 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
412-489 |
2.50e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.16 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 412 ISTLSGGE--RSRLLFVGL----TLARYS-LLMLDEPTNHLDMEGKEALAQTLQQFE---GGVLLVSHDRQLISQSCNRF 481
Cdd:PRK03695 124 VNQLSGGEwqRVRLAAVVLqvwpDINPAGqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHDLNHTLRHADRV 203
|
....*...
gi 556426975 482 WLIEEGKL 489
Cdd:PRK03695 204 WLLKQGKL 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-157 |
2.83e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.32 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhcLMARVEQHL-------------PDAIFPLTMLD 87
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLwdirnkagmvfqnPDNQIVATIVE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 88 AVLAQLPL---AERDSLRWKAETLLAGMG------FTPQdmalqsaTLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK13633 105 EDVAFGPEnlgIPPEEIRERVDESLKKVGmyeyrrHAPH-------LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
411-501 |
3.42e-06 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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: 213266 [Multi-domain] Cd Length: 235 Bit Score: 48.49 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 411 KISTLSGGERSRllfvgLTLARY-----SLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRF 481
Cdd:cd03299 126 KPETLSGGEQQR-----VAIARAlvvnpKILLLDEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHDFEEAWALADKV 200
|
90 100
....*....|....*....|
gi 556426975 482 WLIEEGKLSEWHDAEAVFER 501
Cdd:cd03299 201 AIMLNGKLIQVGKPEEVFKK 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
296-491 |
3.56e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 48.26 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLPP-LFNIEmARLKSGDRVAIVGRNGCGKSSLM----RLIwqqfadeSAESGlKIH------PRVSP 364
Cdd:cd03244 3 IEFKNVSLRYRPNLPPvLKNIS-FSIKPGEKVGIVGRTGSGKSSLLlalfRLV-------ELSSG-SILidgvdiSKIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 365 GYYDQTLNQLPDDATLLDA-----LEPF--APDPQNRKmALISAGFpwsrhGQKISTLSGGERSRL------LFVG---- 427
Cdd:cd03244 74 HDLRSRISIIPQDPVLFSGtirsnLDPFgeYSDEELWQ-ALERVGL-----KEFVESLPGGLDTVVeeggenLSVGqrql 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 428 LTLAR-----YSLLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHDRQLISQsCNRFWLIEEGKLSE 491
Cdd:cd03244 148 LCLARallrkSKILVLDEATASVDPETDALIQKTIREAFKDctVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
320-489 |
3.59e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 48.48 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLI------------------WQQ-----------FA-------DESAESGLKIHP--- 360
Cdd:cd03267 44 IEKGEIVGFIGPNGAGKTTTLKILsgllqptsgevrvaglvpWKRrkkflrrigvvFGqktqlwwDLPVIDSFYLLAaiy 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 361 RVSPGYYDQTLNQLPDdatLLDaLEPFApDPQNRKmalisagfpwsrhgqkistLSGGERSRLLFVGLTLARYSLLMLDE 440
Cdd:cd03267 124 DLPPARFKKRLDELSE---LLD-LEELL-DTPVRQ-------------------LSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556426975 441 PTNHLDMEGKEALAQTLQQF----EGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
319-489 |
4.33e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 48.13 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHPRVS-PGYYDQTLNQLPDDATLLDALEPFapdpQNRKMA 397
Cdd:cd03265 22 RVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRePREVRRRIGIVFQDLSVDDELTGW----ENLYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 398 LISAGFPWSRHGQKI-----------------STLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQ- 459
Cdd:cd03265 98 ARLYGVPGAERRERIdelldfvglleaadrlvKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKl 177
|
170 180 190
....*....|....*....|....*....|...
gi 556426975 460 ---FEGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03265 178 keeFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-181 |
4.63e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 1 MSTLLTAQSLRVDTAfGTLFDSLSFTLKKGDRIGLLGDNGCGKS----TLLKVLDGTDSPAAGTVALAGHCL-------- 68
Cdd:PRK10418 1 MPQQIELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVapcalrgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 69 -MARVEQHLPDAIFPL-TMLD-AVLAQLPLAERDSLRWKAETLLA-GMGFTPQDMALQSATLSGGQHTRLLLARALIHDP 144
Cdd:PRK10418 80 kIATIMQNPRSAFNPLhTMHThARETCLALGKPADDATLTAALEAvGLENAARVLKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556426975 145 DLLLLDEPSNHLDLPTML----WLEHFLQNWSGSFVLVSHD 181
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQArildLLESIVQKRALGMLLVTHD 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
296-470 |
4.90e-06 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. 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: 213260 [Multi-domain] Cd Length: 220 Bit Score: 47.85 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSV---PPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkIHP---RVSpgYYDQ 369
Cdd:cd03293 1 LEVRNVSKtygGGGGAVTALEDISL-SVEEGEFVALVGPSGCGKSTLLRII----------AGL-ERPtsgEVL--VDGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 370 TLNQLPDDATLL---DALEPFAPDPQNRKMALISAGFPWSRHGQKI-----------------STLSGGERSRllfVGL- 428
Cdd:cd03293 67 PVTGPGPDRGYVfqqDALLPWLTVLDNVALGLELQGVPKAEARERAeellelvglsgfenaypHQLSGGMRQR---VALa 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556426975 429 -TLA-RYSLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHD 470
Cdd:cd03293 144 rALAvDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-157 |
5.69e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.87 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLR-VDTAFGTLFDSLSFTL--KKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVaLAGHCLMARVEqhlPD------- 78
Cdd:PRK11000 5 TLRnVTKAYGDVVISKDINLdiHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVP---PAergvgmv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 79 ----AIFP-LTMLDAV-----LAQLPLAERDS-LRWKAETL-LAGMgftpqdMALQSATLSGGQHTRLLLARALIHDPDL 146
Cdd:PRK11000 81 fqsyALYPhLSVAENMsfglkLAGAKKEEINQrVNQVAEVLqLAHL------LDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170
....*....|.
gi 556426975 147 LLLDEPSNHLD 157
Cdd:PRK11000 155 FLLDEPLSNLD 165
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-499 |
6.03e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.12 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 405 WSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF--EGGVLLVSHDRQLISQSCNRFW 482
Cdd:PRK14246 144 YDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVA 223
|
90
....*....|....*..
gi 556426975 483 LIEEGKLSEWHDAEAVF 499
Cdd:PRK14246 224 FLYNGELVEWGSSNEIF 240
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
410-477 |
6.41e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 410 QKISTLSGGERSRLLF-VGLTLARY-----SLLMLDEPTNHLDMEGKEALAQ----TLQQFEG--GVLLVSHDRQLISQS 477
Cdd:PRK01156 797 EGIDSLSGGEKTAVAFaLRVAVAQFlnndkSLLIMDEPTAFLDEDRRTNLKDiieySLKDSSDipQVIMISHHRELLSVA 876
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
323-489 |
6.54e-06 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; 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: 213228 [Multi-domain] Cd Length: 235 Bit Score: 47.50 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 323 GDRVAIVGRNGCGKSSLMRLIWQQFADESAE---SGLKIHpRVSPGYYDQTLNQ---LPDDATLLDAL-----------E 385
Cdd:cd03261 26 GEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvliDGEDIS-GLSEAELYRLRRRmgmLFQSGALFDSLtvfenvafplrE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 386 PFA-PDPQNRK---MALISAGFPWSRHgQKISTLSGGERSRllfVGLtlARY-----SLLMLDEPTNHLD---MEGKEAL 453
Cdd:cd03261 105 HTRlSEEEIREivlEKLEAVGLRGAED-LYPAELSGGMKKR---VAL--ARAlaldpELLLYDEPTAGLDpiaSGVIDDL 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 556426975 454 AQTLQQFEG-GVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03261 179 IRSLKKELGlTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
288-501 |
6.97e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 288 DALRADRLLEMENLSVP---PAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKS----SLMRLIWQQFADESAESG-LKIH 359
Cdd:PRK10261 5 DELDARDVLAVENLNIAfmqEQQKIAAVRNLSF-SLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMlLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 360 PRVSPGYYDQTLNQL-----PDDATL----LDALEP-FAPDPQ-----------NRKMALISAG-------FPWSRH--G 409
Cdd:PRK10261 84 SRQVIELSEQSAAQMrhvrgADMAMIfqepMTSLNPvFTVGEQiaesirlhqgaSREEAMVEAKrmldqvrIPEAQTilS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 410 QKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIE 485
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvlqKEMSMGVIFITHDMGVVAEIADRVLVMY 243
|
250
....*....|....*.
gi 556426975 486 EGKLSEWHDAEAVFER 501
Cdd:PRK10261 244 QGEAVETGSVEQIFHA 259
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
314-485 |
8.13e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 314 NIEMARLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLkihPRVSPGYydqtlnqlpddatlldalEPfapdpqn 393
Cdd:cd03222 16 LVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW---DGITPVY------------------KP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 394 rkmalisagfpwsrhgQKIStLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF----EGGVLLVSH 469
Cdd:cd03222 68 ----------------QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEH 130
|
170
....*....|....*.
gi 556426975 470 DRQLISQSCNRFWLIE 485
Cdd:cd03222 131 DLAVLDYLSDRIHVFE 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
319-469 |
8.40e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLI------------WQ---------QFADESA----ESGLKihPRVSP----GYYdQ 369
Cdd:PRK13538 23 TLNAGELVQIEGPNGAGKTSLLRILaglarpdagevlWQgepirrqrdEYHQDLLylghQPGIK--TELTAlenlRFY-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 370 TLNQLPDDATLLDALEpfapdpqnrKMALisAGF---PwsrhgqkISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLD 446
Cdd:PRK13538 100 RLHGPGDDEALWEALA---------QVGL--AGFedvP-------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|....*.
gi 556426975 447 MEGKEALAQTLQQF--EGG-VLLVSH 469
Cdd:PRK13538 162 KQGVARLEALLAQHaeQGGmVILTTH 187
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
319-502 |
8.82e-06 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 48.18 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLI-----------------WQqfaDESAESGLKIHPRvSPGYYDQtlnqlpdDATLL 381
Cdd:TIGR02142 19 TLPGQGVTAIFGRSGSGKTTLIRLIagltrpdegeivlngrtLF---DSRKGIFLPPEKR-RIGYVFQ-------EARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 382 --------------DALEPFAPDPQNRKMALISAGFPWSRhgqKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDM 447
Cdd:TIGR02142 88 phlsvrgnlrygmkRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 448 EGKEALAQTLQ----QFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFERL 502
Cdd:TIGR02142 165 PRKYEILPYLErlhaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
327-474 |
9.42e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 327 AIVGRNGCGKSSLMRLIwqQFADESAESGLKIHPRVSPGYYdqtlnqlpddatlldalepfapdpqnrkMALISAGFPWS 406
Cdd:cd03227 25 IITGPNGSGKSTILDAI--GLALGGAQSATRRRSGVKAGCI----------------------------VAAVSAELIFT 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 407 RHGqkistLSGGERSR----LLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGG---VLLVSHDRQLI 474
Cdd:cd03227 75 RLQ-----LSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITHLPELA 144
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
415-496 |
9.52e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.18 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 415 LSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEG---GVLLVSHDRQLISQSCNRFWLIEEGKLSE 491
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
....*
gi 556426975 492 WHDAE 496
Cdd:PRK10908 218 GVGGE 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-151 |
1.07e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMA--RVE-QHLPDAIFP-LTMLDAVLAQLPLAER 98
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAeqPEDyRKLFSAVFTdFHLFDQLLGPEGKPAN 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 99 DSL--RWkAETLLAGMGFTPQDMALQSATLSGGQHTRLLLARALIHDPDLLLLDE 151
Cdd:PRK10522 422 PALveKW-LERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
312-565 |
1.08e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 312 LFNIEMArLKSGDRVAIVGRNGCGKSSL----MRLI------------WQQFADESAESGLKIHPR------------VS 363
Cdd:cd03289 20 LENISFS-ISPGQRVGLLGRTGSGKSTLlsafLRLLntegdiqidgvsWNSVPLQKWRKAFGVIPQkvfifsgtfrknLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 364 P--GYYDQTLNQLPDDATLLDALEPFapdPQNRKMALISAGFpwsrhgqkisTLSGGERSRLLFVGLTLARYSLLMLDEP 441
Cdd:cd03289 99 PygKWSDEEIWKVAEEVGLKSVIEQF---PGQLDFVLVDGGC----------VLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 442 TNHLDMEGKEALAQTLQQ-FEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVferLRESAGLatstapvidTAA 520
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL---LNEKSHF---------KQA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 556426975 521 VQPSpyddllERLVALETLLEDDLARKPKHQKPHLQAQWRKEIEE 565
Cdd:cd03289 234 ISPS------DRLKLFPRRNSSKSKRKPRPQIQALQEETEEEVQD 272
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-157 |
1.19e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQH-LPDAI------- 80
Cdd:PRK10762 257 RLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIvyisedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 81 --------------FPLTMLDAvLAQLPLaerdSLRWKAETLLAG---MGF---TPqDMALQSATLSGGQHTRLLLARAL 140
Cdd:PRK10762 337 krdglvlgmsvkenMSLTALRY-FSRAGG----SLKHADEQQAVSdfiRLFnikTP-SMEQAIGLLSGGNQQKVAIARGL 410
|
170
....*....|....*..
gi 556426975 141 IHDPDLLLLDEPSNHLD 157
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD 427
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
300-469 |
1.31e-05 |
|
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: 46.76 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 300 NLSVPPAPGLPPL--FNIEmarLKSGDRVAIVGRNGCGKSSLMRLIwQQFADESAES----GLKIHPRVSPGYYDQT--L 371
Cdd:cd03249 7 SFRYPSRPDVPILkgLSLT---IPPGKTVALVGSSGCGKSTVVSLL-ERFYDPTSGEilldGVDIRDLNLRWLRSQIglV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 372 NQLPD--DATLLDALEPFAPDPQNR------KMALIS---AGFPWSRH---GQKISTLSGGERSRllfvgLTLARY---- 433
Cdd:cd03249 83 SQEPVlfDGTIAENIRYGKPDATDEeveeaaKKANIHdfiMSLPDGYDtlvGERGSQLSGGQKQR-----IAIARAllrn 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 556426975 434 -SLLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSH 469
Cdd:cd03249 158 pKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
295-499 |
1.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.90 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSVPPAPGLPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkIHPR----VSPGYYDQT 370
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLV-IKKGEYIGIIGKNGSGKSTLALHL----------NGL-LRPQkgkvLVSGIDTGD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 LNQLPDDATLLDAL--------------EPFAPDPQN--------RK---MALISAGFPWSRHgQKISTLSGGERSRLLF 425
Cdd:PRK13644 69 FSKLQGIRKLVGIVfqnpetqfvgrtveEDLAFGPENlclppieiRKrvdRALAEIGLEKYRH-RSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 426 VGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF-EGG--VLLVSHDRQLIsQSCNRFWLIEEGKLSEWHDAEAVF 499
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGktIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-157 |
1.68e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.34 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPD-------------AIFP-LTMLDAV 89
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkkiamvfqsfALMPhMTVLDNT 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556426975 90 -----LAQLPLAERdslRWKAETLLAGMGFTPQDMALQSAtLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK10070 128 afgmeLAGINAEER---REKALDALRQVGLENYAHSYPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
415-509 |
1.70e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.96 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 415 LSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKE---ALAQTLQ-QFEGGVLLVSHDRQLISQSCNRFWLIEEGKLS 490
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDeilNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
90 100
....*....|....*....|..
gi 556426975 491 EWHDAEAVF---ERLrESAGLA 509
Cdd:PRK13637 225 LQGTPREVFkevETL-ESIGLA 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
322-474 |
1.73e-05 |
|
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: 45.06 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 322 SGDRVAIVGRNGCGKSSLMRLIwqqfADESAESGLKIhprvspgyydqtlnqlpddatLLDALEPFAPDPQNRKMALISA 401
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL----ARELGPPGGGV---------------------IYIDGEDILEEVLDQLLLIIVG 55
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556426975 402 GFPWSrhgqkistLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGGVLLVSHDRQLI 474
Cdd:smart00382 56 GKKAS--------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
320-504 |
1.82e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.65 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHPRVSPGYYDQ-----TLNQLPDD----ATLLD----ALEP 386
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIrhkigMVFQNPDNqfvgATVEDdvafGLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 387 FAPDPQNRK----MALISAGFPWSRHgQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL----Q 458
Cdd:PRK13650 110 KGIPHEEMKervnEALELVGMQDFKE-REPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIkgirD 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556426975 459 QFEGGVLLVSHDRQLISQScNRFWLIEEGKLSEWHDAEAVFERLRE 504
Cdd:PRK13650 189 DYQMTVISITHDLDEVALS-DRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
309-487 |
1.95e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 46.27 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 309 LPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMRLIWQQF-ADE------SAESGLKIHpRVSP-----------GYYDQT 370
Cdd:COG4778 24 LPVLDGVSFS-VAAGECVALTGPSGAGKSTLLKCIYGNYlPDSgsilvrHDGGWVDLA-QASPreilalrrrtiGYVSQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 LNQLPDDATLLDALEPFAPDPQNRKMALISAG---------------FPwsrhgqkiSTLSGGERSRLlfvglTLAR--- 432
Cdd:COG4778 102 LRVIPRVSALDVVAEPLLERGVDREEARARARellarlnlperlwdlPP--------ATFSGGEQQRV-----NIARgfi 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 433 --YSLLMLDEPTNHLDMEGKEALAQTLQQF-EGGVLLVS--HDRQLISQSCNRFWLIEEG 487
Cdd:COG4778 169 adPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGifHDEEVREAVADRVVDVTPF 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
320-474 |
1.98e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIhpRVSpgYYDQTLnqLPD-DATLLDALEPFAPDpqnrkmal 398
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL--KIS--YKPQYI--KPDyDGTVEDLLRSITDD-------- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 399 ISAGFPWSR----------HGQKISTLSGGERSRLLfVGLTLARYS-LLMLDEPTNHLDMEGKEALAQTLQQF----EGG 463
Cdd:PRK13409 428 LGSSYYKSEiikplqlerlLDKNVKDLSGGELQRVA-IAACLSRDAdLYLLDEPSAHLDVEQRLAVAKAIRRIaeerEAT 506
|
170
....*....|.
gi 556426975 464 VLLVSHDRQLI 474
Cdd:PRK13409 507 ALVVDHDIYMI 517
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-492 |
1.99e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLM----RLI------------WQQFADESAESGLKIHPR---VSPG-----------YYDQ 369
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLsallRLLstegeiqidgvsWNSVTLQTWRKAFGVIPQkvfIFSGtfrknldpyeqWSDE 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 370 TLNQLPDDATLLDALEPFaPDPQNrkMALISAGFpwsrhgqkisTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEG 449
Cdd:TIGR01271 1322 EIWKVAEEVGLKSVIEQF-PDKLD--FVLVDGGY----------VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556426975 450 KEALAQTLQQ-FEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEW 492
Cdd:TIGR01271 1389 LQIIRKTLKQsFSNCTVILSEHRVEALLECQQFLVIEGSSVKQY 1432
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-157 |
2.02e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.57 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDG--TDSPAAGTVALAGHCLMARVEQHL-----PDAIFP-LTMLDAV 89
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQILKRTgfvtqDDILYPhLTVRETL 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 90 ----LAQLP--LAERDSLRwKAETLLAGMGFTPQDMALQSAT----LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PLN03211 162 vfcsLLRLPksLTKQEKIL-VAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
126-198 |
2.38e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.78 E-value: 2.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 126 LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD--LPTMLWLE---HFLQNWSGSFVLVSHDRQLLdavTNGSWILRDK 198
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihLSDHLMQEgilKFLQDDKRTLVLVTHKLQYL---PHADWIIAMK 215
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-157 |
2.63e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGtDSPAA-------------------------GTVALAGHcLMARVEQH 75
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfgrrrgsgetiwdikkhiGYVSSSLH-LDYRVSTS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 76 LPDAIFPlTMLDAV-LAQlplAERDSLRWKAETLLAGMGFTPQ--DMALQSatLSGGQHTRLLLARALIHDPDLLLLDEP 152
Cdd:PRK10938 355 VRNVILS-GFFDSIgIYQ---AVSDRQQKLAQQWLDILGIDKRtaDAPFHS--LSWGQQRLALIVRALVKHPTLLILDEP 428
|
....*
gi 556426975 153 SNHLD 157
Cdd:PRK10938 429 LQGLD 433
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
377-487 |
2.81e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.07 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 377 DATLLDALEPFAPDPQ-NRKM-ALISAGFPWSRHGQKISTLSGGERSRllfVGLT--LARYS----LLMLDEPTNHLDME 448
Cdd:cd03271 130 DMTVEEALEFFENIPKiARKLqTLCDVGLGYIKLGQPATTLSGGEAQR---IKLAkeLSKRStgktLYILDEPTTGLHFH 206
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 556426975 449 GKEALAQTLQQF-EGG--VLLVSHDRQLISQSCnrfWLIEEG 487
Cdd:cd03271 207 DVKKLLEVLQRLvDKGntVVVIEHNLDVIKCAD---WIIDLG 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
319-469 |
2.83e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 47.08 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaesglkihprvsPGYYD---------------QTLNQL-------PD 376
Cdd:COG1132 362 TIPPGETVALVGPSGSGKSTLVNLL--------------------LRFYDptsgrilidgvdirdLTLESLrrqigvvPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 377 DATLLDA--LE------PFAPDPQNR---KMALIS---AGFPW---SRHGQKISTLSGGERSRllfvgLTLARY-----S 434
Cdd:COG1132 422 DTFLFSGtiREnirygrPDATDEEVEeaaKAAQAHefiEALPDgydTVVGERGVNLSGGQRQR-----IAIARAllkdpP 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 556426975 435 LLMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSH 469
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-157 |
3.01e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.02 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 33 IGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHlpdaifPLTMLDAVLAQLPLAeRD-- 99
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslshsvlrqgVAMVQQD------PVVLADTFLANVTLG-RDis 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 100 -SLRWKA-ETL-LAGMGFTPQD-----MALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK10790 443 eEQVWQAlETVqLAELARSLPDglytpLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
295-489 |
3.59e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMR-------------LIWQQFADESAESGLKIHPR 361
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINF-KAEKGEMVALLGPNGAGKSTLFLhfngilkptsgevLIKGEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 362 VSPGYydqtlnQLPDDATLLDALE---PFAP--------DPQNR-KMALISAGFpwSRHGQKIST-LSGGERSRLLFVGL 428
Cdd:PRK13639 80 VGIVF------QNPDDQLFAPTVEedvAFGPlnlglskeEVEKRvKEALKAVGM--EGFENKPPHhLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556426975 429 TLARYSLLMLDEPTNHLDMEGKEALAQTLQQF--EGGVLLVS-HDRQLISQSCNRFWLIEEGKL 489
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
404-489 |
3.90e-05 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 45.15 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 404 PWSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF--EGGVLLVSHDRQLISQScNRF 481
Cdd:cd03248 140 YDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVERA-DQI 218
|
....*...
gi 556426975 482 WLIEEGKL 489
Cdd:cd03248 219 LVLDGGRI 226
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
412-485 |
4.22e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 412 ISTLSGGERSRL-LFVGLTLARY-----SLLMLDEPTNHLDMEGKE-ALAQTLQQFEGG----VLLVSHDRQLIsQSCNR 480
Cdd:cd03240 113 RGRCSGGEKVLAsLIIRLALAETfgsncGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELV-DAADH 191
|
....*
gi 556426975 481 FWLIE 485
Cdd:cd03240 192 IYRVE 196
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-160 |
4.35e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.48 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 9 SLRVDTAFGTLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGhCLMARVEQHlpDAIFPLTmlda 88
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-LNIAKIGLH--DLRFKIT---- 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 VLAQLPLAERDSLR--------------WKAETLLAGMGFT---PQDMALQSA----TLSGGQHTRLLLARALIHDPDLL 147
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRmnldpfsqysdeevWWALELAHLKTFVsalPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKIL 1443
|
170
....*....|...
gi 556426975 148 LLDEPSNHLDLPT 160
Cdd:TIGR00957 1444 VLDEATAAVDLET 1456
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-61 |
4.36e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 4.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTV 61
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-188 |
4.45e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.46 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTV-----ALAGHCLMARVEQHLPDAIFPLTMLDAV------ 89
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkDEKNKKKTKEKEKVLEKLVIQKTRFKKIkkikei 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 90 ---------LAQLPLAErdslrwkaETLLAGMGFTPQDM------ALQSAT-------------------LSGGQHTRLL 135
Cdd:PRK13651 104 rrrvgvvfqFAEYQLFE--------QTIEKDIIFGPVSMgvskeeAKKRAAkyielvgldesylqrspfeLSGGQKRRVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 136 LARALIHDPDLLLLDEPSNHLD---LPTMLWLEHFLQNWSGSFVLVSHDrqlLDAV 188
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNV 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
320-501 |
4.92e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 45.39 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQFADESA-----------ESGLKIHPRVSPGYydqtlnQLPDD----ATLLD-- 382
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtitvggmvlseETVWDVRRQVGMVF------QNPDNqfvgATVQDdv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 383 --ALEpfapdpqNRKM-----------ALISAGFPWSRHgQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEG 449
Cdd:PRK13635 104 afGLE-------NIGVpreemvervdqALRQVGMEDFLN-REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 450 KEALAQTLQQF--EGG--VLLVSHDRQLISQScNRFWLIEEGKLSEWHDAEAVFER 501
Cdd:PRK13635 176 RREVLETVRQLkeQKGitVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEEIFKS 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
308-447 |
5.01e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 308 GLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWQQFadESAESGLKIHPRVS---------PGY----------YD 368
Cdd:TIGR01271 438 VTPVLKNISF-KLEKGQLLAVAGSTGSGKSSLLMMIMGEL--EPSEGKIKHSGRISfspqtswimPGTikdniifglsYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 369 Q-------TLNQLPDDATLLdalepfapdPQNRKMALISAGFpwsrhgqkisTLSGGERSRllfVGLTLARYS---LLML 438
Cdd:TIGR01271 515 EyrytsviKACQLEEDIALF---------PEKDKTVLGEGGI----------TLSGGQRAR---ISLARAVYKdadLYLL 572
|
....*....
gi 556426975 439 DEPTNHLDM 447
Cdd:TIGR01271 573 DSPFTHLDV 581
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
319-480 |
5.19e-05 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 44.41 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAESGLKIHP--RVSPGYYDQTL--NQLPDDATLLDALEP---FAPDP 391
Cdd:cd03231 22 TLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldFQRDSIARGLLylGHAPGIKTTLSVLENlrfWHADH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 392 QNRKM--ALISAGFPWSRHgQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQFEGG---VLL 466
Cdd:cd03231 102 SDEQVeeALARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARggmVVL 180
|
170
....*....|....
gi 556426975 467 VSHDRQLISQSCNR 480
Cdd:cd03231 181 TTHQDLGLSEAGAR 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
297-469 |
5.34e-05 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. 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: 213221 [Multi-domain] Cd Length: 229 Bit Score: 44.91 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 297 EMENLSVPPAPGLPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMRLI-----WQQ---FADESAESGLKIHP-RVSPGYY 367
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFS-IKPGETVAIVGPTGAGKTTLINLLmrfydPQKgqiLIDGIDIRDISRKSlRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 368 DQTLNQLPDdaTLLDALEPFAPDPQNRKMALIS--AGF-PWSRH---------GQKISTLSGGERSRLLFVGLTLARYSL 435
Cdd:cd03254 83 LQDTFLFSG--TIMENIRLGRPNATDEEVIEAAkeAGAhDFIMKlpngydtvlGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 556426975 436 LMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSH 469
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
321-470 |
5.81e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.05 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 321 KSGDRVAIVGRNGCGKSSLMRLI----------------WQQFADESAESGL----------KIHPRVSPGYYDQTLNQL 374
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdWDEILDEFRGSELqnyftkllegDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 375 pdDATLLDALEpfAPDPQNRKMALISAGFPWSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALA 454
Cdd:cd03236 104 --KGKVGELLK--KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170
....*....|....*....
gi 556426975 455 QTLQQF---EGGVLLVSHD 470
Cdd:cd03236 180 RLIRELaedDNYVLVVEHD 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
321-491 |
5.85e-05 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR 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: 213218 [Multi-domain] Cd Length: 234 Bit Score: 44.91 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 321 KSGDRVAIVGRNGCGKSSLMRLIwQQFADESAES----GLKIHprvspgyyDQTLNQL-------PDDATLLDAL----- 384
Cdd:cd03251 26 PAGETVALVGPSGSGKSTLVNLI-PRFYDVDSGRilidGHDVR--------DYTLASLrrqiglvSQDVFLFNDTvaeni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 385 ---EPFAPDPQNRKMALISA------GFPWSRH---GQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEA 452
Cdd:cd03251 97 aygRPGATREEVEEAARAANahefimELPEGYDtviGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556426975 453 LAQTLQQFEGG--VLLVSHDRQLISQScNRFWLIEEGKLSE 491
Cdd:cd03251 177 VQAALERLMKNrtTFVIAHRLSTIENA-DRIVVLEDGKIVE 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
320-491 |
5.98e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.77 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLM--------------RLIWQQFA--DESAESGLKIHprvSPGYYDQTLNQLPDDATL--- 380
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLailaglddgssgevSLVGQPLHqmDEEARAKLRAK---HVGFVFQSFMLIPTLNALenv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 381 -LDALEPFAPDPQNRKMA---LISAGFpwsrhGQKI----STLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEA 452
Cdd:PRK10584 110 eLPALLRGESSRQSRNGAkalLEQLGL-----GKRLdhlpAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556426975 453 LAQTL----QQFEGGVLLVSHDRQLISQsCNRFWLIEEGKLSE 491
Cdd:PRK10584 185 IADLLfslnREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-157 |
7.90e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.39 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQ--HLPDaifpltmlD 87
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlaslrnqVALVSQnvHLFN--------D 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 88 AVLAQLPLAERDSLRW----KAETLLAGMGFTPQ-DMALQS------ATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL 156
Cdd:PRK11176 432 TIANNIAYARTEQYSReqieEAARMAYAMDFINKmDNGLDTvigengVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
.
gi 556426975 157 D 157
Cdd:PRK11176 512 D 512
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
416-499 |
9.05e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 416 SGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEgKEALAQTL-----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLS 490
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVT-VQAQIMTLlnelkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
....*....
gi 556426975 491 EWHDAEAVF 499
Cdd:PRK09473 242 EYGNARDVF 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-491 |
9.41e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.29 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIwqqFADESAESGlkihpRVSpgYYDQTLNQLPD--------DATLLDALEPFAPDP 391
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLL---VGLESPSQG-----NVS--WRGEPLAKLNRaqrkafrrDIQMVFQDSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 392 QNRKMALISAGFpwsRHgqkISTLSGGERSR-----LLFVGLT--------------------LARY-----SLLMLDEP 441
Cdd:PRK10419 105 RKTVREIIREPL---RH---LLSLDKAERLArasemLRAVDLDdsvldkrppqlsggqlqrvcLARAlavepKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556426975 442 TNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSE 491
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
323-489 |
1.01e-04 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 43.96 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 323 GDRVAIVGRNGCGKSSLMRLIWQQFA--------DESAESGLKIHPRVSPG----YydQTLNQLPDdATLLDALEPFAPD 390
Cdd:cd03219 26 GEIHGLIGPNGAGKTTLFNLISGFLRptsgsvlfDGEDITGLPPHEIARLGigrtF--QIPRLFPE-LTVLENVMVAAQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 391 PQNRKMALISAGFPWSRHGQKI-----------------STLSGGERsRLLFVGLTLA-RYSLLMLDEPTNHLDMEGKEA 452
Cdd:cd03219 103 RTGSGLLLARARREEREARERAeellervgladladrpaGELSYGQQ-RRLEIARALAtDPKLLLLDEPAAGLNPEETEE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556426975 453 LAQTLQQF-EGG--VLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:cd03219 182 LAELIRELrERGitVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-195 |
1.17e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.09 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL-----------MARVEQHlpdaifPLTMLDAVLA 91
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswrsrLAVVSQT------PFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 92 QLPLAERDSLRWKAETL--LAGMG----FTPQ----DMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTM 161
Cdd:PRK10789 408 NIALGRPDATQQEIEHVarLASVHddilRLPQgydtEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190
....*....|....*....|....*....|....*
gi 556426975 162 LWLEHFLQNWS-GSFVLVSHDRqlLDAVTNGSWIL 195
Cdd:PRK10789 488 HQILHNLRQWGeGRTVIISAHR--LSALTEASEIL 520
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
296-502 |
1.31e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.96 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSVPPAPGLP----PLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLKIHPRVSPGYYDQTL 371
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegrALFDVNL-TIEDGSYTAFIGHTGSGKSTIMQLL----------NGLHVPTQGSVRVDDTLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 372 N-------------------QLPDdATLLD--ALEPFAPDPQN-------------RKMALIsaGFPWSRHGQKISTLSG 417
Cdd:PRK13649 72 TstsknkdikqirkkvglvfQFPE-SQLFEetVLKDVAFGPQNfgvsqeeaealarEKLALV--GISESLFEKNPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 418 GERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF-EGG--VLLVSHDRQLISQSCNRFWLIEEGKLSEWHD 494
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGmtIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
....*...
gi 556426975 495 AEAVFERL 502
Cdd:PRK13649 229 PKDIFQDV 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
377-487 |
1.38e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 377 DATLLDALEPFAPDPQ-NRKM-ALISAGFPWSRHGQKISTLSGGERSRllfvgLTLARY--------SLLMLDEPTNHLD 446
Cdd:TIGR00630 790 DMTVEEAYEFFEAVPSiSRKLqTLCDVGLGYIRLGQPATTLSGGEAQR-----IKLAKElskrstgrTLYILDEPTTGLH 864
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 556426975 447 MEGKEALAQTLQQF-EGG--VLLVSHDRQLISQSCnrfWLIEEG 487
Cdd:TIGR00630 865 FDDIKKLLEVLQRLvDKGntVVVIEHNLDVIKTAD---YIIDLG 905
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
371-475 |
1.39e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 LNQL-PDDATLLDALEPFapdpQNRKMALISAGFPWSRHGQKISTLSGGERSRLLFVGLTLARYSLLM--LDEPTNHLDM 447
Cdd:PRK00635 436 LSQLpSKSLSIEEVLQGL----KSRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHP 511
|
90 100 110
....*....|....*....|....*....|.
gi 556426975 448 EGKEALAQTLQQFE---GGVLLVSHDRQLIS 475
Cdd:PRK00635 512 QDTHKLINVIKKLRdqgNTVLLVEHDEQMIS 542
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
327-488 |
1.40e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 44.32 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 327 AIVGRNGCGKSSLMRLI-----------------WQqfaDESAESGLKIHPRvSPGYYDQtlnqlpdDATLLDAL----- 384
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIaglerpdsgrirlggevLQ---DSARGIFLPPHRR-RIGYVFQ-------EARLFPHLsvrgn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 385 ----EPFAPdPQNRKMAL--------ISagfpwsrH--GQKISTLSGGERSRllfVGLT---LARYSLLMLDEPTNHLDM 447
Cdd:COG4148 98 llygRKRAP-RAERRISFdevvellgIG-------HllDRRPATLSGGERQR---VAIGralLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556426975 448 EGKEA----LAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:COG4148 167 ARKAEilpyLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGR 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-182 |
1.67e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.69 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVL------DG---TDSPAAGTVALAGHCLMARVeqhLPDAIF----PLT 84
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntEGdiqIDGVSWNSVPLQKWRKAFGV---IPQKVFifsgTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 85 M-LDAVLAQ-----LPLAERDSLRWKAETLLAGMGFTPQDmalQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDL 158
Cdd:cd03289 95 KnLDPYGKWsdeeiWKVAEEVGLKSVIEQFPGQLDFVLVD---GGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180
....*....|....*....|....*
gi 556426975 159 PTMLWLEHFL-QNWSGSFVLVSHDR 182
Cdd:cd03289 172 ITYQVIRKTLkQAFADCTVILSEHR 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-157 |
1.72e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 1.72e-04
10 20 30
....*....|....*....|....*....|...
gi 556426975 125 TLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-186 |
1.73e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.01 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCL---MARVEQHL-----PDAIFPLTMLdavl 90
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdLCTYQKQLcfvghRSGINPYLTL---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 91 aqlplaeRDSLRWKAETLLAGMGFTP--------QDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLDLPTML 162
Cdd:PRK13540 92 -------RENCLYDIHFSPGAVGITElcrlfsleHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|....*....
gi 556426975 163 WL-----EHFLQnwSGSFVLVSHDRQLLD 186
Cdd:PRK13540 165 TIitkiqEHRAK--GGAVLLTSHQDLPLN 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
312-493 |
2.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 43.23 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 312 LFNIEMArLKSGDRVAIVGRNGCGKSSLMrliwQQF------ADESAE-SGLKIHPRVSPGYYDQT------LNQLPDDA 378
Cdd:PRK13646 23 IHDVNTE-FEQGKYYAIVGQTGSGKSTLI----QNInallkpTTGTVTvDDITITHKTKDKYIRPVrkrigmVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 379 TLLDALEP---FApdPQNRKM-----------ALISAGFPWSRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNH 444
Cdd:PRK13646 98 LFEDTVEReiiFG--PKNFKMnldevknyahrLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 445 LDMEGKEALAQTLQQFE----GGVLLVSHDR----------------QLISQSCNRFWLIEEGKLSEWH 493
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQtdenKTIILVSHDMnevaryadevivmkegSIVSQTSPKELFKDKKKLADWH 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
293-488 |
3.23e-04 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 42.28 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 293 DRLLEMENLSVppA-PGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGLkihPRVSPG--YYD- 368
Cdd:COG0410 1 MPMLEVENLHA--GyGGIHVLHGVSL-EVEEGEIVALLGRNGAGKTTLLKAI----------SGL---LPPRSGsiRFDg 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 369 QTLNQLPDDA-------------------TLLDALE---PFAPDPQNRKMAL--ISAGFPW--SRHGQKISTLSGGERsR 422
Cdd:COG0410 65 EDITGLPPHRiarlgigyvpegrrifpslTVEENLLlgaYARRDRAEVRADLerVYELFPRlkERRRQRAGTLSGGEQ-Q 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426975 423 LLFVGLTL-ARYSLLMLDEPTnhldmegkEALA--------QTLQQF--EG-GVLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:COG0410 144 MLAIGRALmSRPKLLLLDEPS--------LGLApliveeifEIIRRLnrEGvTILLVEQNARFALEIADRAYVLERGR 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
414-488 |
3.32e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 42.67 E-value: 3.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 414 TLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGK 488
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-473 |
3.41e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 412 ISTLSGGERSRL-LFVGLTLARY-----SLLMLDEPTNHLDMEGKEALAQTLQQFE---GGVLLVSHDRQL 473
Cdd:PRK03918 786 LTFLSGGERIALgLAFRLALSLYlagniPLLILDEPTPFLDEERRRKLVDIMERYLrkiPQVIIVSHDEEL 856
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
295-502 |
3.50e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 42.80 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 295 LLEMENLSVPPAPGLP----PLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWQQFadESAESGLKIHPRVSPGYYDQ- 369
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfasrALFDIDL-EVKKGSYTALIGHTGSGKSTLLQHLNGLL--QPTEGKVTVGDIVVSSTSKQk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 370 ----------TLNQLPDDATLLDA-LEPFAPDPQN---------------RKMALISAGFpWSRHGQKistLSGGERSRL 423
Cdd:PRK13643 78 eikpvrkkvgVVFQFPESQLFEETvLKDVAFGPQNfgipkekaekiaaekLEMVGLADEF-WEKSPFE---LSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 424 LFVGLTLARYSLLMLDEPTNHLDMEGK---EALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFE 500
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
..
gi 556426975 501 RL 502
Cdd:PRK13643 234 EV 235
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-151 |
3.60e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHCLMARVEQHLPDAIFPLTMLDAVLAQLPLAERDS 100
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKI 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 556426975 101 LRWKAETL-LAGMG-FTPQDMalqsATLSGGQHTRLLLARALIHDPDLLLLDE 151
Cdd:PRK13545 121 KEIIPEIIeFADIGkFIYQPV----KTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
412-470 |
4.18e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 42.38 E-value: 4.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 412 ISTLSGGERSRLlFVGLTLA---RYslLMLDEPTNHLDMEGKEALAQTLQQF--EGG--VLLVSHD 470
Cdd:COG4604 133 LDELSGGQRQRA-FIAMVLAqdtDY--VLLDEPLNNLDMKHSVQMMKLLRRLadELGktVVIVLHD 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
296-488 |
4.39e-04 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 41.69 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 296 LEMENLSV----PPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMRLIWQQFadeSAESG-LKIHPRVSpgYYDQT 370
Cdd:cd03250 1 ISVEDASFtwdsGEQETSFTLKDINL-EVPKGELVAIVGPVGSGKSSLLSALLGEL---EKLSGsVSVPGSIA--YVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 371 ---LNqlpddATLLD---ALEPFapDPQ-----------NRKMALISAGfPWSRHGQKISTLSGGERSRllfvgLTLAR- 432
Cdd:cd03250 75 pwiQN-----GTIREnilFGKPF--DEEryekvikacalEPDLEILPDG-DLTEIGEKGINLSGGQKQR-----ISLARa 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 433 -YS---LLMLDEPTNHLDmegkealAQTLQQ-FE---GG-------VLLVSHDRQLISQsCNRFWLIEEGK 488
Cdd:cd03250 142 vYSdadIYLLDDPLSAVD-------AHVGRHiFEnciLGlllnnktRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-500 |
5.05e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 327 AIVGRNGCGKSSLMRL---IWQQFADESAESGLKI------HPRVSP-------GYYDQTLNQLP-----DDATL---LD 382
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTfnrLLELNEEARVEGEVRLfgrniySPDVDPievrrevGMVFQYPNPFPhltiyDNVAIgvkLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 383 AL-EPFAPDPQNRKMALISAGFpW----SRHGQKISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL 457
Cdd:PRK14267 114 GLvKSKKELDERVEWALKKAAL-WdevkDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556426975 458 QQF--EGGVLLVSHDRQLISQSCNRFWLIEEGKLSEWHDAEAVFE 500
Cdd:PRK14267 193 FELkkEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-157 |
5.41e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 24 SFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTValagHCLMARV-------EQHLPDAIFPLTMLDAvlaqLPLA 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER----QSQFSHItrlsfeqLQKLVSDEWQRNNTDM----LSPG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 97 ERDSLRWKAETLLagMGFTPQDMALQSAT--------------LSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK10938 95 EDDTGRTTAEIIQ--DEVKDPARCEQLAQqfgitalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
410-470 |
5.62e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426975 410 QKISTLSGGERSRLLfVGLTLAR----YsllMLDEPTNHLDMEGKEALAQTLQQFEGG--VLLVSHD 470
Cdd:PRK13409 208 RDISELSGGELQRVA-IAAALLRdadfY---FFDEPTSYLDIRQRLNVARLIRELAEGkyVLVVEHD 270
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-506 |
6.89e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 30 GDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmarveqhlpDAIF--PLTMLDA----------VLAQLPLAE 97
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK-----------EVTFngPKSSQEAgigiihqelnLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 98 -----RD------SLRWK-----AETLLAGMG--FTPQDMAlqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNHL-DL 158
Cdd:PRK10762 99 niflgREfvnrfgRIDWKkmyaeADKLLARLNlrFSSDKLV---GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 159 PT--MLWLEHFLQNWSGSFVLVSHdR-----QLLDAVTngswILRDKTLhyfalpctAARKALEAKDEsdaqrhkaeqke 231
Cdd:PRK10762 176 ETesLFRVIRELKSQGRGIVYISH-RlkeifEICDDVT----VFRDGQF--------IAEREVADLTE------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 232 iDRVtasakrlatwgkvydnedlarkakqMEKQVERLKESQTAltagsqwtltlRGDALRADRLLEMENLSvppAPGLPp 311
Cdd:PRK10762 231 -DSL-------------------------IEMMVGRKLEDQYP-----------RLDKAPGEVRLKVDNLS---GPGVN- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 312 lfNIEMArLKSGDRVAIVGRNGCGKSSLMRLIWQQFADESAE---SGLKIHPRvSPgyYDQTLNQLP--------DDATL 380
Cdd:PRK10762 270 --DVSFT-LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYvtlDGHEVVTR-SP--QDGLANGIVyisedrkrDGLVL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 381 ---------LDALEPFAP-----DPQNRKMA------LISAGFPwSRhGQKISTLSGGERSRLLFV-GLtLARYSLLMLD 439
Cdd:PRK10762 344 gmsvkenmsLTALRYFSRaggslKHADEQQAvsdfirLFNIKTP-SM-EQAIGLLSGGNQQKVAIArGL-MTRPKVLILD 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 440 EPTNHLDMEGKEALAQTLQQF--EG-GVLLVSHDRQLISQSCNRFWLIEEGKLS-EWHDAEAVFERLRESA 506
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFkaEGlSIILVSSEMPEVLGMSDRILVMHEGRISgEFTREQATQEKLMAAA 491
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
410-470 |
6.92e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.46 E-value: 6.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556426975 410 QKISTLSGGERSRLLfVGLTLARYS-LLMLDEPTNHLDMEGKEALAQTLQQF-EGG--VLLVSHD 470
Cdd:COG1245 208 RDISELSGGELQRVA-IAAALLRDAdFYFFDEPSSYLDIYQRLNVARLIRELaEEGkyVLVVEHD 271
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
326-475 |
9.29e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.09 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 326 VAIVGRNGCGKSSLMrliwqqFADESAESGLKIHPRVSPgYYDQTLNQLP-DDATLLDALEP--------FAPDPQ---- 392
Cdd:cd03270 24 VVITGVSGSGKSSLA------FDTIYAEGQRRYVESLSA-YARQFLGQMDkPDVDSIEGLSPaiaidqktTSRNPRstvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 393 -------------------NRKMALISAGFPWSRHGQKISTLSGGE--RSRL---LFVGLTLARYsllMLDEPTNHLDME 448
Cdd:cd03270 97 tvteiydylrllfarvgirERLGFLVDVGLGYLTLSRSAPTLSGGEaqRIRLatqIGSGLTGVLY---VLDEPSIGLHPR 173
|
170 180 190
....*....|....*....|....*....|
gi 556426975 449 GKEALAQTLQQFE---GGVLLVSHDRQLIS 475
Cdd:cd03270 174 DNDRLIETLKRLRdlgNTVLVVEHDEDTIR 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
412-500 |
9.46e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.17 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 412 ISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF-EGGVLLVSHDRQLISQSCNRF---WLIEEG 487
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLaQKGKTIVTSMHQPSSRVYQMFdsvLVLSEG 283
|
90
....*....|....*.
gi 556426975 488 K---LSEWHDAEAVFE 500
Cdd:PLN03211 284 RclfFGKGSDAMAYFE 299
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
323-489 |
1.08e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.93 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 323 GDRVAIVGRNGCGKSSLMRLI--------------------WQQ--FADESA--------ESGLKIHPRVSPGYY----- 367
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLgrhqppsegeilldaqplesWSSkaFARKVAylpqqlpaAEGMTVRELVAIGRYpwhga 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 368 ----DQTLNQLPDDATLLDALEPFApdpqNRKmalisagfpwsrhgqkISTLSGGERSRLlFVGLTLARYS-LLMLDEPT 442
Cdd:PRK10575 117 lgrfGAADREKVEEAISLVGLKPLA----HRL----------------VDSLSGGERQRA-WIAMLVAQDSrCLLLDEPT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556426975 443 NHLDMEGKE---ALAQTLQQFEG-GVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:PRK10575 176 SALDIAHQVdvlALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-157 |
1.25e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.37 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 23 LSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAGHclmaRVEQHLPD-----------AIFP-LTMLDAV- 89
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR----VVNELEPAdrdiamvfqnyALYPhMSVRENMa 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556426975 90 ----LAQLPLAERDSLRWKAETLLAGMGFtpqdMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PRK11650 99 yglkIRGMPKAEIEERVAEAARILELEPL----LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
406-488 |
1.31e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 40.94 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 406 SRHGQKISTLSGGERSRLlfvglTLARY-----SLLMLDEPTNHLDMEGKEALAQTLQQFEGG---VLLVSHDRQLISQS 477
Cdd:PRK13537 130 NKADAKVGELSGGMKRRL-----TLARAlvndpDVLVLDEPTTGLDPQARHLMWERLRSLLARgktILLTTHFMEEAERL 204
|
90
....*....|.
gi 556426975 478 CNRFWLIEEGK 488
Cdd:PRK13537 205 CDRLCVIEEGR 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
320-446 |
1.49e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.57 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 320 LKSGDRVAIVGRNGCGKSSLMRLIWQQfadesAESGLKIHPRVspgyydqTLNQLPDDATLLDAL-------EPFAPDPQ 392
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFR-----SPKGVKGSGSV-------LLNGMPIDAKEMRAIsayvqqdDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 393 NRKMALISAGFPWSRHGQK-----------------------------ISTLSGGERSRLLFVGLTLARYSLLMLDEPTN 443
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKkekrervdevlqalglrkcantrigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
...
gi 556426975 444 HLD 446
Cdd:TIGR00955 196 GLD 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-454 |
1.66e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 39.86 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 319 RLKSGDRVAIVGRNGCGKSSLMRLIwqqfadesaeSGL--KIHPRVSPGYYDQTLNQLPDDATLL---DALEPFAPDPQN 393
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLI----------AGLlpPAAGTIKLDGGDIDDPDVAEACHYLghrNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 394 RKMalisagfpWSR-HGQKIS--------------------TLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEA 452
Cdd:PRK13539 94 LEF--------WAAfLGGEELdiaaaleavglaplahlpfgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
..
gi 556426975 453 LA 454
Cdd:PRK13539 166 FA 167
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-489 |
1.75e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 40.84 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 313 FNIEmarlkSGDRVAIVGRNGCGKSSLMRLI------------------WQQ---FA---------------DESAESGL 356
Cdd:COG4586 43 FTIE-----PGEIVGFIGPNGAGKSTTIKMLtgilvptsgevrvlgyvpFKRrkeFArrigvvfgqrsqlwwDLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 357 KIHP---RVSPGYYDQTLNQLpddATLLDaLEPFApDPQNRKMALisagfpwsrhgqkistlsgGERSRLLFVGLTLARY 433
Cdd:COG4586 118 RLLKaiyRIPDAEYKKRLDEL---VELLD-LGELL-DTPVRQLSL-------------------GQRMRCELAAALLHRP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 434 SLLMLDEPTNHLDMEGKEALAQTLQQF--EGG--VLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYnrERGttILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-157 |
1.78e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 4 LLTAQSLRVDTAFGTLFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTV---------------ALAGHCL 68
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyykncninniakpycTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 69 MARVEqhlpdaifpLTMLDAvlaqlpLAERDSLRWKAETLLAGMG-FTPQD-MALQSATLSGGQHTRLLLARALIHDPDL 146
Cdd:PRK13541 80 GLKLE---------MTVFEN------LKFWSEIYNSAETLYAAIHyFKLHDlLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170
....*....|.
gi 556426975 147 LLLDEPSNHLD 157
Cdd:PRK13541 145 WLLDEVETNLS 155
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
415-506 |
2.01e-03 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 40.94 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 415 LSGGERSRLLFVgLTLARYSLLML-DEPTNHLDMEG----KEALAQTLQQFEGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:TIGR03269 169 LSGGEKQRVVLA-RQLAKEPFLFLaDEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEI 247
|
90
....*....|....*..
gi 556426975 490 SEWHDAEAVFERLRESA 506
Cdd:TIGR03269 248 KEEGTPDEVVAVFMEGV 264
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-157 |
2.22e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 19 LFDSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTV------------------ALAGHCLMARVEQ--HLPD 78
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaersiayvpqqawimnaTVRGNILFFDEEDaaRLAD 754
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 79 AIfPLTMLDAVLAQLPLAerdslrwkAETLLAGMGftpqdmalqsATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PTZ00243 755 AV-RVSQLEADLAQLGGG--------LETEIGEKG----------VNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
415-489 |
2.28e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 40.38 E-value: 2.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 415 LSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTL----QQFEGGVLLVSHDRQLISQSCNRFWLIEEGKL 489
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
195-270 |
2.42e-03 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 37.17 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426975 195 LRDKTLHYFALPCTAARKALEAKDESDAQRHKAEQKEIDRVTASAKRLATWGKvydnedLARKAKQMEKQVERLKE 270
Cdd:pfam12848 3 LERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKAS------KAKQAQSRIKALEKMER 72
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
415-501 |
3.26e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.79 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 415 LSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF--EGG--VLLVSHDRQLISQSCNRFWLIEEGKLS 490
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGmtVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
90
....*....|.
gi 556426975 491 EWHDAEAVFER 501
Cdd:PRK13652 218 AYGTVEEIFLQ 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
411-489 |
3.56e-03 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 39.27 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 411 KISTLSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEALAQTLQQF-EGG--VLLVSHDRQLISQSCNRFWLIEEG 487
Cdd:cd03266 133 RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLrALGkcILFSTHIMQEVERLCDRVVVLHRG 212
|
..
gi 556426975 488 KL 489
Cdd:cd03266 213 RV 214
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-185 |
3.61e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVA--------------------LAGH-----------CL- 68
Cdd:PRK15093 24 DRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTAdrmrfddidllrlsprerrkLVGHnvsmifqepqsCLd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 69 -MARVEQHLPDAIFPLTMLDAVLAQLPLAERdslrwKAETLLAGMGFTPQDMALQS--ATLSGGQHTRLLLARALIHDPD 145
Cdd:PRK15093 104 pSERVGRQLMQNIPGWTYKGRWWQRFGWRKR-----RAIELLHRVGIKDHKDAMRSfpYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556426975 146 LLLLDEPSNHLDLPTMLWLEHFL----QNWSGSFVLVSHDRQLL 185
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLtrlnQNNNTTILLISHDLQML 222
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
412-470 |
3.97e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 3.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 412 ISTLSGGERSRllfvgLTLARYSLLMLDepTNHLDMEGKEALAQTLQQfeggVLLVSHD 470
Cdd:COG0419 156 IETLSGGERLR-----LALADLLSLILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-197 |
4.24e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 21 DSLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGTVALAG---------HCL---MARVEQHLpDAIFPLTMLDA 88
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfksskEALengISMVHQEL-NLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 89 V-LAQLPL----AERDSLRWKAETLLAGMGF--TPQDmalQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLdlpTM 161
Cdd:PRK10982 94 MwLGRYPTkgmfVDQDKMYRDTKAIFDELDIdiDPRA---KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556426975 162 LWLEHF------LQNWSGSFVLVSHDR----QLLDAVTngswILRD 197
Cdd:PRK10982 168 KEVNHLftiirkLKERGCGIVYISHKMeeifQLCDEIT----ILRD 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
293-508 |
5.21e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 38.95 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 293 DRLLEMENLSVPPAPGLPPLFNIEMArLKSGDRVAIVGRNGCGKSSLMR-----LIWQQFADESAesGLKIHPRVSPGYY 367
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLS-IPEGSKTALLGPNGAGKSTLLLhlngiYLPQRGRVKVM--GREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 368 DQT--LNQLPDD----ATLLD--ALEP----FAPDPQNRKM--ALISAGFPWSRHgQKISTLSGGERSRLLFVGLTLARY 433
Cdd:PRK13647 79 SKVglVFQDPDDqvfsSTVWDdvAFGPvnmgLDKDEVERRVeeALKAVRMWDFRD-KPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426975 434 SLLMLDEPTNHLDMEGKEALAQTLQQF--EGGVLLVS-HDRQLISQSCNRFWLIEEGKLSEWHDAEAVFER-LRESAGL 508
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEdIVEQAGL 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-157 |
5.55e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 18 TLFDsLSFTLKKGDRIGLLGDNGCGKSTLLKVLDGTDSPAAGT-VALAGHclMARVEQhlPDAIFPLTMLDAVLAQlplA 96
Cdd:PLN03232 632 TLSD-INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGS--VAYVPQ--VSWIFNATVRENILFG---S 703
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426975 97 ERDSLR-WKA---------ETLLAGMGFTpqDMALQSATLSGGQHTRLLLARALIHDPDLLLLDEPSNHLD 157
Cdd:PLN03232 704 DFESERyWRAidvtalqhdLDLLPGRDLT--EIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
20-50 |
5.98e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 5.98e-03
10 20 30
....*....|....*....|....*....|..
gi 556426975 20 FDSLSFTLKKGDRIGLL-GDNGCGKSTLLKVL 50
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAI 45
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
415-503 |
6.26e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.95 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426975 415 LSGGERSRLLFVGLTLARYSLLMLDEPTNHLDMEGKEA---LAQTLQQFEG-GVLLVSHDRQLISQSCNRFWLIEEGKLS 490
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQiieLLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
90
....*....|...
gi 556426975 491 EWHDAEAVFERLR 503
Cdd:PRK11022 234 ETGKAHDIFRAPR 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
295-341 |
8.34e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.76 E-value: 8.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 556426975 295 LLEMENLsVPPAPGLPPLFNIEMaRLKSGDRVAIVGRNGCGKSSLMR 341
Cdd:PRK13549 5 LLEMKNI-TKTFGGVKALDNVSL-KVRAGEIVSLCGENGAGKSTLMK 49
|
|
| |
