|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-645 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 745.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKALDMPA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDEEYWQIQKQLAQPEQLSDSE-LAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLDVSSFSGGWRMRLNL 159
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANERNDGHaIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYSTFEVTRSE 239
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 240 RLAQQQQAFEKQVEARAHLQKFIDRFKAKATKARQAQSRIKQLEKMQLLAPAHVDTPFTFSFREPTKMSSPLLTLDQAEI 319
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 320 GYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQMDALDGQASPMLQLSR 399
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 400 LADKQiSEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA 479
Cdd:PRK10636 401 LAPQE-LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 480 VVLVSHERQLIASVCDDLLLVHAGRCTEFSGDLQDYAKWLREARQQQinaqtalAQASASTNKTAAPAKVDKEAQRKLAA 559
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQE-------NQTDEAPKENNANSAQARKDQKRREA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 560 QRREETRPLRKKIEQCESQIEKIQPRLASIEEQLADSSLYEASRKEDLLKLMNEQTSLKATLEQAEETMLELMMELETLE 639
Cdd:PRK10636 553 ELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEECEMAWLEAQEQLEQML 632
|
....*.
gi 1348983253 640 QSFQNS 645
Cdd:PRK10636 633 LEGQSN 638
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-518 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 706.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 4 FDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKALD-MPALD 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDdLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 83 FVLSGDEEYWQIQKQLAQPEQLSDS------ELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLDVSSFSGGWRMR 156
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEpdedleRLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYSTFEVT 236
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 237 RSERLAQQQQAFEKQVEARAHLQKFIDRFKAKATKARQAQSRIKQLEKMQLLAPAHVDTPFTFSFREPTKMSSPLLTLDQ 316
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 317 AEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQmDALDGQASPMLQ 396
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 397 LSRLADKQiSEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF 476
Cdd:COG0488 400 LRDGAPGG-TEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1348983253 477 EGAVVLVSHERQLIASVCDDLLLVHAGRCTEFSGDLQDYAKW 518
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-520 |
1.09e-127 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 393.46 E-value: 1.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALlgELGADEGSltrPSGWTVAHMAQEVKALDMPAL 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM--AMHAIDGI---PKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 DFVLSGDEEYWQI----------QKQLAQPEQLSDSE---------------LAQLHGRFDEIHGYSAPSKAAQLMAGLG 136
Cdd:PLN03073 253 QCVLNTDIERTQLleeeaqlvaqQRELEFETETGKGKgankdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 137 FMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHIL 216
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 217 HIENQELTLYTGNYSTFEVTRSERLAQQQQAFEKQVEARAHLQKFIDRFKAKATKARQAQSRIKQLEKMQLLAPAHVDTP 296
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 297 FTFSFREPT-KMSSPLLTLDQAEIGYPGKSIASK-ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELL 374
Cdd:PLN03073 493 YKFEFPTPDdRPGPPIISFSDASFGYPGGPLLFKnLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 NIGYFAQHQMDALDGQASPMLQLSRLAdKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCF-PGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 455 DEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFSGDLQDYAKWLR 520
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQ 717
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-515 |
1.80e-110 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 342.64 E-value: 1.80e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKAL-DMP 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFeEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 ALDFVLSGDEEYWQIQKQ----LAQPEqLSDSE---LAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLDVSSFSGG 152
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQErdriYALPE-MSEEDgmkVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 153 WRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYST 232
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 233 FEVTRSERLAQQQQAFEKQVEARAHLQKFIDRFKAKATKARQAQSRIKQLEKMQL--LAPAHVDTPFtFSFREPTKMSSP 310
Cdd:PRK15064 240 YMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLeeVKPSSRQNPF-IRFEQDKKLHRN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQMDALDGQ 390
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFEND 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 391 ASPMLQLSRLADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:PRK15064 399 LTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLN 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1348983253 471 MALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFSGDLQDY 515
Cdd:PRK15064 479 MALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-641 |
1.42e-85 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 280.68 E-value: 1.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 16 LFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEV-KALDMPALDFVLSGDEE---- 90
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPpRNVEGTVYDFVAEGIEEqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 91 ---YWQIQKQLAQ-PEQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLrldVSSFSGGWRMRLNLARTLMSR 166
Cdd:PRK11147 98 lkrYHDISHLVETdPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAA---LSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 167 SDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYSTFEVTRSERL---AQ 243
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALrveEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 244 QQQAFEKQVearAHLQKFIDR-FKAKATK------ARQA--QSRIKQLE-----KMQLlapahvdtpftfsfrEPTKMSS 309
Cdd:PRK11147 255 QNAEFDRKL---AQEEVWIRQgIKARRTRnegrvrALKAlrRERSERREvmgtaKMQV---------------EEASRSG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 310 PLL-TLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQmDALD 388
Cdd:PRK11147 317 KIVfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-AELD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 389 GQASPMlqlSRLAD-KQISEATLR-----SFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK11147 396 PEKTVM---DNLAEgKQEVMVNGRprhvlGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 463 LDMRHALSMALQDFEGAVVLVSHERQLI-ASVCDDLLLVHAGRCTEFSGDLQDyakwlreARQQQINAQTALAQASASTN 541
Cdd:PRK11147 473 VETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKIGRYVGGYHD-------ARQQQAQYLALKQPAVKKKE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 542 KTAAP-AKVDKEAQRKLAAQRREETRPLRKKIEQCESQIEKIQprlasieEQLADSSLYEASRKEdllklMNEQTSLKAT 620
Cdd:PRK11147 546 EAAAPkAETVKRSSKKLSYKLQRELEQLPQLLEDLEAEIEALQ-------AQVADADFFSQPHEQ-----TQKVLADLAD 613
|
650 660
....*....|....*....|.
gi 1348983253 621 LEQAEETMLELMMELETLEQS 641
Cdd:PRK11147 614 AEQELEVAFERWEELEALKNG 634
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-520 |
7.67e-74 |
|
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: 247.16 E-value: 7.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 12 GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGeLGADEGSLTRPS-GWTVAHMAQE--------VKALDMPALD 82
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFNGEARPQpGIKVGYLPQEpqldptktVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 83 FVLSGDEEYWQIQKQLAQPEQLSDS---ELAQLHGRFDEIHGYSAPSKAAQLMaglgfmeHQLRL-----DVSSFSGGWR 154
Cdd:TIGR03719 95 EIKDALDRFNEISAKYAEPDADFDKlaaEQAELQEIIDAADAWDLDSQLEIAM-------DALRCppwdaDVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYSTFE 234
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 235 VTRSERLAQQqqafEKQVEARahlQKFIDR---FKAKATKARQAQS--RIKQLEKMQLLApahvdtpftFSFREPT---- 305
Cdd:TIGR03719 248 EQKQKRLEQE----EKEESAR---QKTLKReleWVRQSPKGRQAKSkaRLARYEELLSQE---------FQKRNETaeiy 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 306 -----KMSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFA 380
Cdd:TIGR03719 312 ippgpRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QHQmDALDGQASPMLQLS------RLADKQISEatlRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:TIGR03719 392 QSR-DALDPNKTVWEEISggldiiKLGKREIPS---RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 455 DEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHA-GRCTEFSGDLQDYAKWLR 520
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGdSHVEWFEGNFSEYEEDKK 534
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-521 |
2.62e-68 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 232.70 E-value: 2.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 12 GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSlTRPS-GWTVAHMAQEVKaLD---------MPAL 81
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-ARPApGIKVGYLPQEPQ-LDpektvrenvEEGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 DFVLSGDEEYWQIQKQLAQPEQLSD---SELAQLHGRFDEIHGYSAPSKAAQLMAGlgfmehqLRL-----DVSSFSGGW 153
Cdd:PRK11819 96 AEVKAALDRFNEIYAAYAEPDADFDalaAEQGELQEIIDAADAWDLDSQLEIAMDA-------LRCppwdaKVTKLSGGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 154 RMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYSTF 233
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 234 EVTRSERLAQQqqafEKQVEARahlQKFIDR---FKAKATKARQAQS--RIKQLEKMQllapahvdtpfTFSFREptkms 308
Cdd:PRK11819 249 LEQKAKRLAQE----EKQEAAR---QKALKReleWVRQSPKARQAKSkaRLARYEELL-----------SEEYQK----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 309 spllTLDQAEI--------------------GYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQR 368
Cdd:PRK11819 306 ----RNETNEIfippgprlgdkvieaenlskSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 369 KASELLNIGYFAQHQmDALDGQASPMLQLS------RLADKQISEatlRSFLGSFGFSGERMDTPCESFSGGERARLALA 442
Cdd:PRK11819 382 KIGETVKLAYVDQSR-DALDPNKTVWEEISggldiiKVGNREIPS---RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 443 LIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLlvhA----GRCTEFSGDLQDYAKW 518
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHIL---AfegdSQVEWFEGNFQEYEED 534
|
...
gi 1348983253 519 LRE 521
Cdd:PRK11819 535 KKR 537
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-222 |
3.02e-57 |
|
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: 189.97 E-value: 3.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQevkaldmpal 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 dfvlsgdeeywqiqkqlaqpeqlsdselaqlhgrfdeihgysapskaaqlmaglgfmehqlrldvssFSGGWRMRLNLAR 161
Cdd:cd03221 71 -------------------------------------------------------------------LSGGEKMRLALAK 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQE 222
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-234 |
1.86e-55 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 196.82 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKALD--M 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDpdK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 PALDfvlsgdeeywqiqkqlaqpeqlsdsELAQLHGRFDEIHgysapskAAQLMAGLGFMEHQLRLDVSSFSGGWRMRLN 158
Cdd:COG0488 395 TVLD-------------------------ELRDGAPGGTEQE-------VRGYLGRFLFSGDDAFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYSTFE 234
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
312-504 |
8.30e-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: 161.85 E-value: 8.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQhqmdaldgqa 391
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 spmlqlsrladkqiseatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 472 ALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
314-536 |
5.40e-43 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 162.16 E-value: 5.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 314 LDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQH----------- 382
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEppldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 --------------QMDALDGQ-ASPMLQLSRLADKQI---------SEATLRSFLGSFGFSGERMDTPCESFSGGERAR 438
Cdd:COG0488 81 tvldgdaelraleaELEELEAKlAEPDEDLERLAELQEefealggweAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 439 LALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFSGdlqDYAKW 518
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPG---NYSAY 237
|
250 260
....*....|....*....|
gi 1348983253 519 L--REARQQQINAQTALAQA 536
Cdd:COG0488 238 LeqRAERLEQEAAAYAKQQK 257
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-517 |
4.66e-36 |
|
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: 142.35 E-value: 4.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 7 VSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGEL---GADEGSLtRPSGWTVAHMAQEVKALD------ 77
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEV-LLDGRDLLELSEALRGRRigmvfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 78 --MPALDFVLSGDEEYWQIQKQLAQPEQlsdselaqlhgrfdeihgysAPSKAAQLMAGLGfMEHQLRLDVSSFSGGWRM 155
Cdd:COG1123 91 dpMTQLNPVTVGDQIAEALENLGLSRAE--------------------ARARVLELLEAVG-LERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 156 RLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLNAYEG-TLILISHDRDFLDAVTDHILHIENQELtlytgnys 231
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI-------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 232 tfevtrserlaqqqqafekqVEArahlqkfidrfkakaTKARQAQSRIKQLEKMQLLAPAHVDTPftfsfrEPTKMSSPL 311
Cdd:COG1123 222 --------------------VED---------------GPPEEILAAPQALAAVPRLGAARGRAA------PAAAAAEPL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASK-----ISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASE 372
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVravddVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSLREL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 373 LLNIGYFAQHQMDALD-----GQ--ASPMLQLSRLADKQIsEATLRSFLGSFGFSGERMDTPCESFSGGERARLALA--L 443
Cdd:COG1123 341 RRRVQMVFQDPYSSLNprmtvGDiiAEPLRLHGLLSRAER-RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAraL 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 444 IVwqRPNVLILDEPTNHLDLDMRHA---LSMALQD-FEGAVVLVSHERQLIASVCDDLLLVHAGRCTE-------FSGDL 512
Cdd:COG1123 420 AL--EPKLLILDEPTSALDVSVQAQilnLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEdgpteevFANPQ 497
|
....*
gi 1348983253 513 QDYAK 517
Cdd:COG1123 498 HPYTR 502
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
216-301 |
3.72e-35 |
|
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: 127.69 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 216 LHIENQELTLYTGNYSTFEVTRSERLAQQQQAFEKQVEARAHLQKFIDRFKAKATKARQAQSRIKQLEKMQLLAPAHVDT 295
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*.
gi 1348983253 296 PfTFSF 301
Cdd:pfam12848 81 P-KLRF 85
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-241 |
1.78e-32 |
|
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: 132.37 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpSGWTV--AHMAQEVKALDmp 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE--IGETVklAYVDQSRDALD-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 aldfvlsGDEEYWqiqkqlaqpEQLSDSeLAQLhgrfdEIHGYSAPSKAaqLMAGLGFM--EHQLRldVSSFSGGWRMRL 157
Cdd:TIGR03719 399 -------PNKTVW---------EEISGG-LDII-----KLGKREIPSRA--YVGRFNFKgsDQQKK--VGQLSGGERNRV 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIE-NQELTLYTGNYSTFEVT 236
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEED 532
|
....*
gi 1348983253 237 RSERL 241
Cdd:TIGR03719 533 KKRRL 537
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-220 |
1.29e-31 |
|
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: 121.82 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgWTVAHMAQevkALDMPA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL----WNGEPIRD---AREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDeeywqiqkQLAQPEQLSDSELAQLHGRFdeiHGYSAPSKAA-QLMAGLGfMEHQLRLDVSSFSGGWRMRLNL 159
Cdd:COG4133 75 RRLAYLGH--------ADGLKPELTVRENLRFWAAL---YGLRADREAIdEALEAVG-LAGLADLPVRQLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY---EGTLILISHDRDFLDAvtDHILHIEN 220
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAA--ARVLDLGD 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-241 |
2.77e-30 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 125.62 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpSGWTV--AHMAQEVKALDmp 79
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK--IGETVklAYVDQSRDALD-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 aldfvlsGDEEYWqiqkqlaqpEQLSDSElaqlhgrfDEIH--GYSAPSKAaqLMAGLGFM--EHQLRldVSSFSGGWRM 155
Cdd:PRK11819 401 -------PNKTVW---------EEISGGL--------DIIKvgNREIPSRA--YVGRFNFKggDQQKK--VGVLSGGERN 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 156 RLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIE-NQELTLYTGNYSTFE 234
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEYE 532
|
....*..
gi 1348983253 235 VTRSERL 241
Cdd:PRK11819 533 EDKKRRL 539
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
311-504 |
2.04e-29 |
|
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: 117.07 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQR----KASEL-LNIGYF 379
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpssgevLLDGRDlaslSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 380 AQHQMDALD---------GQA---SPMLQLSRlADKQISEATLRSfLGSFGFSgermDTPCESFSGGERAR--LALALIv 445
Cdd:COG1120 81 PQEPPAPFGltvrelvalGRYphlGLFGRPSA-EDREAVEEALER-TGLEHLA----DRPVDELSGGERQRvlIARALA- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 446 wQRPNVLILDEPTNHLDLdmRHALSM-----ALQDFEG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG1120 154 -QEPPLLLLDEPTSHLDL--AHQLEVlellrRLARERGrTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
307-527 |
3.02e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLAL------LNGQRKASELLNIGYFA 380
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPtsgtvrLFGKPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QH-QMDA-------------LDGQASPMLQLSRlADKQISEATLRSfLGSFGFSGERMDTpcesFSGGE--RARLALALI 444
Cdd:COG1121 82 QRaEVDWdfpitvrdvvlmgRYGRRGLFRRPSR-ADREAVDEALER-VGLEDLADRPIGE----LSGGQqqRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 445 vwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGRCteFSGDLQDY--AKWL 519
Cdd:COG1121 156 --QDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVltPENL 231
|
....*...
gi 1348983253 520 REARQQQI 527
Cdd:COG1121 232 SRAYGGPV 239
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-257 |
5.72e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.88 E-value: 5.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT------RPSGWTVAHMAQEVK 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 75 A-LDMPA--LDFVLSGdeeywqiqkqlaqpeqlsdseLAQLHGRFdeiHGYSAPSKAA--QLMAGLGfMEHQLRLDVSSF 149
Cdd:COG1121 86 VdWDFPItvRDVVLMG---------------------RYGRRGLF---RRPSRADREAvdEALERVG-LEDLADRPIGEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIeNQELtLY 226
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAateEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGL-VA 218
|
250 260 270
....*....|....*....|....*....|.
gi 1348983253 227 TGnySTFEVTRSERLaqqQQAFEKQVEARAH 257
Cdd:COG1121 219 HG--PPEEVLTPENL---SRAYGGPVALLAH 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
319-506 |
9.80e-28 |
|
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: 109.83 E-value: 9.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 319 IGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNG----------QRKASEL-LNIGYFAQhqmdAL 387
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeilldgkdlaSLSPKELaRKIAYVPQ----AL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 388 DgqaspMLQLSRLADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH 467
Cdd:cd03214 83 E-----LLGLAHLADRPFNE-----------------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 468 ALsMAL-----QDFEGAVVLVSHERQLIASVCDDLLLVHAGRCT 506
Cdd:cd03214 135 EL-LELlrrlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-233 |
8.43e-27 |
|
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: 109.18 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSlTRPSGWTVAHMAQEVKAlDMpa 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGS-ILIDGEDVRKEPREARR-QI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 ldFVLSGDEEYWqiqkqlaqpEQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLdVSSFSGGWRMRLNLA 160
Cdd:COG4555 77 --GVLPDERGLY---------DRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRR-VGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILIS-HDRDFLDAVTDHILHIENQELtLYTGNYSTF 233
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHKGKV-VAQGSLDEL 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-223 |
1.25e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.98 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RP-SGWT-------VAHMA 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgKPlSAMPppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 71 QEVKALDMPALDFvlsgdeeywqiqkqLAQPEQLSdselaqlHGRFDeihgysaPSKAAQLMAGLGFMEHQLRLDVSSFS 150
Cdd:COG4619 81 QEPALWGGTVRDN--------------LPFPFQLR-------ERKFD-------RERALELLERLGLPPDILDKPVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA----ILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQEL 223
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
312-504 |
2.43e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.82 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLV-------GDLaLLNGQ----------RKAsell 374
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAdldpptsGEI-YLDGKplsampppewRRQ---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 nIGYFAQhQMDALDGQASPMLQL-SRLADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:COG4619 76 -VAYVPQ-EPALWGGTVRDNLPFpFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 454 LDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
330-504 |
3.40e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.46 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQ---RKASELL-NIGYFAQHqmDALDGQASPMLQLSR 399
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrptsgeVRVLGEdvaRDPAEVRrRIGYVPQE--PALYPDLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 400 LA-----DKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQ 474
Cdd:COG1131 97 FArlyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLR 175
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 475 DF--EG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG1131 176 ELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
322-526 |
4.31e-26 |
|
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: 112.72 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQ-------------------H 382
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQepqldptktvrenveegvaE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 QMDALD-------GQASPMLQLSRLADKQiseATLRSFLGSF-GFSGERM-------------DTPCESFSGGERARLAL 441
Cdd:TIGR03719 96 IKDALDrfneisaKYAEPDADFDKLAAEQ---AELQEIIDAAdAWDLDSQleiamdalrcppwDADVTKLSGGERRRVAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 442 ALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFSGdlqDYAKWL-- 519
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG---NYSSWLeq 249
|
....*..
gi 1348983253 520 REARQQQ 526
Cdd:TIGR03719 250 KQKRLEQ 256
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
3.88e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 104.38 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQEVKA-----L 76
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV-LGEDVARDPAEVRRrigyvP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DMPALDfvlsgdeeywqiqkqlaqpEQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGfMEHQLRLDVSSFSGGWRMR 156
Cdd:COG1131 80 QEPALY-------------------PDLTVRENLRFFARLYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILIS-HDRDFLDAVTDHIL 216
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-220 |
1.02e-24 |
|
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: 100.78 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 3 QFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqevkaldmpaLD 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------------------ID 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 83 FVLSGDEEYWQIQKQLAqpeqlsdselaqlhgrfdeihgysapskaaqlmaglgfMEHQLrldvssfSGGWRMRLNLART 162
Cdd:cd00267 60 GKDIAKLPLEELRRRIG--------------------------------------YVPQL-------SGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EG-TLILISHDRDFLDAVTDHILHIEN 220
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-223 |
1.15e-24 |
|
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: 102.23 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 3 QFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RPSGWT---VAHMAQEVKAL 76
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPLEKErkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 -DMP--ALDFVLSGdeeywqiqkqlaqpeqlsdselaqLHGRFDEIHGYSAPSKAAQLMA----GLGFMEHQLrldVSSF 149
Cdd:cd03235 81 rDFPisVRDVVLMG------------------------LYGHKGLFRRLSKADKAKVDEAlervGLSELADRQ---IGEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIeNQEL 223
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPktqEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
321-504 |
2.72e-24 |
|
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: 99.78 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQRKASELL----NIGYFAQHqmdaldgq 390
Cdd:cd03230 10 YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkpdsgeIKVLGKDIKKEPEevkrRIGYLPEE-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 391 asPMLqlsrladkqISEATLRSFLgsfgfsgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:cd03230 82 --PSL---------YENLTVRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 1348983253 471 MALQDF---EGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03230 136 ELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-318 |
4.22e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 107.34 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFD--QVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKALDmp 79
Cdd:PRK11147 318 IVFEmeNVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 aldfvlsgdeeywqiqkqlaqPEQLSDSELAQ------LHGRFDEIHGY-----SAPSKAaqlmaglgfmehqlRLDVSS 148
Cdd:PRK11147 396 ---------------------PEKTVMDNLAEgkqevmVNGRPRHVLGYlqdflFHPKRA--------------MTPVKA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHDRDFLD-AVTDHILHIENQELTLYT 227
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDnTVTECWIFEGNGKIGRYV 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 228 GNYSTFEVTRSERLAQQQQAFEKQVEARAHLQKFIDRFKAKATKARQAQ-----SRIKQLEKMQLLAPAHVDTPFTFSfR 302
Cdd:PRK11147 521 GGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLSYKLQREleqlpQLLEDLEAEIEALQAQVADADFFS-Q 599
|
330
....*....|....*.
gi 1348983253 303 EPTKMSSPLLTLDQAE 318
Cdd:PRK11147 600 PHEQTQKVLADLADAE 615
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
314-500 |
5.45e-24 |
|
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: 100.30 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 314 LDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQRKASELLNIGYFAQH-QMD- 385
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkptsgsIRVFGKPLEKERKRIGYVPQRrSIDr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 ------------ALDGQASPMLQLSRlADKQISEATLRsFLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLI 453
Cdd:cd03235 82 dfpisvrdvvlmGLYGHKGLFRRLSK-ADKAKVDEALE-RVGLSELADRQIGE----LSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 454 LDEPTNHLDLDMRHA---LSMALQDFEGAVVLVSHERQLIASVCDDLLLV 500
Cdd:cd03235 156 LDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-223 |
1.00e-23 |
|
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: 98.24 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqevkaldmpal 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 dfvlsgdeeywqiqkqlaqpeqlsdselaqlhgrfdeIHGYSAPSKAAQLMAGLGFMEHQLRL-------DVSSFSGGWR 154
Cdd:cd03230 59 -------------------------------------VLGKDIKKEPEEVKRRIGYLPEEPSLyenltvrENLKLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILI-SHDRDFLDAVTDHILHIENQEL 223
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkEGKTILLsSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-220 |
1.09e-23 |
|
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: 99.46 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 3 QFDQVSLRRGG--RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT----RPSGWTVAHMAQEVK-A 75
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkDLTKLSLKELRRKVGlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 76 LDMPALDFVLS--GDEeywqiqkqLAQ-PEQLSDSElaqlhgrfDEIHgysapSKAAQLMAGLGfMEHQLRLDVSSFSGG 152
Cdd:cd03225 81 FQNPDDQFFGPtvEEE--------VAFgLENLGLPE--------EEIE-----ERVEEALELVG-LEGLRDRSPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 153 WRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EG-TLILISHDRDFLDAVTDHILHIEN 220
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
322-526 |
5.50e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 103.27 E-value: 5.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQ-------------------H 382
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQepqldpektvrenveegvaE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 QMDALD-------GQASPMLQLSRLADKQ-----ISEAT----LRSFLgsfgfsgER-M--------DTPCESFSGGERA 437
Cdd:PRK11819 98 VKAALDrfneiyaAYAEPDADFDALAAEQgelqeIIDAAdawdLDSQL-------EIaMdalrcppwDAKVTKLSGGERR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 438 RLALALIVWQRPNVLILDEPTNHLDldmrhALSMA-----LQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFSGdl 512
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLD-----AESVAwleqfLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG-- 243
|
250
....*....|....*.
gi 1348983253 513 qDYAKWL--REARQQQ 526
Cdd:PRK11819 244 -NYSSWLeqKAKRLAQ 258
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
330-504 |
9.49e-23 |
|
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: 97.62 E-value: 9.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQRKASELL-----------------------NIGYFA 380
Cdd:COG4555 20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkpdsgsILIDGEDVRKEPRearrqigvlpderglydrltvreNIRYFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QhqmdaldgqaspmlqLSRLADKQISEATlRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNH 460
Cdd:COG4555 100 E---------------LYGLFDEELKKRI-EELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 461 LDLDMRHALS---MALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG4555 163 LDVMARRLLReilRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-204 |
3.34e-22 |
|
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: 96.27 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RP-SGWT-------VAHM 69
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlASLSrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 70 AQEVKA-LDMPALDFVLsgdeeywqiqkqlaqpeqlsdselaqlHGRFDEIHGYSAPSK-----AAQLMAGLGFMEHQLR 143
Cdd:COG1120 81 PQEPPApFGLTVRELVA---------------------------LGRYPHLGLFGRPSAedreaVEEALERTGLEHLADR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 144 lDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLNAYEG-TLILISHD 204
Cdd:COG1120 134 -PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqlEVLELLRRLARERGrTVVMVLHD 197
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
7-216 |
4.07e-22 |
|
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: 96.04 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 7 VSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrPSGWTVAHMAQEVKALdmpaldfvls 86
Cdd:TIGR03873 7 VSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-LAGVDLHGLSRRARAR---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 87 gdeeywqiqkQLAQPEQLSDSEL------AQLHGR--FDEIHGYSAPSKAAQLMAGLGFME--HQLRLDVSSFSGGWRMR 156
Cdd:TIGR03873 76 ----------RVALVEQDSDTAVpltvrdVVALGRipHRSLWAGDSPHDAAVVDRALARTElsHLADRDMSTLSGGERQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLN--AYEGTLILIS-HDRDFLDAVTDHIL 216
Cdd:TIGR03873 146 VHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRelAATGVTVVAAlHDLNLAASYCDHVV 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-223 |
5.68e-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: 95.09 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR-RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGsltrpsgwtvahmaqEVKALDMPA 80
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG---------------EVLVDGKDI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 ldfvlsGDEEYWQIQKQLA----QPEQlsdselaQLHGR--FDEI------HGYS---APSKAAQLMAGLGfMEHQLRLD 145
Cdd:COG1122 66 ------TKKNLRELRRKVGlvfqNPDD-------QLFAPtvEEDVafgpenLGLPreeIRERVEEALELVG-LEHLADRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 146 VSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EG-TLILISHDRDFLDAVTDHILHIENQE 222
Cdd:COG1122 132 PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
.
gi 1348983253 223 L 223
Cdd:COG1122 212 I 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
321-504 |
8.32e-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: 94.32 E-value: 8.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIA-SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ----RKASELL-NIGY---FAQHQM- 384
Cdd:COG1122 10 YPGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKptsgevLVDGKditkKNLRELRrKVGLvfqNPDDQLf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 ------D-ALdgqaSPM-LQLSR-LADKQISEAtlrsfLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILD 455
Cdd:COG1122 90 aptveeDvAF----GPEnLGLPReEIRERVEEA-----LELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 456 EPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
1.43e-21 |
|
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: 93.05 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT-RPSGWTVAHMAQEVKA--LDM 78
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRIGalIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 PALDFVLSGDEEYWQIQKQLAQPEQLSDSELAqlhgrfdeihgysapskaaqlMAGLGFMEHQLrldVSSFSGGWRMRLN 158
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLD---------------------VVGLKDSAKKK---VKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LNAYEGTLILISHDRDFLDAVTDHI 215
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
330-459 |
3.08e-21 |
|
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: 90.40 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQ-----RKASELLNIGYFAQH-----QMDALD--GQA 391
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsptegtILLDGQdltddERKSLRKEIGYVFQDpqlfpRLTVREnlRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 392 SPMLQLSRLADKQISEAtLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:pfam00005 84 LLLKGLSKREKDARAEE-ALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
321-504 |
3.42e-21 |
|
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: 92.14 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIAS--KISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKASELL-----NIGY---FAQHQM 384
Cdd:cd03225 9 YPDGARPAldDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGptsgevLVDGKDLTKLSLkelrrKVGLvfqNPDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 ---DALDGQASPMLQLSrLADKQISEATLRSfLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03225 89 fgpTVEEEVAFGLENLG-LPEEEIEERVEEA-LELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1348983253 462 DLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03225 166 DPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-177 |
3.81e-21 |
|
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: 90.01 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqevkaldmpaLDFVLSGDEEYWQIQKQLA- 99
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIL---------------------LDGQDLTDDERKSLRKEIGy 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 100 --QPEQLSDSELAQ----LHGRFDEIHGYSAPSKAAQLMAGLG---FMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLL 170
Cdd:pfam00005 64 vfQDPQLFPRLTVRenlrLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 1348983253 171 LLDEPTN 177
Cdd:pfam00005 144 LLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
321-504 |
6.02e-21 |
|
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: 90.00 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQrkasellnIgyfaqhqmdaldgqaspmlqlsRL 400
Cdd:cd00267 9 YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE--------I----------------------LI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 401 ADKQISEATLRSFLGSFGFsgermdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG 478
Cdd:cd00267 59 DGKDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEG 130
|
170 180
....*....|....*....|....*..
gi 1348983253 479 -AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd00267 131 rTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
2.12e-20 |
|
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: 95.22 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRR--GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---------RPSGW--TVAH 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 69 MAQEVKALDMPALDFVLsgdeeywqiqkqLAQPEqLSDSELAQlhgrfdeihgysapskAAQLmAGLGFMEHQLR--LDV 146
Cdd:COG4987 414 VPQRPHLFDTTLRENLR------------LARPD-ATDEELWA----------------ALER-VGLGDWLAALPdgLDT 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 147 ------SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIlwLEDWLNAYEG-TLILISHDRDFLDAVtDHIL 216
Cdd:COG4987 464 wlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQAL--LADLLEALAGrTVLLITHRLAGLERM-DRIL 540
|
....*...
gi 1348983253 217 HIENQELT 224
Cdd:COG4987 541 VLEDGRIV 548
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
321-504 |
2.17e-20 |
|
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: 89.94 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSrIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ---RKASELLN-IGYFAQHQM------ 384
Cdd:cd03264 10 YGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPpssgtiRIDGQdvlKQPQKLRRrIGYLPQEFGvypnft 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 --DALDGQASpmlqLSRLADKQISEATLRSfLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03264 89 vrEFLDYIAW----LKGIPSKEVKARVDEV-LELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 463 LDMRHALSMALQDF-EGAVVLVS-HERQLIASVCDDLLLVHAGR 504
Cdd:cd03264 163 PEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGK 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
310-493 |
5.63e-20 |
|
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: 88.69 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 310 PLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKASELL----NIGYF 379
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpsagevLWNGEPIRDAREdyrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 380 AQHqmDALDGQASP--MLQL-SRLADKQISEATLRSFLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILD 455
Cdd:COG4133 81 GHA--DGLKPELTVreNLRFwAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALArLLLSPAP-LWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1348983253 456 EPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASV 493
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
321-504 |
7.90e-20 |
|
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: 87.27 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKS--IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKasellnigyfaqhqmdaLDGQASpmlqls 398
Cdd:cd03246 10 YPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----------------LDGADI------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 399 rladKQISEATLRSFLGSFG-----FSGERMDTpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL 473
Cdd:cd03246 67 ----SQWDPNELGDHVGYLPqddelFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....
gi 1348983253 474 QDFEGA---VVLVSHERQLIASvCDDLLLVHAGR 504
Cdd:cd03246 140 AALKAAgatRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-219 |
9.25e-20 |
|
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: 88.65 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 11 RGGRVL--FQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS--LTRPSGWT-VAHmAQEVKALDM------- 78
Cdd:COG4778 19 QGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVdLAQ-ASPREILALrrrtigy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 -----------PALDFVlsgdeeywqiqkqlAQP--EQLSDSELAQlhgrfdeihgysapSKAAQLMAGLGFMEHQLRLD 145
Cdd:COG4778 98 vsqflrviprvSALDVV--------------AEPllERGVDREEAR--------------ARARELLARLNLPERLWDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 146 VSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDwlnayEGTLIL-ISHDRDFLDAVTDHILH 217
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravvVELIEEAKA-----RGTAIIgIFHDEEVREAVADRVVD 224
|
..
gi 1348983253 218 IE 219
Cdd:COG4778 225 VT 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-504 |
1.37e-19 |
|
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: 87.66 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG------DLALLNG---QRKASELLNIGYFAQHQmdALDGQA 391
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlikpdsGEITFDGksyQKNIEALRRIGALIEAP--GFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 SPMLQLSRLAD-KQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LDMR 466
Cdd:cd03268 88 TARENLRLLARlLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgiKELR 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1348983253 467 hALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03268 167 -ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
309-507 |
1.54e-19 |
|
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: 92.27 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 309 SPLLTLDQAEIGYPGKSIAS--KISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL---------ALLNGQ--RKASELL- 374
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggrisgeVLLDGRdlLELSEALr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 --NIGYFAQHQMDALDG-----QASPMLQLSRLADKQISEATLRSfLGSFGFsGERMDTPCESFSGGERARLALALIVWQ 447
Cdd:COG1123 82 grRIGMVFQDPMTQLNPvtvgdQIAEALENLGLSRAEARARVLEL-LEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 448 RPNVLILDEPTNHLDLDMRH---ALSMALQDFEG-AVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAeilDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
2.07e-19 |
|
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: 88.22 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGsltrpsgwtvahmaQEVKALDMPA 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG--------------NDVRLFGERR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 ldfvlsGDEEYWQIQKQLAqpeqLSDSELAQ------------LHGRFDEIHGYSAPS-----KAAQLMAGLGfMEHQLR 143
Cdd:COG1119 69 ------GGEDVWELRKRIG----LVSPALQLrfprdetvldvvLSGFFDSIGLYREPTdeqreRARELLELLG-LAHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 144 LDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLN--AYEG--TLILISHDRDFLDAVTDHILHIE 219
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDklAAEGapTLVLVTHHVEEIPPGITHVLLLK 217
|
.
gi 1348983253 220 N 220
Cdd:COG1119 218 D 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
2.29e-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: 92.13 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRR-GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtrpsgwTVAHmaQEVKALDMPA 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI------LING--VDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LdfvlsgdeeywqiQKQLA----QP---------------EQLSDSEL------AQLHgrfDEIhgysapskaAQLMAGL 135
Cdd:COG4988 409 W-------------RRQIAwvpqNPylfagtirenlrlgrPDASDEELeaaleaAGLD---EFV---------AALPDGL 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 136 GFM--EHQLRLdvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLedwlnAYEGTLILISHDRD 206
Cdd:COG4988 464 DTPlgEGGRGL-----SGGQAQRLALARALLRDAPLLLLDEPTAHLDaeteaeiLQALRRL-----AKGRTVILITHRLA 533
|
250
....*....|....*...
gi 1348983253 207 FLDAVtDHILHIENQELT 224
Cdd:COG4988 534 LLAQA-DRILVLDDGRIV 550
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
272-507 |
2.77e-19 |
|
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: 91.75 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 272 ARQAQSRIKQLekmqllapAHVDTPFTFSFREPTKMSSPLLTLDQAEIGYPGKS--IASKISLQITPSSRIGLLGMNGAG 349
Cdd:COG4987 302 VRAAARRLNEL--------LDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 350 KSTLIKSLVGDLA------LLNGqRKASELL------NIGYFAQHQ-------MDALdgqaspmlqlsRLADKQISEATL 410
Cdd:COG4987 374 KSTLLALLLRFLDpqsgsiTLGG-VDLRDLDeddlrrRIAVVPQRPhlfdttlRENL-----------RLARPDATDEEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 411 RSFLGSFGFSG------ERMDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsmaLQDFEGA- 479
Cdd:COG4987 442 WAALERVGLGDwlaalpDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEAl 518
|
250 260 270
....*....|....*....|....*....|..
gi 1348983253 480 ----VVLVSHERQLIASVcDDLLLVHAGRCTE 507
Cdd:COG4987 519 agrtVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
2.87e-19 |
|
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: 87.79 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS-------LTRPSGWTVAH--MA- 70
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRilfdgrdITGLPPHRIARlgIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 71 --QEVKAL-DMPALDFVLSGdeeywqiqKQLAQPEQLSDSELAQLHGRFDEIhgySAPSKAAQLMAGLGfMEHQLRLDVS 147
Cdd:COG0411 84 tfQNPRLFpELTVLENVLVA--------AHARLGRGLLAALLRLPRARREER---EARERAEELLERVG-LADRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPT---NHLDLDAILWLEDWLNAYEG-TLILISHDRDFLDAVTDHIL 216
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
307-535 |
4.10e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 91.55 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSspLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ------------------- 367
Cdd:PRK11147 1 MS--LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivarlqqdpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 368 -------------RKASELLNIGYFAQHQMdALDGQASPMLQLSRLADK-------QIsEATLRSFLGSFGFSGermDTP 427
Cdd:PRK11147 79 vegtvydfvaegiEEQAEYLKRYHDISHLV-ETDPSEKNLNELAKLQEQldhhnlwQL-ENRINEVLAQLGLDP---DAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 428 CESFSGG--ERARLALALIVwqRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRC 505
Cdd:PRK11147 154 LSSLSGGwlRKAALGRALVS--NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1348983253 506 TEFSGDLQDY----AKWLR-EARQqqiNAQ--TALAQ 535
Cdd:PRK11147 232 VSYPGNYDQYllekEEALRvEELQ---NAEfdRKLAQ 265
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
4.21e-19 |
|
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: 85.18 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 5 DQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqevkaldmpaldfv 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 85 LSGDEeywqiqkqlaqPEQLSDSELAQLhgrfdeIhGYsapskAAQLMAGLGfMEHQLRLDVSSFSGGWRMRLNLARTLM 164
Cdd:cd03214 58 LDGKD-----------LASLSPKELARK------I-AY-----VPQALELLG-LAHLADRPFNELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 165 SRSDLLLLDEPTNHLDL---DAILWLEDWLNAYEG-TLILISHDRDFLDAVTDHILHIENQELTLY 226
Cdd:cd03214 114 QEPPILLLDEPTSHLDIahqIELLELLRRLARERGkTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
312-504 |
9.91e-19 |
|
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: 86.41 E-value: 9.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLAL-----------LNGQRKASELLNIGYFA 380
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPdagtvdlagvdLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QHQMDALDGQASPMLQLSRL-------ADKQISEATLRSFLGSFG---FSGERMDTpcesFSGGERARLALALIVWQRPN 450
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIphrslwaGDSPHDAAVVDRALARTElshLADRDMST----LSGGERQRVHVARALAQEPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 451 VLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVS-HERQLIASVCDDLLLVHAGR 504
Cdd:TIGR03873 158 LLLLDEPTNHLDVRAQLETLALVRELaaTGVTVVAAlHDLNLAASYCDHVVVLDGGR 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-504 |
2.19e-18 |
|
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: 88.71 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgADEGSLTrpSGWTVAHMA--QEVKALDMP 79
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG---MDQYEPT--SGRIIYHVAlcEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 A-----------------LDFVLSGDEEYWQIQKQLAQPEQLS------DSELAQLHGRFDEIhGYSAPS---KAAQLMA 133
Cdd:TIGR03269 76 SkvgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfalygdDTVLDNVLEALEEI-GYEGKEavgRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 134 GLGfMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-LDAIL---WLEDWLNAYEGTLILISHDRDFLD 209
Cdd:TIGR03269 155 MVQ-LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLvhnALEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 210 AVTDHILHIENQELTLyTGNYStfEVtrSERLAQQQQAFEKQVEARahlqkfidrFKAKATKARQAQSRIKQLEKMQLLA 289
Cdd:TIGR03269 234 DLSDKAIWLENGEIKE-EGTPD--EV--VAVFMEGVSEVEKECEVE---------VGEPIIKVRNVSKRYISVDRGVVKA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 290 PAHVDtpftfsfreptkmssplLTLDQAEIgypgksiaskislqitpssrIGLLGMNGAGKSTLIKSLVGDLALLNGQ-- 367
Cdd:TIGR03269 300 VDNVS-----------------LEVKEGEI--------------------FGIVGTSGAGKTTLSKIIAGVLEPTSGEvn 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 368 -RKASELLN---------------IGYFaqHQMDALDGQASPMLQLSRLADKQISE--ATLRSF--LGSFGFSGER---- 423
Cdd:TIGR03269 343 vRVGDEWVDmtkpgpdgrgrakryIGIL--HQEYDLYPHRTVLDNLTEAIGLELPDelARMKAVitLKMVGFDEEKaeei 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 424 MDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLL 499
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAAL 500
|
....*
gi 1348983253 500 VHAGR 504
Cdd:TIGR03269 501 MRDGK 505
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
330-504 |
3.47e-18 |
|
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: 83.71 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQRKASELL----NIGYFAQHqmDALDGQASPM--LQL 397
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrptsgtAYINGYSIRTDRKaarqSLGYCPQF--DALFDELTVRehLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 -------SRLADKQISEATLRSF-LGSFgfsgerMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHAL 469
Cdd:cd03263 99 yarlkglPKSEIKEEVELLLRVLgLTDK------ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1348983253 470 SMALQDFEG--AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03263 173 WDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
311-508 |
1.05e-17 |
|
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: 82.55 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKSIASK----ISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASE 372
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalddVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiifdgkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 373 LLNIGYFAQHQMDALD-----GQ--ASPMLQLSRLADKQISEATLRSFLGSFGFSGERMDT-PCEsFSGGERAR--LALA 442
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprmtiGEqiAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHE-LSGGQRQRvaIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 443 LIVwqRPNVLILDEPTNHLDLDMRH---ALSMALQD-FEGAVVLVSHERQLIASVCDDLLLVHAGRCTEF 508
Cdd:cd03257 160 LAL--NPKLLIADEPTSALDVSVQAqilDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
320-504 |
2.89e-17 |
|
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: 79.73 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 320 GYPGKS--IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGqrkasELLnigyfaqhqmdaLDGQASPMLQL 397
Cdd:cd03228 9 SYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG-----EIL------------IDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 SRLAdKQISEATLRSFLgsfgFSGermdTPCES-FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF 476
Cdd:cd03228 72 ESLR-KNIAYVPQDPFL----FSG----TIRENiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|
gi 1348983253 477 EG--AVVLVSHERQLIASvCDDLLLVHAGR 504
Cdd:cd03228 143 AKgkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
312-504 |
3.89e-17 |
|
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: 80.71 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIAS--KISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNG----QRKASELL-NIGY 378
Cdd:cd03245 3 IEFRNVSFSYPNQEIPAldNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkptsgsVLLDGtdirQLDPADLRrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 379 FAQHQMdALDGQASPMLQLSRLA--DKQISEATLRSFLGSF------GFS---GERMDtpceSFSGGERARLALALIVWQ 447
Cdd:cd03245 83 VPQDVT-LFYGTLRDNITLGAPLadDERILRAAELAGVTDFvnkhpnGLDlqiGERGR----GLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 448 RPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHeRQLIASVCDDLLLVHAGR 504
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGR 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-246 |
5.24e-17 |
|
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: 84.89 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR--RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---------RPSGWT--VAH 68
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASLRrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 69 MAQEVK----------ALDMPALDfvlsgDEEYWQIqkqlaqpeqlsdSELAQLHgrfDEIhgysapskaAQLMAGLgfm 138
Cdd:COG2274 554 VLQDVFlfsgtireniTLGDPDAT-----DEEIIEA------------ARLAGLH---DFI---------EALPMGY--- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 139 EHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAIL-WLEDWlnayegTLILISHDRDFLDA 210
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDaeteaiiLENLRrLLKGR------TVIIIAHRLSTIRL 675
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1348983253 211 VtDHILHIEN---------QELTLYTGNYStfevtrseRLAQQQQ 246
Cdd:COG2274 676 A-DRIIVLDKgrivedgthEELLARKGLYA--------ELVQQQL 711
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
323-505 |
5.29e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKAS----ELlnigyfAQHQmdALDGQAS 392
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSpdsgevRLNGRPLADwspaEL------ARRR--AVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 PM----------------LQLSRLADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLALALI---VWQ---RPN 450
Cdd:PRK13548 86 SLsfpftveevvamgrapHGLSRAEDDALVAAALAQ-VDLAHLAGRDYPQ----LSGGEQQRVQLARVlaqLWEpdgPPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 451 VLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDDLLLVHAGRC 505
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
323-504 |
5.87e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.93 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQR----KASELlnigyfAQHQmdALDGQAS 392
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTpssgevRLNGRPlaawSPWEL------ARRR--AVLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 PM----------------LQLSRLADKQISEATLrsflgsfgfsgERMDtpCESF--------SGGERAR--LALALI-V 445
Cdd:COG4559 85 SLafpftveevvalgrapHGSSAAQDRQIVREAL-----------ALVG--LAHLagrsyqtlSGGEQQRvqLARVLAqL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 446 WQ----RPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG4559 152 WEpvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
6.44e-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: 80.10 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLR----RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrPSGWTVAHMAQEVKAl 76
Cdd:cd03266 1 MITADALTKRfrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT-VDGFDVVKEPAEARR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 dmpALDFVLSGDEEYwqiqkqlaqpEQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGfMEHQLRLDVSSFSGGWRMR 156
Cdd:cd03266 79 ---RLGFVSDSTGLY----------DRLTARENLEYFAGLYGLKGDELTARLEELADRLG-MEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILIS-HDRDFLDAVTDHI 215
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGKCILFStHIMQEVERLCDRV 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
330-504 |
8.59e-17 |
|
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: 79.63 E-value: 8.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKASELLN-IGYFAQHQ-----MDALDgqasPMLQL 397
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILpdsgevLFDGKPLDIAARNrIGYLPEERglypkMKVID----QLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 SRLADKQISEA--TLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD-LDMRHALS--MA 472
Cdd:cd03269 95 AQLKGLKKEEArrRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpVNVELLKDviRE 173
|
170 180 190
....*....|....*....|....*....|..
gi 1348983253 473 LQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03269 174 LARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
1.09e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.33 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLR-RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS-------LTRPSGWTVAHM--- 69
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdLSRLKRREIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 70 ----AQEVKAL-DMPALD---FVLsgdeeywqiqkqlaqpeqlsdselaqlhgrfdEIHGYSAPSKAAQLMA-----GLG 136
Cdd:COG2884 81 igvvFQDFRLLpDRTVYEnvaLPL--------------------------------RVTGKSRKEIRRRVREvldlvGLS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 137 ----FMEHQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLNAyEGTLILI-SHDRDFL 208
Cdd:COG2884 129 dkakALPHEL-------SGGEQQRVAIARALVNRPELLLADEPTGNLDPETsweIMELLEEINR-RGTTVLIaTHDLELV 200
|
250
....*....|....*.
gi 1348983253 209 DAVTDHILHIENQELT 224
Cdd:COG2884 201 DRMPKRVLELEDGRLV 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
270-485 |
1.15e-16 |
|
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: 83.56 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 270 TKARQAQSRIKQLEKMQLLAPAHVD-TPFTFSFREPTkmssplLTLDQAEIGYPGKSIA-SKISLQITPSSRIGLLGMNG 347
Cdd:TIGR02868 298 TRVRAAAERIVEVLDAAGPVAEGSApAAGAVGLGKPT------LELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 348 AGKSTLIKSLVGDLA------LLNGQRKASELLN-----IGYFAQ--HQMDaldgqaSPMLQLSRLADKQISEATLRSFL 414
Cdd:TIGR02868 372 SGKSTLLATLAGLLDplqgevTLDGVPVSSLDQDevrrrVSVCAQdaHLFD------TTVRENLRLARPDATDEELWAAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 415 GSFGFS------GERMDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA-LSMALQDFEG-AVVL 482
Cdd:TIGR02868 446 ERVGLAdwlralPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADElLEDLLAALSGrTVVL 525
|
...
gi 1348983253 483 VSH 485
Cdd:TIGR02868 526 ITH 528
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.52e-16 |
|
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: 78.95 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrPSGWTVAHMAQEVKA-----L 76
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHDVVREPREVRRrigivF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DMPALDFVLSGDEE-YWqiqkqlaqpeqlsdselaqlHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLdVSSFSGGWRM 155
Cdd:cd03265 80 QDLSVDDELTGWENlYI--------------------HARLYGVPGAERRERIDELLDFVGLLEAADRL-VKTYSGGMRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 156 RLNLARTLMSRSDLLLLDEPTNHLDLDAI--LW--LEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQEL 223
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-181 |
1.85e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RP-SGWTVAHMAQ----- 71
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngRPlADWSPAELARrravl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 72 -------------EVKAldMPALDFVLSGDEEywqiqKQLAQpEQLSDSELAQLHGRFdeihgYsapskaaqlmaglgfm 138
Cdd:PRK13548 82 pqhsslsfpftveEVVA--MGRAPHGLSRAED-----DALVA-AALAQVDLAHLAGRD-----Y---------------- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1348983253 139 eHQLrldvssfSGGWRMRLNLARTLMSRSD------LLLLDEPTNHLDL 181
Cdd:PRK13548 133 -PQL-------SGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDL 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
302-507 |
2.45e-16 |
|
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: 82.50 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 302 REPTKMSSPLLTLDQAEIGYP-GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQrkasELL 374
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPpysgsiLINGV----DLS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 NIGYFAQHQMDALDGQASPMLQLS-----RLADKQISEATLRSFLGSFGFSG------ERMDTPCES----FSGGERARL 439
Cdd:COG4988 403 DLDPASWRRQIAWVPQNPYLFAGTirenlRLGRPDASDEELEAALEAAGLDEfvaalpDGLDTPLGEggrgLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEG-AVVLVSHERQLIASvCDDLLLVHAGRCTE 507
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGrTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
312-507 |
2.62e-16 |
|
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: 77.35 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKS--IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGqrkasELLnigyfaqhqmdaLDG 389
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG-----EIT------------LDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 390 qaSPMLQLSRLADKQISEATLRSFLgsfgFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD-LDMRHA 468
Cdd:cd03247 64 --VPVSDLEKALSSLISVLNQRPYL----FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1348983253 469 LSMALQDFEG-AVVLVSHERQLIASVcDDLLLVHAGRCTE 507
Cdd:cd03247 138 LSLIFEVLKDkTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-220 |
3.43e-16 |
|
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: 78.69 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRG----GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT--------RPSGW---T 65
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrRRRKAfrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 66 VAHMAQEVKAldmpALDfvlsgdeEYWQIQKQLAQPeqlsdselAQLHGRFDeihgysAPSKAAQLMA--GLG--FME-- 139
Cdd:COG1124 81 VQMVFQDPYA----SLH-------PRHTVDRILAEP--------LRIHGLPD------REERIAELLEqvGLPpsFLDry 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 140 -HQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIL-WLEDWLNAYEGTLILISHDRDFLDAVTDH 214
Cdd:COG1124 136 pHQL-------SGGQRQRVAIARALILEPELLLLDEPTSALDVsvqAEILnLLKDLREERGLTYLFVSHDLAVVAHLCDR 208
|
....*.
gi 1348983253 215 ILHIEN 220
Cdd:COG1124 209 VAVMQN 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
329-504 |
3.53e-16 |
|
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: 78.14 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 329 KISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL----------ALLNGQRKASELLNIGY-FAQHQMDALDgqASPMLQL 397
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqptsgevrvaGLVPWKRRKKFLRRIGVvFGQKTQLWWD--LPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 SRLAD-KQISEATLRSFLGsfGFS-----GERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03267 117 YLLAAiYDLPPARFKKRLD--ELSelldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190
....*....|....*....|....*....|....*..
gi 1348983253 472 ALQDF----EGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03267 195 FLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
323-505 |
4.15e-16 |
|
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: 77.21 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA--------LLNGQRKASELLN--IGYFAQHqmDALdgqas 392
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglgvsgevLINGRPLDKRSFRkiIGYVPQD--DIL----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 pmlqlsrladkqISEATLRSFLGsfgFSGErmdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMA 472
Cdd:cd03213 94 ------------HPTLTVRETLM---FAAK-----LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1348983253 473 LQDF--EGAVVLVS-HE-RQLIASVCDDLLLVHAGRC 505
Cdd:cd03213 154 LRRLadTGRTIICSiHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
330-504 |
4.80e-16 |
|
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: 77.41 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNG----QRKASELLNIGYFAQHqmDALDGQASPMLQLSR 399
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLepdagfATVDGfdvvKEPAEARRRLGFVSDS--TGLYDRLTARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 400 LAD-----KQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQ 474
Cdd:cd03266 102 FAGlyglkGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 475 DF--EG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03266 181 QLraLGkCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
321-503 |
5.21e-16 |
|
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: 76.91 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNG-QRKASELL-NIGYFAQHQMDALdGQAS 392
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkessgsILLNGkPIKAKERRkSIGYVMQDVDYQL-FTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 PMLQLsRLADKQISE--ATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLdmRHALS 470
Cdd:cd03226 89 VREEL-LLGLKELDAgnEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY--KNMER 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1348983253 471 MA-----LQDFEGAVVLVSHERQLIASVCDDLLLVHAG 503
Cdd:cd03226 165 VGelireLAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
320-499 |
6.40e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 320 GYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQmdALD----------- 388
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRS--EVPdslpltvrdlv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 389 -----GQASPMLQLSRLADKQISEATLRsfLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDL 463
Cdd:NF040873 79 amgrwARRGLWRRLTRDDRAAVDDALER--VGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1348983253 464 DMRHALSMALQDFEG---AVVLVSHERQLIASVCDDLLL 499
Cdd:NF040873 153 ESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-218 |
7.19e-16 |
|
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: 80.79 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR-RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtRPSGWTVAHmaqevkaldmpa 80
Cdd:TIGR02857 322 LEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-AVNGVPLAD------------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 ldfvlsGDEEYWQiqKQLA----QPEQLSDS-----ELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEH-QLRLDVSSFS 150
Cdd:TIGR02857 389 ------ADADSWR--DQIAwvpqHPFLFAGTiaeniRLARPDASDAEIREALERAGLDEFVAALPQGLDtPIGEGGAGLS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEG--TLILISHDRDFLdAVTDHILHI 218
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
318-514 |
8.59e-16 |
|
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: 77.16 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 318 EIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQR----KASELL----NIGYFAQH- 382
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpdsgevLIDGEDisglSEAELYrlrrRMGMLFQSg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 ----QMDALDGQASPMLQLSRLADKQISEATlRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPT 458
Cdd:cd03261 87 alfdSLTVFENVAFPLREHTRLSEEEIREIV-LEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 459 NHLD---LDMRHALSMALQDFEGA-VVLVSHERQLIASVCDDLLLVHAGRcTEFSGDLQD 514
Cdd:cd03261 165 AGLDpiaSGVIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGK-IVAEGTPEE 223
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
314-562 |
1.15e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 80.67 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 314 LDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL---------------------VGD------------ 360
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkncqilhveqevVGDdttalqcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 361 ----------LALLNGQRKASELLNIGYFAQHQMDALDGQA-----SPMLQLSRLADKQISEATLRSFLGSFGFSGERMD 425
Cdd:PLN03073 260 iertqlleeeAQLVAQQRELEFETETGKGKGANKDGVDKDAvsqrlEEIYKRLELIDAYTAEARAASILAGLSFTPEMQV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 426 TPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRC 505
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 506 TEFSGDLQDYAKwlreARQQQINAQTALAQASASTnKTAAPAKVDK---EAQRKLAAQRR 562
Cdd:PLN03073 420 VTYKGDYDTFER----TREEQLKNQQKAFESNERS-RSHMQAFIDKfryNAKRASLVQSR 474
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
1.19e-15 |
|
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: 76.14 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 7 VSLRRGGRVLfQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALDMPALDFVLS 86
Cdd:cd03226 7 FSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAG--------LIKESSGSILLNGKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 87 GDEEYwqiqkqlaqpeQL-SDSELAQLHGRFDEIHGYsaPSKAAQLMAGLGFMEHQLRLDVSsFSGGWRMRLNLARTLMS 165
Cdd:cd03226 78 QDVDY-----------QLfTDSVREELLLGLKELDAG--NEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 166 RSDLLLLDEPTNHLDLDAILWLEDW---LNAYEGTLILISHDRDFLDAVTDHILHIEN 220
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
309-498 |
1.20e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 309 SPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQ--HQMDA 386
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 LDGQASPMLQLS-RLADKQISEATLRSflgsfgFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:PRK09544 82 LPLTVNRFLRLRpGTKKEDILPALKRV------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1348983253 466 RHAL----SMALQDFEGAVVLVSHERQLIASVCDDLL 498
Cdd:PRK09544 156 QVALydliDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-220 |
1.27e-15 |
|
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: 75.11 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGR--VLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqevkaldmp 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 aldfvLSGDEeywqiqkqlaqpeqLSDSELAQLHGRFdeihGYsAPSKAaQLMAGlgfmehqlrldvsS-----FSGGWR 154
Cdd:cd03228 61 -----IDGVD--------------LRDLDLESLRKNI----AY-VPQDP-FLFSG-------------TireniLSGGQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 155 MRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDwlnayEGTLILISHDRDFLDAVtDHILHIEN 220
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDpetealiLEALRALAK-----GKTVIVIAHRLSTIRDA-DRIIVLDD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-498 |
2.79e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.08 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 26 PGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGW------------------------TVAHMAQEV----KALD 77
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWdevlkrfrgtelqnyfkklyngeiKVVHKPQYVdlipKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 78 MPALDFVLSGDEeywqiqkqlaqpeqlsdselaqlHGRFDEIhgysapskAAQLmaglgFMEHQLRLDVSSFSGGWRMRL 157
Cdd:PRK13409 178 GKVRELLKKVDE-----------------------RGKLDEV--------VERL-----GLENILDRDISELSGGELQRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 158 NLARTLMSRSDLLLLDEPTNHLDL-------DAILWLedwlnAYEGTLILISHDRDFLDAVTDHIlHIenqeltLY--TG 228
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHDLAVLDYLADNV-HI------AYgePG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 229 NYSTFEVTRSERLAQQQqafekqvearaHLQKFID----RFKakatkarqaqsrikqlekmqllapahvDTPFTFSFREP 304
Cdd:PRK13409 290 AYGVVSKPKGVRVGINE-----------YLKGYLPeenmRIR---------------------------PEPIEFEERPP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 305 T--KMSSPLLTLDQAEIGYPGKSIASKiSLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASelLNIGYFAQH 382
Cdd:PRK13409 332 RdeSERETLVEYPDLTKKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISYKPQY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 QMDALDGQASPMLqlsrladKQISEATLRSFLGS---FGFSGER-MDTPCESFSGGERARLALALIVWQRPNVLILDEPT 458
Cdd:PRK13409 409 IKPDYDGTVEDLL-------RSITDDLGSSYYKSeiiKPLQLERlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1348983253 459 NHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDDLL 498
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
300-508 |
3.34e-15 |
|
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: 75.26 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 300 SFREPTKMSSPLLTLDQAE--IGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ----RKASEL 373
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvtvrGRVSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 374 LNIGYFaqhqmdaLDGQAS---------PMLQLSRLADKQISEATLrsflgsfGFS--GERMDTPCESFSGGERARLALA 442
Cdd:cd03220 89 LGLGGG-------FNPELTgreniylngRLLGLSRKEIDEKIDEII-------EFSelGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 443 LIVWQRPNVLILDEPTNHLDLD--------MRHALSMAlqdfeGAVVLVSHERQLIASVCDDLLLVHAGRCTEF 508
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAfqekcqrrLRELLKQG-----KTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
272-525 |
3.92e-15 |
|
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: 78.64 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 272 ARQAQSRIKQLEKMQLLAPAHVDTPftfsfrEPTkmssPLLTLDQAEIGYPG--KSIASKISLQITPSSRIGLLGMNGAG 349
Cdd:COG4618 301 ARQAYRRLNELLAAVPAEPERMPLP------RPK----GRLSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 350 KSTLIKSLVG--------------DLALLNGQRKASellNIGYFAQH-------------QMDALDGQAspMLQLSRLAD 402
Cdd:COG4618 371 KSTLARLLVGvwpptagsvrldgaDLSQWDREELGR---HIGYLPQDvelfdgtiaeniaRFGDADPEK--VVAAAKLAG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 403 kqISEATLR------SFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF 476
Cdd:COG4618 446 --VHEMILRlpdgydTRIGEGGAR----------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 477 --EGA-VVLVSHERQLIAsVCDDLLLVHAGRCTEFsGDLQDYAKWLREARQQ 525
Cdd:COG4618 514 kaRGAtVVVITHRPSLLA-AVDKLLVLRDGRVQAF-GPRDEVLARLARPAAA 563
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
309-504 |
6.32e-15 |
|
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: 74.74 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 309 SPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGD--------LALLnGQRKASELL-----N 375
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygndVRLF-GERRGGEDVwelrkR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 376 IGYFAQHQMDALDGQASPmLQ--LS----------RLADKQISEAtlRSFLGSFGFSgERMDTPCESFSGGERAR--LAL 441
Cdd:COG1119 80 IGLVSPALQLRFPRDETV-LDvvLSgffdsiglyrEPTDEQRERA--RELLELLGLA-HLADRPFGTLSQGEQRRvlIAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 442 ALIvwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG--AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG1119 156 ALV--KDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
330-504 |
6.53e-15 |
|
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: 74.40 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ----RKASEL--LNIGYFAQH-----QMDALD---- 388
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditgLPPHEIarLGIGRTFQIprlfpELTVLEnvmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 389 ----GQASPMLQLSRLADKQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLD 464
Cdd:cd03219 99 aaqaRTGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1348983253 465 MRHALS---MALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03219 178 ETEELAeliRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
311-522 |
8.54e-15 |
|
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: 74.45 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKSIASK----ISLQITPSSRIGLLGMNGAGKSTLIKSLVGdLA-------LLNGQ-----RKASELL 374
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPvlkdVSLEVAPGESFGLVGESGSGKSTLLRALAG-LErpwsgevTFDGRpvtrrRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 NIGYFAQHQMDALDGQ-------ASPmLQLSRLADkqiSEATLRSFLGSFGFSGERMD-TPcESFSGGERARLAL--ALI 444
Cdd:COG1124 80 RVQMVFQDPYASLHPRhtvdrilAEP-LRIHGLPD---REERIAELLEQVGLPPSFLDrYP-HQLSGGQRQRVAIarALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 445 VwqRPNVLILDEPTNHLDLDMR----HALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTE-------FSGDLQ 513
Cdd:COG1124 155 L--EPELLLLDEPTSALDVSVQaeilNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEeltvadlLAGPKH 232
|
....*....
gi 1348983253 514 DYAKWLREA 522
Cdd:COG1124 233 PYTRELLAA 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
330-523 |
9.08e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.35 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGqrKASELL--------------NIGYFAQhqmdaldg 389
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptsgrvEVNG--RVSALLelgagfhpeltgreNIYLNGR-------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 390 qaspMLQLSRladKQISEAT--LRSF--LGSFgfsgerMDTPCESFSGGERARLALALIVWQRPNVLILDEptnhldldm 465
Cdd:COG1134 115 ----LLGLSR---KEIDEKFdeIVEFaeLGDF------IDQPVKTYSSGMRARLAFAVATAVDPDILLVDE--------- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 466 rhALS-----------MALQDF---EGAVVLVSHERQLIASVCDDLLLVHAGRCTEFsGDLQD----YAKWLREAR 523
Cdd:COG1134 173 --VLAvgdaafqkkclARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD-GDPEEviaaYEALLAGRE 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
312-504 |
9.40e-15 |
|
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: 73.71 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKAS---ELLNIGYFAQH 382
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpdsgeiLIDGRDVTGvppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 -----QMDALDGQASPM-LQLSRLADKQISEATLRSFLGSFGFSGERMDTpcesFSGGERARLALA--LIVwqRPNVLIL 454
Cdd:cd03259 81 yalfpHLTVAENIAFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALAraLAR--EPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 455 DEPTNHLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03259 155 DEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-181 |
1.21e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS-------LTRPSGWTVAH----M 69
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvrlngrpLAAWSPWELARrravL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 70 AQEVK-ALDMPALDFVLSGdeeywqiqkqlAQPEQLSDSELAQLhgrfdeihgysapskAAQLMA--GLGFMEHQlrlDV 146
Cdd:COG4559 81 PQHSSlAFPFTVEEVVALG-----------RAPHGSSAAQDRQI---------------VREALAlvGLAHLAGR---SY 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1348983253 147 SSFSGGWRMRLNLARTL-------MSRSDLLLLDEPTNHLDL 181
Cdd:COG4559 132 QTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
312-504 |
1.47e-14 |
|
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: 77.18 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIA--SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ----------RKasel 373
Cdd:COG2274 474 IELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEptsgriLIDGIdlrqidpaslRR---- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 374 lNIGYFAQHQM-------DALdgqaspmlqlsRLADKQISEATLRSFLGSFGFSGE------RMDTPC----ESFSGGER 436
Cdd:COG2274 550 -QIGVVLQDVFlfsgtirENI-----------TLGDPDATDEEIIEAARLAGLHDFiealpmGYDTVVgeggSNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 437 ARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASvCDDLLLVHAGR 504
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGR 686
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-215 |
2.07e-14 |
|
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: 72.92 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKALDM-PALDfvlsgdeeywqiqkqlA 99
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYcPQFD----------------A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 100 QPEQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLdVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTnhL 179
Cdd:cd03263 86 LFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKR-ARTLSGGMKRKLSLAIALIGGPSVLLLDEPT--S 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1348983253 180 DLDA----ILWleDWLNAYEG--TLILISHDRDFLDAVTDHI 215
Cdd:cd03263 163 GLDPasrrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
2.46e-14 |
|
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: 72.54 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKA----SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT--------------RPS 62
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrrlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 63 GWTVAHMAQEVkaldMPALDFVLSgdeeywqIQKQLAqpeqlsdsELAQLHGRfdeIHGYSAPSKAA-QLMAGLGFMEHQ 141
Cdd:cd03257 81 RKEIQMVFQDP----MSSLNPRMT-------IGEQIA--------EPLRIHGK---LSKKEARKEAVlLLLVGVGLPEEV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 142 LRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDwlnAYEGTLILISHDRDFLDAVTDH 214
Cdd:cd03257 139 LNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqaqiLDLLKKLQE---ELGLTLLFITHDLGVVAKIADR 215
|
..
gi 1348983253 215 IL 216
Cdd:cd03257 216 VA 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-214 |
2.50e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 12 GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKALD-MPaldfvlsgdee 90
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDsLP----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 91 ywqiqkqlaqpeqLSDSELAQLhGRFDEI-----HGYSAPSKAAQLMAGLGfMEHQLRLDVSSFSGGWRMRLNLARTLMS 165
Cdd:NF040873 72 -------------LTVRDLVAM-GRWARRglwrrLTRDDRAAVDDALERVG-LADLAGRQLGELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 166 RSDLLLLDEPTNHLDLDAILWLEDWLNAYEG---TLILISHDrdfLDAVTDH 214
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD---LELVRRA 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-204 |
2.57e-14 |
|
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: 75.86 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 12 GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPS-----------GWTVAHMAQEVKALDMPA 80
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevRRRVSVCAQDAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDEEywqiqkqlAQPEQLSDS-ELAQLHGRFDEIhgysaPSKAAQLMAGLGfmehqlrldvSSFSGGWRMRLNL 159
Cdd:TIGR02868 426 RENLRLARPD--------ATDEELWAAlERVGLADWLRAL-----PDGLDTVLGEGG----------ARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 160 ARTLMSRSDLLLLDEPTNHLDLDAIL-WLEDWLNAYEG-TLILISHD 204
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-507 |
2.58e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 324 KSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASEllNIGYFAQH--QMDALD---------GQAS 392
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDifQIDAIKlrkevgmvfQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 PMLQLS----------------RLADKQISEATLRSfLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDE 456
Cdd:PRK14246 101 PFPHLSiydniayplkshgikeKREIKKIVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 457 PTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
308-491 |
4.28e-14 |
|
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: 75.40 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 308 SSPLLTLDQAEIGYPGKSIA-SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQR-----KASELLN 375
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPAlRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDptegsiAVNGVPladadADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 376 IGYFAQH------------QMDALDGQASPMLQLSRLADKQISEATLRSFLGS-FGFSGERMdtpcesfSGGERARLALA 442
Cdd:TIGR02857 398 IAWVPQHpflfagtiaeniRLARPDASDAEIREALERAGLDEFVAALPQGLDTpIGEGGAGL-------SGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 443 LIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIA 491
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAA 521
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
4.33e-14 |
|
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: 72.15 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELgadegsltRPSGWTVAHMAQEVkaldmpal 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLL--------RPDSGEVLIDGEDI-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 dFVLSGDEEY-----WQIQKQ-----------------LAQPEQLSDSELAQLhgrfdeihgysAPSKAAqlMAGLGFME 139
Cdd:cd03261 65 -SGLSEAELYrlrrrMGMLFQsgalfdsltvfenvafpLREHTRLSEEEIREI-----------VLEKLE--AVGLRGAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 140 HQLrldVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLNAyegTLILISHDRDFLDAVT 212
Cdd:cd03261 131 DLY---PAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDTAFAIA 204
|
....
gi 1348983253 213 DHIL 216
Cdd:cd03261 205 DRIA 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-223 |
5.12e-14 |
|
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: 70.32 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGG--RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALDMp 79
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG--------LLRPTSGRVRLDGADISQWDP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 aldfvlsgdEEYWQIQKQLAQPEQLSDSELAqlhgrfDEIhgysapskaaqlmaglgfmehqlrldvssFSGGWRMRLNL 159
Cdd:cd03246 72 ---------NELGDHVGYLPQDDELFSGSIA------ENI-----------------------------LSGGQRQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LNAYEGTLILISHDRDFLDAVtDHILHIENQEL 223
Cdd:cd03246 108 ARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
330-504 |
5.93e-14 |
|
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: 71.37 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASELL-NIGY-FAQHQ----MDALDG 389
Cdd:cd03255 23 VSLSIEKGEFVAIVGPSGSGKSTLLNILGGldrptsgevrvdgtDISKLSEKELAAFRRrHIGFvFQSFNllpdLTALEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 390 QASPMLqLSRLADKQIsEATLRSFLGSFGFsGERMDTPCESFSGGERARLALA--LIvwQRPNVLILDEPTNHLDLDMRH 467
Cdd:cd03255 103 VELPLL-LAGVPKKER-RERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIAraLA--NDPKIILADEPTGNLDSETGK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1348983253 468 A---LSMALQDFEG-AVVLVSHERQLiASVCDDLLLVHAGR 504
Cdd:cd03255 178 EvmeLLRELNKEAGtTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
312-504 |
6.60e-14 |
|
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: 70.29 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASELlNIG 377
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleepdsgsilidgeDLTDLEDELPPLRR-RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 378 Y-FAQHQ----MDALDGQASPMlqlsrladkqiseatlrsflgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVL 452
Cdd:cd03229 80 MvFQDFAlfphLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 453 ILDEPTNHLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
330-507 |
6.75e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.66 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKS------------LVGDLALLNGQRKASEL-LNIGYFAQH-----QMDALDGQA 391
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCinkleeitsgdlIVDGLKVNDPKVDERLIrQEAGMVFQQfylfpHLTALENVM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 SPMLQLsRLADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:PRK09493 100 FGPLRV-RGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1348983253 472 ALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK09493 178 VMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-498 |
6.91e-14 |
|
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: 74.82 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 30 VGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWtvahmaQEVkaldmpaLDFvLSGDE--EYWQ--IQKQL--AQPEQ 103
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPSW------DEV-------LKR-FRGTElqDYFKklANGEIkvAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 104 LSD----------SEL---AQLHGRFDEIhgysapskaAQLMAglgfMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLL 170
Cdd:COG1245 168 YVDlipkvfkgtvRELlekVDERGKLDEL---------AEKLG----LENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 171 LLDEPTNHLDL-------DAILWLedwlnAYEG-TLILISHDRDFLDAVTDHIlHIenqeltLY--TGNYSTFEVTRSER 240
Cdd:COG1245 235 FFDEPSSYLDIyqrlnvaRLIREL-----AEEGkYVLVVEHDLAILDYLADYV-HI------LYgePGVYGVVSKPKSVR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 241 LAQQQqafekqvearahlqkFID--------RFKakatkarqaqsrikqlekmqllapahvDTPFTFSFREPT--KMSSP 310
Cdd:COG1245 303 VGINQ---------------YLDgylpeenvRIR---------------------------DEPIEFEVHAPRreKEEET 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKSIASKiSLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGqrKASELLNIGYFAQH-------- 382
Cdd:COG1245 341 LVEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQYispdydgt 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 QMDALDGQASPM-------------LQLSRLADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRP 449
Cdd:COG1245 418 VEEFLRSANTDDfgssyykteiikpLGLEKLLDKNVKD-----------------------LSGGELQRVAIAACLSRDA 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 450 NVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLV-SHERQLIASVCDDLL 498
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFaenRGKTAMVvDHDIYLIDYISDRLM 527
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-219 |
7.45e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRR-GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVK----- 74
Cdd:COG4178 362 ALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYlplgt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 75 ---ALDMPaldfvlsgdeeywqiqkqlAQPEQLSDSELAQ-LHgrfdeihgysapskaaqlMAGLGFMEHqlRLDVSS-- 148
Cdd:COG4178 442 lreALLYP-------------------ATAEAFSDAELREaLE------------------AVGLGHLAE--RLDEEAdw 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 149 ---FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNA--YEGTLILISHdRDFLDAVTDHILHIE 219
Cdd:COG4178 483 dqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-462 |
7.89e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.28 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQEvkaldmpa 80
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQS-QFSHITRLSFE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 ldfvlsgdeeywQIQKQLAQPEQ------LSDSElaQLHGRFD-EI--HGYSAPSKAAQLMAGLGfMEHQLRLDVSSFSG 151
Cdd:PRK10938 74 ------------QLQKLVSDEWQrnntdmLSPGE--DDTGRTTaEIiqDEVKDPARCEQLAQQFG-ITALLDRRFKYLST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEG---TLILISHDRDFLDAVTDHILHIENQELTLyTG 228
Cdd:PRK10938 139 GETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLAE-TG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 229 nystfevTRSERLAQqqqafekqvearahlqkfidrfkakatkarqaqSRIKQLEKMQLLAPAHVDTPFTFSFREPTKMS 308
Cdd:PRK10938 218 -------EREEILQQ---------------------------------ALVAQLAHSEQLEGVQLPEPDEPSARHALPAN 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 309 SPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGD--------LALLNGQRKASELL-----N 375
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndLTLFGRRRGSGETIwdikkH 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 376 IGYFAQ--HqmdaLDGQASPMLQ---LSRLAD-----KQISEAT---LRSFLGSFGFSGERMDTPCESFSGGERaRLAL- 441
Cdd:PRK10938 338 IGYVSSslH----LDYRVSTSVRnviLSGFFDsigiyQAVSDRQqklAQQWLDILGIDKRTADAPFHSLSWGQQ-RLALi 412
|
490 500
....*....|....*....|...
gi 1348983253 442 --ALIvwQRPNVLILDEPTNHLD 462
Cdd:PRK10938 413 vrALV--KHPTLLILDEPLQGLD 433
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
328-507 |
9.44e-14 |
|
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: 71.07 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 328 SKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNG--QRKASEllNIGYFAQH-----QMDA 386
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGkeLRKARR--RIGMIFQHfnllsSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 LDGQASPmLQLSRLADKQISEATLRsFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLD---- 462
Cdd:cd03258 100 FENVALP-LEIAGVPKAEIEERVLE-LLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDpett 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1348983253 463 ---LDMRHALSmalQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:cd03258 177 qsiLALLRDIN---RELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-220 |
1.09e-13 |
|
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: 70.70 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGG--RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS---------------LTRPSGW 64
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtdirqldpadLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 65 tvahMAQEVK----------ALDMPALDfvlsgDEEYwqiqkqLAQPEQLSDSELAQLHGrfdeiHGYsapskaaQLMAG 134
Cdd:cd03245 83 ----VPQDVTlfygtlrdniTLGAPLAD-----DERI------LRAAELAGVTDFVNKHP-----NGL-------DLQIG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 135 LGFMehqlrldvsSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEG--TLILISHDRDFLDAVt 212
Cdd:cd03245 136 ERGR---------GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLV- 205
|
....*...
gi 1348983253 213 DHILHIEN 220
Cdd:cd03245 206 DRIIVMDS 213
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
10-216 |
1.10e-13 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 70.88 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 10 RRGGRVL--FQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS-----------LTRPSGW--------TVAH 68
Cdd:TIGR02324 15 QQGGVRLpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRilvrhegawvdLAQASPRevlevrrkTIGY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 69 MAQEVKALD-MPALDFVlsgdeeywqiqkqlAQPEQLSDSELAQlhgrfdeihgysAPSKAAQLMAGLGFMEHQLRLDVS 147
Cdd:TIGR02324 95 VSQFLRVIPrVSALEVV--------------AEPLLERGVPREA------------ARARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLNAYEGTLILISHDRDFLDAVTDHIL 216
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVM 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
313-504 |
1.14e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.36 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 313 TLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL-------VGDlALLNGQRKASelLNIGYFAQ---- 381
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsEGE-ILLDAQPLES--WSSKAFARkvay 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 382 --HQMDALDGQASPML----------QLSRL--ADKQISEATLrSFLGSFGFSGERMDtpceSFSGGERARLALALIVWQ 447
Cdd:PRK10575 90 lpQQLPAAEGMTVRELvaigrypwhgALGRFgaADREKVEEAI-SLVGLKPLAHRLVD----SLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 448 RPNVLILDEPTNHLD-------LDMRHALSmalQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK10575 165 DSRCLLLDEPTSALDiahqvdvLALVHRLS---QERGLTVIAVLHDINMAARYCDYLVALRGGE 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
312-504 |
1.14e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.94 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIasKISLQITPSSRIGLLGMNGAGKSTLIkSLV--------GDLaLLNGQ---------RKASELl 374
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLL-NLIagflppdsGRI-LWNGQdltalppaeRPVSML- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 nigyFAQH----QMDALDGQA---SPMLQLSRLADKQISEATLRSFLGSFGfsgERMdtpCESFSGGERARLALA-LIVW 446
Cdd:COG3840 77 ----FQENnlfpHLTVAQNIGlglRPGLKLTAEQRAQVEQALERVGLAGLL---DRL---PGQLSGGQRQRVALArCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 447 QRPnVLILDEPTNHLDLDMRH---ALSMALQDFEGAVVL-VSHERQLIASVCDDLLLVHAGR 504
Cdd:COG3840 147 KRP-ILLLDEPFSALDPALRQemlDLVDELCRERGLTVLmVTHDPEDAARIADRVLLVADGR 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
330-504 |
1.25e-13 |
|
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: 70.48 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQ---RKASELL-NIGYFAQHQM--DALDGQASpMLQL 397
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkptsgrATVAGHdvvREPREVRrRIGIVFQDLSvdDELTGWEN-LYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 SRLADKQISEATLR--SFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHAL----SM 471
Cdd:cd03265 98 ARLYGVPGAERRERidELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVweyiEK 176
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 472 ALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03265 177 LKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-223 |
1.70e-13 |
|
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: 70.21 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKA----SMQIHPGWKVGLTGVNGAGKSTLFAALlgelgadeGSLTRPSGWTVAHMAQEVKALD 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQAlkgvSLSIEKGEFVAIVGPSGSGKSTLLNIL--------GGLDRPTSGEVRVDGTDISKLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 78 MPALDFVLsgdeeywqiQKQLA---Q-----PEqLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGfMEHQLRLDVSSF 149
Cdd:cd03255 73 EKELAAFR---------RRHIGfvfQsfnllPD-LTALENVELPLLLAGVPKKERRERAEELLERVG-LGDRLNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLNAYEG-TLILISHDRDFLDAvTDHILHIENQEL 223
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkEVMELLRELNKEAGtTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
330-505 |
2.07e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA-----LLNGQR----KASELLNI-GYFAQHQMdaldgQASPM----- 394
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPlsdwSAAELARHrAYLSQQQS-----PPFAMpvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 395 --LQLSRLADKQISEATLRSFLGSFGFSgERMDTPCESFSGGE--RARLALALI-VWQRPN----VLILDEPTNHLDLDM 465
Cdd:COG4138 90 laLHQPAGASSEAVEQLLAQLAEALGLE-DKLSRPLTQLSGGEwqRVRLAAVLLqVWPTINpegqLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1348983253 466 RHALSMALQDF---EGAVVLVSHERQLIASVCDDLLLVHAGRC 505
Cdd:COG4138 169 QAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
312-492 |
2.36e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 69.70 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIA-SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQR----KASELL----NI 376
Cdd:COG2884 2 IRFENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEErptsgqVLVNGQDlsrlKRREIPylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 377 GY-FAQHQ----MDALDGQASPmLQLSRLADKQIsEATLRSFLGSFGFSGeRMDTPCESFSGGERARLAL--ALIVwqRP 449
Cdd:COG2884 82 GVvFQDFRllpdRTVYENVALP-LRVTGKSRKEI-RRRVREVLDLVGLSD-KAKALPHELSGGEQQRVAIarALVN--RP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1348983253 450 NVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIAS 492
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
324-507 |
2.51e-13 |
|
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: 70.60 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 324 KSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASELLNIGYFAQHQMDALDG 389
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlekpaqgtvsfrgqDLYQLDRKQRRAFRRDVQLVFQDSPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 390 QAS-------PMLQLSRLaDKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:TIGR02769 104 RMTvrqiigePLRHLTSL-DESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1348983253 463 LDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:TIGR02769 183 MVLQAVILELLrklqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
310-506 |
2.92e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 310 PLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQrkaselLNIGYFAQHQMDA--L 387
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT------VLVAGDDVEALSAraA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 388 DGQASPMLQLSRLA----DKQISEATLRSFLGSFGFSGER-----------------MDTPCESFSGGERARLALALIVW 446
Cdd:PRK09536 76 SRRVASVPQDTSLSfefdVRQVVEMGRTPHRSRFDTWTETdraaveramertgvaqfADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 447 QRPNVLILDEPTNHLDLDmrHA-----LSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCT 506
Cdd:PRK09536 156 QATPVLLLDEPTASLDIN--HQvrtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-514 |
3.16e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.91 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQItPSSRI-GLLGMNGAGKSTLIKSLVGDLA------LLNGQRKASELLN-IGYFAQH-----QMDALDgqaspmlQ 396
Cdd:COG4152 20 VSFTV-PKGEIfGLLGPNGAGKTTTIRIILGILApdsgevLWDGEPLDPEDRRrIGYLPEErglypKMKVGE-------Q 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 397 LSRLA-----DKQISEATLRSFLGSFGFsGERMDTPCESFSGGE--RARLALALIvwQRPNVLILDEPTNHLDLDMRHAL 469
Cdd:COG4152 92 LVYLArlkglSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNqqKVQLIAALL--HDPELLILDEPFSGLDPVNVELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1348983253 470 SMALQDF--EGA-VVLVSHERQLIASVCDDLLLVHAGRcTEFSGDLQD 514
Cdd:COG4152 169 KDVIRELaaKGTtVIFSSHQMELVEELCDRIVIINKGR-KVLSGSVDE 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-504 |
3.80e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 302 REPTKMSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL-------VGDLALLNGQRKASELL 374
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtspdAGKITVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 ---NIGYFAQhqMDALDGQASPMLQL------SRLADKQIsEATLRSFLgSFGFSGERMDTPCESFSGGERARLALALIV 445
Cdd:PRK13536 112 araRIGVVPQ--FDNLDLEFTVRENLlvfgryFGMSTREI-EAVIPSLL-EFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 446 WQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLArgkTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
4.57e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKaldmpa 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSgdeeywqiqkqlaqpeqLSDSELAQLHGRfdeihgysapSKAAQLMAGLGFME--HQLRLDVSSFSGGWRMRLN 158
Cdd:PRK09544 78 LDTTLP-----------------LTVNRFLRLRPG----------TKKEDILPALKRVQagHLIDAPMQKLSGGETQRVL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTL----ILISHDRDFLDAVTDHIL 216
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVL 192
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
312-504 |
6.14e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLvgdlALLNGQRKASELLN---IGYFAQHQMD--- 385
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF----ARLLTPQSGTVFLGdkpISMLSSRQLArrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 ALDGQA-----------------SPMLQL-SRLA--DKQISE-ATLRSFLGSFGfsgermDTPCESFSGGERARLALALI 444
Cdd:PRK11231 79 ALLPQHhltpegitvrelvaygrSPWLSLwGRLSaeDNARVNqAMEQTRINHLA------DRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 445 VWQRPNVLILDEPTNHLDLD-----MRhaLSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINhqvelMR--LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
307-504 |
6.92e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNG----------QRKASELLNI 376
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgepvpSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 377 GYFAQhqMDALDgqaspmlqlsrlADKQISEaTLRSFLGSFGFSG-----------------ERMDTPCESFSGGERARL 439
Cdd:PRK13537 83 GVVPQ--FDNLD------------PDFTVRE-NLLVFGRYFGLSAaaaralvppllefakleNKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA---VVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgktILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-222 |
7.77e-13 |
|
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: 67.63 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 32 LTGVNGAGKSTLFAALLGEL-GadEGSLTRPSGWTVAHMAQEVKALDMPALDFVLSGDEEYwQIQKQLAQPEQLsdselA 110
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALtG--ELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKY-TITRSLAILENV-----I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 111 QLH-GRFDEIhgysapskaaqLMAGLGFMehqlrldvssfSGGWRM------RLNLARTLMSRSDLLLLDEPTNHLDLDA 183
Cdd:cd03240 99 FCHqGESNWP-----------LLDMRGRC-----------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 184 I-LWLEDWLNAYEGT----LILISHDRDFLDAVtDHILHIENQE 222
Cdd:cd03240 157 IeESLAEIIEERKSQknfqLIVITHDEELVDAA-DHIYRVEKDG 199
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-220 |
8.16e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.45 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtRPSGWTV---AHMAQE----VK 74
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-SLCGEPVpsrARHARQrvgvVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 75 ALDMPALDFVLSgdeeywqiqkqlaqpeqlsdsELAQLHGRFdeiHGYSAPSKAAQLMAGLGFMEHQLRLD--VSSFSGG 152
Cdd:PRK13537 87 QFDNLDPDFTVR---------------------ENLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADakVGELSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 153 WRMRLNLARTLMSRSDLLLLDEPTNHLDLDA--ILW--LEDWLnAYEGTLILISHDRDFLDAVTDHILHIEN 220
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
340-514 |
8.73e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 340 IGLLGMNGAGKSTLIKSLVGDLALlNGQRKAS------ELLNIgyfAQHQMDALDGQ------ASPMLQLS---RLAD-- 402
Cdd:PRK09473 45 LGIVGESGSGKSQTAFALMGLLAA-NGRIGGSatfngrEILNL---PEKELNKLRAEqismifQDPMTSLNpymRVGEql 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 403 -------KQISEATlrSFLGSFGF--------SGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRh 467
Cdd:PRK09473 121 mevlmlhKGMSKAE--AFEESVRMldavkmpeARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ- 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 468 ALSMAL-----QDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFsGDLQD 514
Cdd:PRK09473 198 AQIMTLlnelkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY-GNARD 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
330-508 |
8.88e-13 |
|
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: 67.82 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKasellnigyfaqhqMDALDGQASPMLQL-SRLA----DKQ 404
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE--------------IDGIDISTIPLEDLrSSLTiipqDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 405 ISEATLRSFLGSFG-------FSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL-QDF 476
Cdd:cd03369 93 LFSGTIRSNLDPFDeysdeeiYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEF 172
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 477 EGAVVL-VSHERQLIASvCDDLLLVHAGRCTEF 508
Cdd:cd03369 173 TNSTILtIAHRLRTIID-YDKILVMDAGEVKEY 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-243 |
1.25e-12 |
|
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: 68.08 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSltrpsgwtvahmaqevkaldmpa 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE----------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 ldfVLSGDEEYWQiqkqlaqpeqLSDSELAQLHGRF-----------------------DEIHGYSaPSKAAQL------ 131
Cdd:COG1127 62 ---ILVDGQDITG----------LSEKELYELRRRIgmlfqggalfdsltvfenvafplREHTDLS-EAEIRELvlekle 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 132 MAGLGFMEHQLrldVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD------LDA-ILWLEDWLNAyegTLILISHD 204
Cdd:COG1127 128 LVGLPGAADKM---PSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDElIRELRDELGL---TSVVVTHD 201
|
250 260 270
....*....|....*....|....*....|....*....
gi 1348983253 205 RDFLDAVTDHILHIENQELtLYTGNYSTFEVTRSERLAQ 243
Cdd:COG1127 202 LDSAFAIADRVAVLADGKI-IAEGTPEELLASDDPWVRQ 239
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-204 |
1.33e-12 |
|
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: 67.59 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELgaDEGSLTRPSGwTVAHMAQEVKALDMPAL 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLN--DLIPGAPDEG-EVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 D--------------FVLSgdeeywqIQKQLAQPEQLSDSelaQLHGRFDEIhgysapSKAAQLMAGLgFMEHQLRLDVS 147
Cdd:cd03260 78 ElrrrvgmvfqkpnpFPGS-------IYDNVAYGLRLHGI---KLKEELDER------VEEALRKAAL-WDEVKDRLHAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLN--AYEGTLILISHD 204
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
311-505 |
1.33e-12 |
|
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: 71.58 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKS--IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKA---SELLNIGYFAQH--- 382
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagkSILTNISDVHQNmgy 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 --QMDALD----GQASPML--QLSRLADKQISEATLRSfLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:TIGR01257 2017 cpQFDAIDdlltGREHLYLyaRLRGVPAEEIEKVANWS-IQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 455 DEPTNHLDLDMRHAL---SMALQDFEGAVVLVSHERQLIASVCDDLLLVHAG--RC 505
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLwntIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGafQC 2150
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-504 |
1.38e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNG---QRKASELL-NIGY-FAQHQ--------MDALD-- 388
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILvptsgeVRVLGyvpFKRRKEFArRIGVvFGQRSqlwwdlpaIDSFRll 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 389 ---------------GQASPMLQLSRLADKQISEATLrsflgsfgfsGERMdtpcesfsggeRARLALALIvwQRPNVLI 453
Cdd:COG4586 121 kaiyripdaeykkrlDELVELLDLGELLDTPVRQLSL----------GQRM-----------RCELAAALL--HRPKILF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 454 LDEPTNHLDLDMRHalsmALQDF-------EGA-VVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG4586 178 LDEPTIGLDVVSKE----AIREFlkeynreRGTtILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-180 |
1.39e-12 |
|
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: 71.09 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 12 GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLgELGADEGSLTRPS-GWTVAHMAQEVKALD-MPALDFVLSGde 89
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvSWNSVTLQTWRKAFGvIPQKVFIFSG-- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 90 eywQIQKQLAQPEQLSDSELAQLHgrfDEIhgySAPSKAAQLMAGLGFmehQLRLDVSSFSGGWRMRLNLARTLMSRSDL 169
Cdd:TIGR01271 1307 ---TFRKNLDPYEQWSDEEIWKVA---EEV---GLKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|.
gi 1348983253 170 LLLDEPTNHLD 180
Cdd:TIGR01271 1375 LLLDEPSAHLD 1385
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
321-491 |
1.67e-12 |
|
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: 67.05 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIA-SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGD------LALLNGQ------RKASELL--NIGYFAQ---- 381
Cdd:cd03292 10 YPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEelptsgTIRVNGQdvsdlrGRAIPYLrrKIGVVFQdfrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 382 -HQMDALDGQASPMLQLS---RLADKQISEAtlrsfLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:cd03292 90 lPDRNVYENVAFALEVTGvppREIRKRVPAA-----LELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1348983253 458 TNHLDLDMRHALSMALQDFE--GAVVLVS-HERQLIA 491
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVD 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-180 |
1.98e-12 |
|
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: 66.83 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWkVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQEVKAL----- 76
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRI-DGQDVLKQPQKLRRRigylp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 -------DMPALDFVlsgdeEYwqiqkqlaqpeqlsdseLAQLHGrfdeIHGYSAPSKAAQLMAGLGFMEHQLRLdVSSF 149
Cdd:cd03264 79 qefgvypNFTVREFL-----DY-----------------IAWLKG----IPSKEVKARVDEVLELVNLGDRAKKK-IGSL 131
|
170 180 190
....*....|....*....|....*....|.
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03264 132 SGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
330-504 |
2.28e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.63 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGdL-------ALLNGQRKASEL----LNIGYFAQH-----QMD-------A 386
Cdd:COG1118 21 VSLEIASGELVALLGPSGSGKTTLLRIIAG-LetpdsgrIVLNGRDLFTNLppreRRVGFVFQHyalfpHMTvaeniafG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 LDGQASP-------------MLQLSRLADK---QISeatlrsflgsfgfsgermdtpcesfsGGERARLALA--LIVwqR 448
Cdd:COG1118 100 LRVRPPSkaeirarveelleLVQLEGLADRypsQLS--------------------------GGQRQRVALAraLAV--E 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 449 PNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG1118 152 PEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
329-504 |
2.87e-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: 66.55 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 329 KISLQiTPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ-----------RKASEL----LNIGYFAQH-----QMDALD 388
Cdd:cd03297 16 KIDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtvlfdsRKKINLppqqRKIGLVFQQyalfpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 389 GQASPMLQLSRLADKQISEATLRSF-LGSFGFSgermdtPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH 467
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLgLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1348983253 468 ALSMAL----QDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03297 169 QLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
330-504 |
2.89e-12 |
|
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: 66.99 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQR----KASELL---------NIGYF----------- 379
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRDitglPPHRIArlgiartfqNPRLFpeltvlenvlv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 380 -AQHQMDALDGQASPMLQLSRLADKQISEATLRsFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPT 458
Cdd:COG0411 103 aAHARLGRGLLAALLRLPRARREEREARERAEE-LLERVGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 459 NHLDLDMRHALS---MALQDFEG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG0411 181 AGLNPEETEELAeliRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
322-507 |
2.90e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASELLNIGYFAQHQMDAL 387
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlespsqgnvswrgePLAKLNRAQRKAFRRDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 388 DGQ-------ASPMLQLSRLaDKQISEATLRSFLGSFGFSGERMDTPCESFSGG--ERARLALALIVwqRPNVLILDEPT 458
Cdd:PRK10419 103 NPRktvreiiREPLRHLLSL-DKAERLARASEMLRAVDLDDSVLDKRPPQLSGGqlQRVCLARALAV--EPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 459 NHLDLdMRHALSMAL-----QDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK10419 180 SNLDL-VLQAGVIRLlkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-216 |
3.15e-12 |
|
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: 66.69 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 5 DQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS-------LTRPSGWTVAHMA-----QE 72
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgedITGLPPHEIARLGigrtfQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 73 VKAL-DMPALDFVLSGdeeywqiqkqlaqpEQLSDSELAQLHGRFDEIHgySAPSKAAQLMAGLGfMEHQLRLDVSSFSG 151
Cdd:cd03219 84 PRLFpELTVLENVMVA--------------AQARTGSGLLLARARREER--EARERAEELLERVG-LADLADRPAGELSY 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 152 GWRMRLNLARTLMSRSDLLLLDEPT---NHLDLDAIL-WLEDwLNAYEGTLILISHDRDFLDAVTDHIL 216
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAeLIRE-LRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-220 |
4.64e-12 |
|
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: 65.57 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSgwTVAHMAQEvkaldmPaldFVLSG--------DEEYw 92
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQE------P---WIQNGtirenilfGKPF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 93 qiqkqlaqpeqlsDSElaqlhgRFDEIhgysapSKAAQLMAGLGFMEHQLRLDV----SSFSGGWRMRLNLARTLMSRSD 168
Cdd:cd03250 93 -------------DEE------RYEKV------IKACALEPDLEILPDGDLTEIgekgINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 169 LLLLDEP--------TNHLDLDAIlwLEDWLNayEGTLILISHDRDFLDAVtDHILHIEN 220
Cdd:cd03250 148 IYLLDDPlsavdahvGRHIFENCI--LGLLLN--NKTRILVTHQLQLLPHA-DQIVVLDN 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
312-504 |
5.40e-12 |
|
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: 66.05 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASK-ISLQITPSSRIGLLGMNGAGKSTLIKSLVG------------DLALLNGQRKASELL--NI 376
Cdd:cd03256 1 IEVENLSKTYPNGKKALKdVSLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 377 GYFAQH-----QMDALD-------GQAS---PMLQLSRLADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLAL 441
Cdd:cd03256 81 GMIFQQfnlieRLSVLEnvlsgrlGRRStwrSLFGLFPKEEKQRALAALER-VGLLDKAYQRADQ----LSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 442 ALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVS-HERQLIASVCDDLLLVHAGR 504
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIVGLKDGR 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
326-491 |
7.12e-12 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 65.45 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 326 IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG-DLA-----LLNGQR-------KASELLNI--GYFAQ--HQM---D 385
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGlDNPtsgevLFNGQSlsklssnERAKLRNKklGFIYQfhHLLpdfT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 ALDGQASPMLqlsrLADKQISEATLRSF--LGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD- 462
Cdd:TIGR02211 100 ALENVAMPLL----IGKKSVKEAKERAYemLEKVGL-EHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDn 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1348983253 463 ------LDMRHALSmalQDFEGAVVLVSHERQLIA 491
Cdd:TIGR02211 175 nnakiiFDLMLELN---RELNTSFLVVTHDLELAK 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
319-508 |
8.99e-12 |
|
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: 65.28 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 319 IGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELL------------------NIGYFA 380
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLldgkdiydldvdvlelrrRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QH----QMDALDGQASPmLQLSRLADKQISEATLRSFLGSFGFSGERMD-TPCESFSGGERARLALA--LIVwqRPNVLI 453
Cdd:cd03260 88 QKpnpfPGSIYDNVAYG-LRLHGIKLKEELDERVEEALRKAALWDEVKDrLHALGLSGGQQQRLCLAraLAN--EPEVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 454 LDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVCDDLLLVHAGRCTEF 508
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-224 |
1.06e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 65.06 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGG-----RVLfQKASMQIHPGWKVGLTGVNGAGKSTLFAALlgelgadeGSLTRPSGWTVAHMAQEVka 75
Cdd:COG1136 4 LLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNIL--------GGLDRPTSGEVLIDGQDI-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 76 ldmpaldfvlsgdeeywqiqkqlaqpEQLSDSELAQLHGR--------------------------FDEIHGYSAPSKAA 129
Cdd:COG1136 73 --------------------------SSLSERELARLRRRhigfvfqffnllpeltalenvalpllLAGVSRKERRERAR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 130 QLMAGLGfMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLNAYEG-TLILISHDR 205
Cdd:COG1136 127 ELLERVG-LGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSktgEEVLELLRELNRELGtTIVMVTHDP 205
|
250
....*....|....*....
gi 1348983253 206 DfLDAVTDHILHIENQELT 224
Cdd:COG1136 206 E-LAARADRVIRLRDGRIV 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
322-510 |
1.29e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.84 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASK----ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKASELLN-------IGYFAQHqm 384
Cdd:PRK13637 14 EGTPFEKKaldnVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKptsgkiIIDGVDITDKKVKlsdirkkVGLVFQY-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 daldgqasPMLQLSR---------------LADKQISEATLRSfLGSFGFSGERM--DTPCEsFSGGERARLALALIVWQ 447
Cdd:PRK13637 92 --------PEYQLFEetiekdiafgpinlgLSEEEIENRVKRA-MNIVGLDYEDYkdKSPFE-LSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 448 RPNVLILDEPTNHLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDDLLLVHAGRCtEFSG 510
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKC-ELQG 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
307-514 |
1.35e-11 |
|
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: 65.00 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQR----KASEL--- 373
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgeiLVDGQDitglSEKELyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 374 -LNIGY-FaqhQMDAL-------DGQASPMLQLSRLADKQISEATLRSfLGSFGFSG--ERMdtPCEsFSGGERARLALA 442
Cdd:COG1127 81 rRRIGMlF---QGGALfdsltvfENVAFPLREHTDLSEAEIRELVLEK-LELVGLPGaaDKM--PSE-LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 443 --LIVwqRPNVLILDEPT-----------NHLDLDMRHALSMalqdfegAVVLVSHERQLIASVCDDLLLVHAGRCtEFS 509
Cdd:COG1127 154 raLAL--DPEILLYDEPTagldpitsaviDELIRELRDELGL-------TSVVVTHDLDSAFAIADRVAVLADGKI-IAE 223
|
....*
gi 1348983253 510 GDLQD 514
Cdd:COG1127 224 GTPEE 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
321-504 |
1.40e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 64.99 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASelLNIGYFAQhqmda 386
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGlvrpdagkilidgqDITHLPMHERAR--LGIGYLPQ----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 ldgQAS------------PMLQLSRLADKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:TIGR04406 84 ---EASifrkltveenimAVLEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 455 DEPTNHLD----LDMRHaLSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:TIGR04406 160 DEPFAGVDpiavGDIKK-IIKHLKERGIGVLITDHNVRETLDICDRAYIISDGK 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-184 |
1.74e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTL---FAALL----GELGADEGSLTRPSGWTVAHMAQEV 73
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLppaaGTIKLDGGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 74 KALDmPAldfvLSGDE--EYWqiqkqlaqpeqlsdselAQLHGRFDeihgySAPSKAAQLMaGLGFMEHqlrLDVSSFSG 151
Cdd:PRK13539 82 NAMK-PA----LTVAEnlEFW-----------------AAFLGGEE-----LDIAAALEAV-GLAPLAH---LPFGYLSA 130
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAI 184
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-228 |
1.83e-11 |
|
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: 64.28 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 18 QKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT----RPSGWTVAHMAQ--------EVKALDMPALD-FV 84
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglVPWKRRKKFLRRigvvfgqkTQLWWDLPVIDsFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 85 LsgdeeywqiqkqLAQPEQLSDSELAQlhgRFDEIhgysapskaAQLMAglgfMEHQLRLDVSSFSGGWRMRLNLARTLM 164
Cdd:cd03267 118 L------------LAAIYDLPPARFKK---RLDEL---------SELLD----LEELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 165 SRSDLLLLDEPTNHLDLDAILWLEDWLNAY----EGTLILISHDRDFLDAVTDHILHIENQELtLYTG 228
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
330-485 |
1.83e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA-----LLNGQR----KASELLNI-GYFAQHQMDALDGQASPMLQLSR 399
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiQFAGQPleawSAAELARHrAYLSQQQTPPFAMPVFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 400 --LADKQISEATLRSFLGSFGFsGERMDTPCESFSGGE--RARLALA-LIVWQRPN----VLILDEPTNHLDLDMRHALS 470
Cdd:PRK03695 95 pdKTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGEwqRVRLAAVvLQVWPDINpagqLLLLDEPMNSLDVAQQAALD 173
|
170
....*....|....*...
gi 1348983253 471 MALQDFE---GAVVLVSH 485
Cdd:PRK03695 174 RLLSELCqqgIAVVMSSH 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-220 |
2.18e-11 |
|
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: 62.97 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQEVKALDmPAL 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-DGEDLTDLEDELPPLR-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 DFVlsgdeeywqiqkqlaqpeqlsdselaqlhgrFDEIHGYSAPSKAAQLMAGLgfmehqlrldvssfSGGWRMRLNLAR 161
Cdd:cd03229 79 GMV-------------------------------FQDFALFPHLTVLENIALGL--------------SGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 162 TLMSRSDLLLLDEPTNHLDL----DAILWLEDwLNAYEG-TLILISHDRDFLDAVTDHILHIEN 220
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPitrrEVRALLKS-LQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-223 |
2.24e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 3 QFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSL---TRP-SGWTVAHMAQEVKALdm 78
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldAQPlESWSSKAFARKVAYL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 paldfvlsgdeeywqiQKQLAQPEQLSDSELAQLhGRFdEIHG----YSAPSKA----AQLMAGLGFMEHQLrldVSSFS 150
Cdd:PRK10575 91 ----------------PQQLPAAEGMTVRELVAI-GRY-PWHGalgrFGAADREkveeAISLVGLKPLAHRL---VDSLS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLNAYEG-TLILISHDRDFLDAVTDHILHIENQEL 223
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
325-507 |
2.29e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 325 SIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNG-QRKASELLNIGYFAQHQM----- 384
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGlddgssgevslvgqPLHQMDEeARAKLRAKHVGFVFQSFMliptl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 DALDGQASPMLqLSRLADKQiSEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD-- 462
Cdd:PRK10584 104 NALENVELPAL-LRGESSRQ-SRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrq 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 463 -----LDMRHALSmalQDFEGAVVLVSHERQLiASVCDDLLLVHAGRCTE 507
Cdd:PRK10584 181 tgdkiADLLFSLN---REHGTTLILVTHDLQL-AARCDRRLRLVNGQLQE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
2.39e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 64.34 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLR----RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSL-------TRPSGwTVAHM 69
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkpvTGPGP-DRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 70 AQEvKALdMP---ALD---FVLsgdeeywqiqkqlaqpeqlsdselaqlhgrfdEIHGYSAPSKAAQLMA-----GL-GF 137
Cdd:COG1116 86 FQE-PAL-LPwltVLDnvaLGL--------------------------------ELRGVPKAERRERAREllelvGLaGF 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 138 ME---HQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAIL------WLEDWLNAYEGTLILISHDRD 206
Cdd:COG1116 132 EDaypHQL-------SGGMRQRVAIARALANDPEVLLMDEPFGA--LDALTrerlqdELLRLWQETGKTVLFVTHDVD 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
321-506 |
3.00e-11 |
|
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: 62.06 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKA----SELLNIGYFAQHQMdaldgq 390
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKpdsgeiLVDGKEVSfaspRDARRAGIAMVYQL------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 391 aspmlqlsrladkqiseatlrsflgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:cd03216 84 -----------------------------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 1348983253 471 MALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGRCT 506
Cdd:cd03216 123 KVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-203 |
3.27e-11 |
|
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: 62.06 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqevkaldmpal 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 dfvlsgdeeywqiqkqlaqpeqlsdselaqLHGRfdEIHGYSaPSKAAQlmAGLGfMEHQLrldvssfSGGWRMRLNLAR 161
Cdd:cd03216 59 ------------------------------VDGK--EVSFAS-PRDARR--AGIA-MVYQL-------SVGERQMVEIAR 95
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1348983253 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLN--AYEG-TLILISH 203
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRrlRAQGvAVIFISH 140
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-220 |
3.38e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.27 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGAD---EGSLtRPSGWTVAHMAQEVKALD 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV-LLNGRRLTALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 78 M---PALDFvlsgdeEYWQIQKQLAqpeqlsdselaqlhgrFDEIHGYSAPSKAAQLM-----AGLGFMEHQlrlDVSSF 149
Cdd:COG4136 80 IlfqDDLLF------PHLSVGENLA----------------FALPPTIGRAQRRARVEqaleeAGLAGFADR---DPATL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDW----LNAYEGTLILISHDRDflDA-VTDHILHIEN 220
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE--DApAAGRVLDLGN 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-216 |
3.54e-11 |
|
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: 63.74 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRG-GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALDMPA 80
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG--------LVEPTSGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDEEYWQiqkQLAQPEQLSDSElAQLHGRFDEIHGYSAPS---------KAAQLMAGLGfMEHQLRLDVSSFSG 151
Cdd:cd03256 73 LRQLRRQIGMIFQ---QFNLIERLSVLE-NVLSGRLGRRSTWRSLFglfpkeekqRALAALERVG-LLDKAYQRADQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLNAYEGTLILIS-HDRDFLDAVTDHIL 216
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASsrqVMDLLKRINREEGITVIVSlHQVDLAREYADRIV 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-224 |
3.91e-11 |
|
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: 63.22 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLR---RGGRV-LFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKAL 76
Cdd:COG4181 8 IIELRGLTKTvgtGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG--------LDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DmpaldfvlsgdEEywqiqkQLA-----------QPEQLSDS-----------ELAqlhGRFDeihgysAPSKAAQLMA- 133
Cdd:COG4181 80 D-----------ED------ARArlrarhvgfvfQSFQLLPTltalenvmlplELA---GRRD------ARARARALLEr 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 134 -GLGFMEH----QLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLNAYEG-TLILISHD 204
Cdd:COG4181 134 vGLGHRLDhypaQL-------SGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHD 206
|
250 260
....*....|....*....|
gi 1348983253 205 RDfLDAVTDHILHIENQELT 224
Cdd:COG4181 207 PA-LAARCDRVLRLRAGRLV 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-204 |
5.28e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 63.32 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLrrGGRVlfQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGAdEGSLT---RP-SGWTVAHMA------- 70
Cdd:COG4138 1 LQLNDVAV--AGRL--GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILlngRPlSDWSAAELArhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 71 -QEVKALDMPALdfvlsgdeEYWQIQKQLAQPEQLSDSELAQLHGRFdeihgysapskaaQLMAGLGFMEHQLrldvssf 149
Cdd:COG4138 76 qQQSPPFAMPVF--------QYLALHQPAGASSEAVEQLLAQLAEAL-------------GLEDKLSRPLTQL------- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 150 SGGWRMRLNLARTLM-------SRSDLLLLDEPTNHLDLDAILWLEDWLNAY---EGTLILISHD 204
Cdd:COG4138 128 SGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
330-504 |
7.30e-11 |
|
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: 62.45 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVG------------------DLAllngQRKASELLN-----IGYFAQH---- 382
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsilvrhdggwvDLA----QASPREILAlrrrtIGYVSQFlrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 -QMDALDGQASPMLQLSrlADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERAR--LALALIVwqRPNVLILDEPTN 459
Cdd:COG4778 106 pRVSALDVVAEPLLERG--VDREEARARARELLARLNLPERLWDLPPATFSGGEQQRvnIARGFIA--DPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1348983253 460 HLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG4778 182 SLDAANRAVVVELIEEAkaRGtAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
321-457 |
8.26e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 62.35 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ--------RKAseLLNIGYFAQHqmda 386
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKpdsgriFLDGEdithlpmhKRA--RLGIGYLPQE---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 ldgqAS------------PMLQLSRLADKQIsEATLRSFLGSFGFSGERmDTPCESFSGGERARL--ALALIVwqRPNVL 452
Cdd:COG1137 87 ----ASifrkltvednilAVLELRKLSKKER-EERLEELLEEFGITHLR-KSKAYSLSGGERRRVeiARALAT--NPKFI 158
|
....*
gi 1348983253 453 ILDEP 457
Cdd:COG1137 159 LLDEP 163
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-204 |
1.07e-10 |
|
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: 61.72 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKA----SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS-------LTRPSGwTVAHMA 70
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEvlvdgepVTGPGP-DRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 71 QEvKALdMP---ALDFVLSGDEeywqIQKqlaqpeqLSDSELAQlhgrfdeihgysapsKAAQLMA--GL-GFME---HQ 141
Cdd:cd03293 80 QQ-DAL-LPwltVLDNVALGLE----LQG-------VPKAEARE---------------RAEELLElvGLsGFENaypHQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 142 LrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLNAYEGTLILISHD 204
Cdd:cd03293 132 L-------SGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
312-491 |
1.26e-10 |
|
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: 60.25 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYP-GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHqmdaldgq 390
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 391 asPMLQLSRLADkQIS---EATLrsflgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH 467
Cdd:cd03223 73 --PYLPLGTLRE-QLIypwDDVL---------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|....
gi 1348983253 468 ALSMALQDFEGAVVLVSHERQLIA 491
Cdd:cd03223 129 RLYQLLKELGITVISVGHRPSLWK 152
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-188 |
1.40e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.71 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT-----------RPSGWTVAHM 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 70 AQEVkaldmpALDFVLSGDeeywQIQKQLAQPEQlsdselaqlhGRFDEiHGYSAPSKAAQLMAGLGFMEHQLRlDVSSF 149
Cdd:PRK09536 83 PQDT------SLSFEFDVR----QVVEMGRTPHR----------SRFDT-WTETDRAAVERAMERTGVAQFADR-PVTSL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD-AILWLE 188
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLE 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-504 |
1.43e-10 |
|
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: 64.08 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLG----------------ELGADEGSLTRPSGWTVAHmaQEVKAL-DMPALDF 83
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASNIRDTERAGIVIIH--QELTLVpELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 84 VLSGDEeywqiqkqLAQPEQLSDSELAQLhgrfdeihgysapsKAAQLMAGLGFMEHQLRLDVSSFSGGWRMRLNLARTL 163
Cdd:TIGR02633 99 IFLGNE--------ITLPGGRMAYNAMYL--------------RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 164 MSRSDLLLLDEPTNHLDLDAILWLEDW---LNAYEGTLILISHDRDFLDAVTDHILHIENQEltlytgnystfevtrser 240
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ------------------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 241 laqqqqafekqvearaHLqkfidrfkakATKARQAQSR---IKQL--EKMQLLAPahvdtpftfsfREPTKMSSPLLTLD 315
Cdd:TIGR02633 219 ----------------HV----------ATKDMSTMSEddiITMMvgREITSLYP-----------HEPHEIGDVILEAR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 316 QA---EIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGdlaLLNGQRKASELLNigyfaQHQMDALDGQAS 392
Cdd:TIGR02633 262 NLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG---AYPGKFEGNVFIN-----GKPVDIRNPAQA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 -----PMLQLSRLAD---------KQISEATLRSF-----------LGSFGFSGERM-------DTPCESFSGGERARLA 440
Cdd:TIGR02633 334 iragiAMVPEDRKRHgivpilgvgKNITLSVLKSFcfkmridaaaeLQIIGSAIQRLkvktaspFLPIGRLSGGNQQKAV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 441 LALIVWQRPNVLILDEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKyeiYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.92e-10 |
|
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: 61.44 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVS----LRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKAL 76
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING--------LERPTSGSVLVDGTDLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DMPALDfvlsgdeeywQIQKQLA---QPEQLSDSELAqlhgrFD------EIHGYS---APSKAAQLMAGLGfMEHQLRL 144
Cdd:cd03258 73 SGKELR----------KARRRIGmifQHFNLLSSRTV-----FEnvalplEIAGVPkaeIEERVLELLELVG-LEDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 145 DVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLNAYEG-TLILISHDRDFLDAVTDHILHIEN 220
Cdd:cd03258 137 YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEK 216
|
...
gi 1348983253 221 QEL 223
Cdd:cd03258 217 GEV 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-511 |
1.93e-10 |
|
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: 63.55 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKS-TLFAA--LLGE----------------LGADEGSLTRPSGWTVAHMAQEvkalDMPAL 81
Cdd:COG4172 30 SFDIAAGETLALVGESGSGKSvTALSIlrLLPDpaahpsgsilfdgqdlLGLSERELRRIRGNRIAMIFQE----PMTSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 DFVLSgdeeywqIQKQLAqpeqlsdsELAQLHGRfdeIHGYSAPSKAAQLMAGLGFMEHQLRLDvsSF----SGGWRMRL 157
Cdd:COG4172 106 NPLHT-------IGKQIA--------EVLRLHRG---LSGAAARARALELLERVGIPDPERRLD--AYphqlSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 158 NLARTLMSRSDLLLLDEPTNHLD--LDA-ILWLEDWLNAYEGT-LILISHD----RDFLDAVTdhilhienqeltlytgn 229
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDvtVQAqILDLLKDLQRELGMaLLLITHDlgvvRRFADRVA----------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 230 ystfeVTRSERLaqqqqafekqVEArAHLQKFIDRFKAKATKarqaqsrikqlekmQLLAPAHVDTPftfsfREPTKMSS 309
Cdd:COG4172 229 -----VMRQGEI----------VEQ-GPTAELFAAPQHPYTR--------------KLLAAEPRGDP-----RPVPPDAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 310 PLLTLDQAEIGYPGKS-----------IASKISLQITPSSRIGLLGMNGAGKSTLikslvGdLALLNGQRKASELLnigy 378
Cdd:COG4172 274 PLLEARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTL-----G-LALLRLIPSEGEIR---- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 379 FAQHQMDALDGQA-------------------SPML---------------QLSRLA-DKQISEAtlrsfLGSFGFSGER 423
Cdd:COG4172 344 FDGQDLDGLSRRAlrplrrrmqvvfqdpfgslSPRMtvgqiiaeglrvhgpGLSAAErRARVAEA-----LEEVGLDPAA 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 424 MDT-PCEsFSGGERARLALA--LIVwqRPNVLILDEPTNHLDLDMRH---ALSMALQDFEG-AVVLVSHERQLIASVCDD 496
Cdd:COG4172 419 RHRyPHE-FSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDVSVQAqilDLLRDLQREHGlAYLFISHDLAVVRALAHR 495
|
570
....*....|....*
gi 1348983253 497 LLLVHAGRCTEfSGD 511
Cdd:COG4172 496 VMVMKDGKVVE-QGP 509
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
330-504 |
2.06e-10 |
|
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: 61.20 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVG------DLALLNGQRKASELL---NIGYFAQH-----QMDALDGQAS--P 393
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGlerpdsGTILFGGEDATDVPVqerNVGFVFQHyalfrHMTVFDNVAFglR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 394 MLQLSRLADKQISEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL 473
Cdd:cd03296 101 VKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1348983253 474 QDFEGAV----VLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03296 180 RRLHDELhvttVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
321-457 |
2.14e-10 |
|
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: 61.02 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ--------RKASelLNIGYFAQhqmda 386
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpdsgkiLLDGQditklpmhKRAR--LGIGYLPQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 ldgQASPMLQLS-----------RLADKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILD 455
Cdd:cd03218 83 ---EASIFRKLTveenilavleiRGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 1348983253 456 EP 457
Cdd:cd03218 159 EP 160
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-203 |
2.16e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.54 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT-----RPSGWTVAHMAQEVkal 76
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpVPARARLARARIGV--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 dMPALDFVlsgDEEYwQIQKQLAqpeqlsdselaqLHGRFdeiHGYSAPSKAAQLMAGLGF--MEHQLRLDVSSFSGGWR 154
Cdd:PRK13536 119 -VPQFDNL---DLEF-TVRENLL------------VFGRY---FGMSTREIEAVIPSLLEFarLESKADARVSDLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDA--ILW--LEDWLnAYEGTLILISH 203
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLL-ARGKTILLTTH 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-176 |
2.62e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT----RPSGWTVAHMAQEVKAL 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 dMPALDFVLSgdeeYWQIQKQLAQPEQLSDSElaQLHGRFDEIHGysapskaaqLMAGLGFMEHQlrlDVSSFSGGWRMR 156
Cdd:PRK11614 85 -VPEGRRVFS----RMTVEENLAMGGFFAERD--QFQERIKWVYE---------LFPRLHERRIQ---RAGTMSGGEQQM 145
|
170 180
....*....|....*....|
gi 1348983253 157 LNLARTLMSRSDLLLLDEPT 176
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPS 165
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
312-511 |
3.30e-10 |
|
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: 60.53 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ---RKASELLN---IGYF 379
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPprsgsiRFDGRditGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 380 AQHQMdaLDGQASPM--LQLSRLA-DKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDE 456
Cdd:cd03224 81 PEGRR--IFPELTVEenLLLGAYArRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 457 PTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGRcTEFSGD 511
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELrdEGvTILLVEQNARFALEIADRAYVLERGR-VVLEGT 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
140-519 |
3.83e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 140 HQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLNAyegTLILISHDRDFLDAVT 212
Cdd:PRK15134 155 HQL-------SGGERQRVMIAMALLTRPELLIADEPTTALDvsvqaqiLQLLRELQQELNM---GLLFITHNLSIVRKLA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 213 DHIlhienqeltlytgnystfEVTRSERLAQQQQAfekqvearahlqkfidrfKAKATKARQAQSRikqlekmQLLAPAH 292
Cdd:PRK15134 225 DRV------------------AVMQNGRCVEQNRA------------------ATLFSAPTHPYTQ-------KLLNSEP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 293 VDTPFTFSfreptKMSSPLLTLDQAEIGYPGK-----------SIASKISLQITPSSRIGLLGMNGAGKSTlikslvGDL 361
Cdd:PRK15134 262 SGDPVPLP-----EPASPLLDVEQLQVAFPIRkgilkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKST------TGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 362 ALLNGQRKASELLNIGY----FAQHQMDALDGQASPMLQ------LSRLADKQISEATLR----------------SFLG 415
Cdd:PRK15134 331 ALLRLINSQGEIWFDGQplhnLNRRQLLPVRHRIQVVFQdpnsslNPRLNVLQIIEEGLRvhqptlsaaqreqqviAVME 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 416 SFGFSGE-RMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQ-DFEGAVVLVSHERQLI 490
Cdd:PRK15134 411 EVGLDPEtRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAqilALLKSLQqKHQLAYLFISHDLHVV 489
|
410 420 430
....*....|....*....|....*....|....*.
gi 1348983253 491 ASVCDDLL------LVHAGRC-TEFSGDLQDYAKWL 519
Cdd:PRK15134 490 RALCHQVIvlrqgeVVEQGDCeRVFAAPQQEYTRQL 525
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-181 |
3.90e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADegslTRPSGWTV----AHMAQEVKAL 76
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG----GAPRGARVtgdvTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DMPALDFVLSgdeeywqIQKQLAQPE-QLSDSELAQLhGRFDEIHGYSAPSKAAQLMA----GLGFMEHQLRLDVSSFSG 151
Cdd:PRK13547 77 DAPRLARLRA-------VLPQAAQPAfAFSAREIVLL-GRYPHARRAGALTHRDGEIAwqalALAGATALVGRDVTTLSG 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 1348983253 152 GWRMRLNLARTL---------MSRSDLLLLDEPTNHLDL 181
Cdd:PRK13547 149 GELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
316-511 |
4.74e-10 |
|
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: 59.46 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 316 QAEIGypGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA--------LLNGQrkasELLNI--------GYF 379
Cdd:cd03217 7 HVSVG--GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevtegeiLFKGE----DITDLppeerarlGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 380 AQHQmdaldgqaSPMlqlsrladkQISEATLRSFLGSFGfsgermdtpcESFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:cd03217 81 LAFQ--------YPP---------EIPGVKNADFLRYVN----------EGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 460 HLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDDLLLV-HAGRCTEfSGD 511
Cdd:cd03217 134 GLDIDALRLVAEVINKLreEGkSVLIITHYQRLLDYIKPDRVHVlYDGRIVK-SGD 188
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
312-507 |
4.95e-10 |
|
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: 60.19 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKS--IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNgqrKASELLN 375
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfyvpengrvlvdghDLALAD---PAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 376 IGYFAQHQM---------DALDGQASPM---LQLSRLADKQisEATLRSFLGSFGFSGERmdtpCESFSGGERARLALAL 443
Cdd:cd03252 78 VGVVLQENVlfnrsirdnIALADPGMSMervIEAAKLAGAH--DFISELPEGYDTIVGEQ----GAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-225 |
5.86e-10 |
|
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: 58.86 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGG--RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSltrpsgwtvahmaqevkaldmp 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 aldfVLSGDEEYWQIQKQLAQpeqlSDSELAQlhgrfdEIHGYSApskaaQLMAGLGfmehqlrldvSSFSGGWRMRLNL 159
Cdd:cd03247 59 ----ITLDGVPVSDLEKALSS----LISVLNQ------RPYLFDT-----TLRNNLG----------RRFSGGERQRLAL 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 160 ARTLMSRSDLLLLDEPTNHLD-LDAILWLEDWLNAYEG-TLILISHDRDFLDAVtDHILHIENQELTL 225
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKDkTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
312-488 |
5.95e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.42 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA---------LLNGQR---KASELLNIGYF 379
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsasgevLLNGRRltaLPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 380 AQhqmDAL------DGQ----ASPMlQLSRLADKQISEATLRSfLGSFGFsGERmdTPcESFSGGERARLALALIVWQRP 449
Cdd:COG4136 82 FQ---DDLlfphlsVGEnlafALPP-TIGRAQRRARVEQALEE-AGLAGF-ADR--DP-ATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1348983253 450 NVLILDEPTNHLDLDMRHALSM----ALQDFEGAVVLVSHERQ 488
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREfvfeQIRQRGIPALLVTHDEE 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-203 |
6.15e-10 |
|
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: 59.29 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 5 DQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSL---TRPSGWTVAHMAQEVKAL-DMPA 80
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwnGTPLAEQRDEPHENILYLgHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDE--EYWQiqkQLAQPEQLSDSE-LAQlhgrfdeihgysapskaaqlmAGLGFMEHqlrLDVSSFSGGWRMRL 157
Cdd:TIGR01189 84 LKPELSALEnlHFWA---AIHGGAQRTIEDaLAA---------------------VGLTGFED---LPAAQLSAGQQRRL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1348983253 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY---EGTLILISH 203
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-226 |
6.41e-10 |
|
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: 59.22 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGsltrpsgwtvahmaqEVKALDMPaL 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSG---------------EVLFDGKP-L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 DFVLSGDEEYWQIQKQLAQPEQLSDS--ELAQLHGRFDEihgySAPSKAAQLMAGLGFMEHQLRlDVSSFSGGWRMRLNL 159
Cdd:cd03269 65 DIAARNRIGYLPEERGLYPKMKVIDQlvYLAQLKGLKKE----EARRRIDEWLERLELSEYANK-RVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEG---TLILISHDRDFLDAVTDHILHIENQELTLY 226
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
7.22e-10 |
|
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: 59.46 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQEVKALDMPAL 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 DFVLsgdeeyWQ---IQKQLAQPeqlsdseLAQLHGRFDEIHgysapSKAAQLMAGLGfMEHQLRLDVSSFSGGWRMRLN 158
Cdd:cd03259 80 DYAL------FPhltVAENIAFG-------LKLRGVPKAEIR-----ARVRELLELVG-LEGLLNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 159 LARTLMSRSDLLLLDEPTNHldLDAIL------WLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQEL 223
Cdd:cd03259 141 LARALAREPSLLLLDEPLSA--LDAKLreelreELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-221 |
7.96e-10 |
|
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: 59.73 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 30 VGLTGVNGAGKSTLFAALLGELGADEGSLTRPsGWTVAHMAQEVKA-LDMPALDFVLS-----GDEEYWQ--IQKQLaQP 101
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKAdYEGTVRDLLSSitkdfYTHPYFKteIAKPL-QI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 102 EQLSDSELAQLhgrfdeihgysapskaaqlmaglgfmehqlrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:cd03237 106 EQILDREVPEL-------------------------------------SGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 182 DAILWLEDWLNAY----EGTLILISHDRDFLDAVTDHILHIENQ 221
Cdd:cd03237 149 EQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-498 |
8.74e-10 |
|
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: 59.73 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 334 ITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQrKASELLNIGYFAQH------------QMDALDGQ----------A 391
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-IEIELDTVSYKPQYikadyegtvrdlLSSITKDFythpyfkteiA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 SPmLQLSRLADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03237 101 KP-LQIEQILDREVPE-----------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|.
gi 1348983253 472 ALQDF----EGAVVLVSHERQLIASVCDDLL 498
Cdd:cd03237 157 VIRRFaennEKTAFVVEHDIIMIDYLADRLI 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
338-506 |
9.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 338 SRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQRKASELLN-----IGYFAQHQMDALdgqASPMLQ-------LSR 399
Cdd:PRK13652 31 SRIAVIGPNGAGKSTLFRHFNGILkptsgsVLIRGEPITKENIRevrkfVGLVFQNPDDQI---FSPTVEqdiafgpINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 400 LADKQISEATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG- 478
Cdd:PRK13652 108 GLDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEt 186
|
170 180 190
....*....|....*....|....*....|.
gi 1348983253 479 ---AVVLVSHERQLIASVCDDLLLVHAGRCT 506
Cdd:PRK13652 187 ygmTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
324-500 |
1.11e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 324 KSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGdlALLNGQRKASELLNIGYFAQHQ--MDALDGQASPMLQLSRLA 401
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVAGCVDVPDNQFGREAslIDAIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 402 DKQISEATLrsFLGSFgfsgermdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF----E 477
Cdd:COG2401 121 AVGLSDAVL--WLRRF-----------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarraG 187
|
170 180
....*....|....*....|...
gi 1348983253 478 GAVVLVSHERQLIASVCDDLLLV 500
Cdd:COG2401 188 ITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
321-504 |
1.26e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKASEllNIGYFAQH---- 382
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivprdagniiiddeDISLLPLHARARR--GIGYLPQEasif 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 -QMDALDGQASpMLQLSRLADKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:PRK10895 91 rRLSVYDNLMA-VLQIRDDLSAEQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 462 D----LDMRHALSMaLQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK10895 169 DpisvIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
431-507 |
1.27e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.98 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 431 FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQ-DFEGAVVLVSHERQLIASVCDDLLLVHAGRCT 506
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnLMMDLQqELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
.
gi 1348983253 507 E 507
Cdd:PRK11308 235 E 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-220 |
1.42e-09 |
|
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: 57.55 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRG-GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKaldMPA 80
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPY---LPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFvlsgdeeywqiQKQLAQPeqlSDSELaqlhgrfdeihgysapskaaqlmaglgfmehqlrldvssfSGGWRMRLNLA 160
Cdd:cd03223 78 GTL-----------REQLIYP---WDDVL----------------------------------------SGGEQQRLAFA 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISHdRDFLDAVTDHILHIEN 220
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
328-500 |
1.45e-09 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 58.56 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 328 SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ------------RKAS--ELLN-----IGYFAQH-----Q 383
Cdd:TIGR02324 25 KNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRilvrhegawvdlAQASprEVLEvrrktIGYVSQFlrvipR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 384 MDALDGQASPMLQLSrlADKQISEATLRSFLGSFGFSgERM-DTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:TIGR02324 105 VSALEVVAEPLLERG--VPREAARARARELLARLNIP-ERLwHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1348983253 463 LDMRHALSMALQDFEG---AVVLVSHERQLIASVCDDLLLV 500
Cdd:TIGR02324 182 AANRQVVVELIAEAKArgaALIGIFHDEEVRELVADRVMDV 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
305-504 |
1.47e-09 |
|
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: 58.60 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 305 TKMSSPLLTLDQAEIGYPGKS----IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG-DLA-----LLNGQ------- 367
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPtsgtvRLAGQdlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 368 ------RKAsellNIGYFAQH-----QMDALDGQASPmLQLSRLADkqiSEATLRSFLGSFGFsGERMD-TPCEsFSGGE 435
Cdd:COG4181 82 dararlRAR----HVGFVFQSfqllpTLTALENVMLP-LELAGRRD---ARARARALLERVGL-GHRLDhYPAQ-LSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQDFEGA-VVLVSHERQLiASVCDDLLLVHAGR 504
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRERGTtLVLVTHDPAL-AARCDRVLRLRAGR 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
330-504 |
1.65e-09 |
|
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: 57.86 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASEllNIGYFAQhqmdaldgqaSPMLQlsrladkqisEAT 409
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQ----------EPWIQ----------NGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 410 LRS---FlgsfgfsGERMDTP--------CE---------------------SFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:cd03250 82 IREnilF-------GKPFDEEryekvikaCAlepdleilpdgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 458 TNHLDLD-----MRHALSMALQDfEGAVVLVSHERQLIASvCDDLLLVHAGR 504
Cdd:cd03250 155 LSAVDAHvgrhiFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
268-507 |
1.68e-09 |
|
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: 60.91 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 268 KATKARQAQSRIKQLekmqLLapahVDTPFTFSfREPTKMSSPLLTLDQAEIGYP---GKSIASKISLQITPSSRIGLLG 344
Cdd:TIGR01193 437 KLQAARVANNRLNEV----YL----VDSEFINK-KKRTELNNLNGDIVINDVSYSygyGSNILSDISLTIKMNSKTTIVG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 345 MNGAGKSTLIKSLVGDLA------LLNG----QRKASELLN-IGYFAQHQ-------MDALDGQASPMLQLSRLaDKQIS 406
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQarsgeiLLNGfslkDIDRHTLRQfINYLPQEPyifsgsiLENLLLGAKENVSQDEI-WAACE 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 407 EATLRSFLGSF--GFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS---MALQDfeGAVV 481
Cdd:TIGR01193 587 IAEIKDDIENMplGY-QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVnnlLNLQD--KTII 663
|
250 260
....*....|....*....|....*.
gi 1348983253 482 LVSHeRQLIASVCDDLLLVHAGRCTE 507
Cdd:TIGR01193 664 FVAH-RLSVAKQSDKIIVLDHGKIIE 688
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
315-463 |
1.78e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 315 DQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNG---------QRKASELL--NIGYFAQHQ 383
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiQHYASKEVarRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 384 MDALDGQAS-----------PMLQLSRLADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVL 452
Cdd:PRK10253 91 TTPGDITVQelvargryphqPLFTRWRKEDEEAVTKAMQA-TGITHLADQSVDT----LSGGQRQRAWIAMVLAQETAIM 165
|
170
....*....|.
gi 1348983253 453 ILDEPTNHLDL 463
Cdd:PRK10253 166 LLDEPTTWLDI 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
322-503 |
2.44e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASK----ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQMDALDGQASPMLQL 397
Cdd:PRK13643 13 PNSPFASRalfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 SrlaDKQISEATLRSFLG----SFGFSGERMD-------------------TPCEsFSGGERARLALALIVWQRPNVLIL 454
Cdd:PRK13643 93 P---ESQLFEETVLKDVAfgpqNFGIPKEKAEkiaaeklemvgladefwekSPFE-LSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 455 DEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAG 503
Cdd:PRK13643 169 DEPTAGLDPKARiemMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-180 |
2.92e-09 |
|
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: 58.01 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR-RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtRPSGwtvahmaQEVKALDMPA 80
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-LIDG-------QDIREVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 L---------DFVLSGDEEYWQIQ--KQLAQPEQLSDS-ELAQLHgrfDEI----HGYSApskaaqlMAGlgfmEHQLRL 144
Cdd:cd03253 73 LrraigvvpqDTVLFNDTIGYNIRygRPDATDEEVIEAaKAAQIH---DKImrfpDGYDT-------IVG----ERGLKL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 1348983253 145 dvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03253 139 -----SGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-248 |
3.04e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 13 GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELgADEGSLTrPSGwtvahmaQEVKALDMpaldfvlsgdeEYW 92
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLK-ING-------IELRELDP-----------ESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 93 QiqKQLA---QPEQLSDSELAQ--LHGRFD----EIHGYSAPSKAA----QLMAGLgfmEHQLRLDVSSFSGGWRMRLNL 159
Cdd:PRK11174 422 R--KHLSwvgQNPQLPHGTLRDnvLLGNPDasdeQLQQALENAWVSeflpLLPQGL---DTPIGDQAAGLSVGQAQRLAL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILISHDRDFLDAVtDHILHIENQELtLYTGNYSTfevtr 237
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDLAQW-DQIWVMQDGQI-VQQGDYAE----- 569
|
250
....*....|.
gi 1348983253 238 serLAQQQQAF 248
Cdd:PRK11174 570 ---LSQAGGLF 577
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-180 |
3.19e-09 |
|
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: 57.50 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR--RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrPSGWTVAHMAQEV--KALD 77
Cdd:cd03244 3 IEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL-IDGVDISKIGLHDlrSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 78 MPALD-FVLSGDeeywqIQKQLAQPEQLSDSELAQ-LhgrfdeihgysapsKAAQLMAGLGFMEHQLRLDVSS----FSG 151
Cdd:cd03244 82 IIPQDpVLFSGT-----IRSNLDPFGEYSDEELWQaL--------------ERVGLKEFVESLPGGLDTVVEEggenLSV 142
|
170 180
....*....|....*....|....*....
gi 1348983253 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVD 171
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
329-509 |
3.27e-09 |
|
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: 58.97 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 329 KISLQITPSSRIGLLGMNGAGKSTLIKSLVG-----------DLALLNGQRKASEL----LNIGYFAQhqmdaldgQASP 393
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGltrpdegeivlNGRTLFDSRKGIFLppekRRIGYVFQ--------EARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 394 MLQLS------------RLADKQISEATLRSFLGSfgfsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:TIGR02142 87 FPHLSvrgnlrygmkraRPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 462 DLDMRHALSMALQ----DFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFS 509
Cdd:TIGR02142 163 DDPRKYEILPYLErlhaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAG 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
330-504 |
3.35e-09 |
|
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: 57.15 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSL------------VGDLALLNGQRKASEL-LNIGYFAQH-----QMDALDGQA 391
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdsgtiiIDGLKLTDDKKNINELrQKVGMVFQQfnlfpHLTVLENIT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 SPMLQLSRLADKQiSEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03262 99 LAPIKVKGMSKAE-AEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLD 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1348983253 472 ALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03262 177 VMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
311-504 |
3.37e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL---ALLNGQRKASELlnigyfaqhqmdAL 387
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDV------------TL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 388 DGQ---ASPMLQLSRLAdKQISEATLRSF---------LGSFGFS----------GERMDTPCE-------------SFS 432
Cdd:PRK13547 69 NGEplaAIDAPRLARLR-AVLPQAAQPAFafsareivlLGRYPHArragalthrdGEIAWQALAlagatalvgrdvtTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 433 GGERARLALALIVWQ---------RPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDDLLL 499
Cdd:PRK13547 148 GGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAARHADRIAM 227
|
....*
gi 1348983253 500 VHAGR 504
Cdd:PRK13547 228 LADGA 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
307-504 |
3.43e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 58.96 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRkASELL------ 374
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpdsgriLLDGRD-VTGLPpekrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 -----------------NIGYFAQHQ-----------MDALDgqaspMLQLSRLADKQISEatlrsfLgsfgfsgermdt 426
Cdd:COG3842 80 gmvfqdyalfphltvaeNVAFGLRMRgvpkaeirarvAELLE-----LVGLEGLADRYPHQ------L------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 427 pcesfSGGERARLALA--LIVwqRPNVLILDEPTNHLDL----DMRHALSMALQDFEGAVVLVSHErQLIA-SVCDDLLL 499
Cdd:COG3842 137 -----SGGQQQRVALAraLAP--EPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHD-QEEAlALADRIAV 208
|
....*
gi 1348983253 500 VHAGR 504
Cdd:COG3842 209 MNDGR 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-216 |
3.47e-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: 59.80 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 23 QIHPGWKVGLTGVNGAGKSTlFAALL-GELGADEGSLtrPSGWTVAHMAQEVKA-LDMPALDFVLSGDEEYWQ---IQKQ 97
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTT-FAKILaGVLKPDEGEV--DEDLKISYKPQYISPdYDGTVEEFLRSANTDDFGssyYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 98 LAQPEQLsdselaqlhgrfdeihgysapskaaqlmaglgfmEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTN 177
Cdd:COG1245 439 IIKPLGL----------------------------------EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1348983253 178 HLDldailwLEDWLNA----------YEGTLILISHDRDFLDAVTDHIL 216
Cdd:COG1245 485 HLD------VEQRLAVakairrfaenRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-180 |
3.56e-09 |
|
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: 58.33 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 12 GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKALD-MPALDFVLSGdee 90
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGvIPQKVFIFSG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 91 ywQIQKQLAQPEQLSDSELAQLHgrfDEIhgySAPSKAAQLMAGLGFmehQLRLDVSSFSGGWRMRLNLARTLMSRSDLL 170
Cdd:cd03289 92 --TFRKNLDPYGKWSDEEIWKVA---EEV---GLKSVIEQFPGQLDF---VLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170
....*....|
gi 1348983253 171 LLDEPTNHLD 180
Cdd:cd03289 161 LLDEPSAHLD 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
312-491 |
3.86e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYP-GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLV-------GDLALLNGQRkaseLLnigYFAQHq 383
Cdd:COG4178 363 LALEDLTLRTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsGRIARPAGAR----VL---FLPQR- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 384 mdaldgqasPMLQLSRLAD--------KQISEATLRSFLGSFGFSG--ERMDTPC---ESFSGGERARLALALIVWQRPN 450
Cdd:COG4178 435 ---------PYLPLGTLREallypataEAFSDAELREALEAVGLGHlaERLDEEAdwdQVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1348983253 451 VLILDEPTNHLDLDMRHALSMALQD--FEGAVVLVSHERQLIA 491
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRSTLAA 548
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
321-504 |
3.95e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.17 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASK-ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQR---KASELLN----IGYFAQHQMDA 386
Cdd:PRK13639 11 YPDGTEALKgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkptsgeVLIKGEPikyDKKSLLEvrktVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 L-------DGQASPM-LQLSR-LADKQISEAtlrsfLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:PRK13639 91 LfaptveeDVAFGPLnLGLSKeEVEKRVKEA-----LKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 458 TNHLDLDMRHALSMALQDF--EGAVVLVS-HERQLIASVCDDLLLVHAGR 504
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGK 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
306-507 |
4.06e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 306 KMSSPLLTLDQaeIGYP--GKSIASKISLQITPSSRIGLLGMNGAGKSTLIK---SLVG-----------DLALLNGQRK 369
Cdd:PRK10247 2 QENSPLLQLQN--VGYLagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKivaSLISptsgtllfegeDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 370 ASEllnIGYFAQHQMDALDGQASPMLQLSRLADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRP 449
Cdd:PRK10247 80 RQQ---VSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 450 NVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASvCDDL--LLVHAGRCTE 507
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIhryvREQNIAVLWVTHDKDEINH-ADKVitLQPHAGEMQE 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-205 |
4.58e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.19 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVS-LRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSG---WTVAHMAQEVKAL 76
Cdd:PRK10908 1 MIRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--------IERPSAgkiWFSGHDITRLKNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DMPALdfvlsgdeeywqiQKQLAQPEQlsDSELAQLHGRFDE------IHGYSAPSKAAQLMAGL---GFMEHQLRLDVs 147
Cdd:PRK10908 73 EVPFL-------------RRQIGMIFQ--DHHLLMDRTVYDNvaipliIAGASGDDIRRRVSAALdkvGLLDKAKNFPI- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLNAYEGTLILISHDR 205
Cdd:PRK10908 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-219 |
6.15e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 58.23 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT--------------RPSGWtVA 67
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlppreRRVGF-VF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 68 -------HM--AQEVKAldmpALDfVLSGDEEywQIQKQLAqpEQLSDSELAQLHGRFdeihgysaPskaaqlmaglgfm 138
Cdd:COG1118 82 qhyalfpHMtvAENIAF----GLR-VRPPSKA--EIRARVE--ELLELVQLEGLADRY--------P------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 139 eHQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAIL------WLEDWLNAYEGTLILISHDRDflDA-- 210
Cdd:COG1118 132 -SQL-------SGGQRQRVALARALAVEPEVLLLDEPFGA--LDAKVrkelrrWLRRLHDELGGTTVFVTHDQE--EAle 199
|
250
....*....|....
gi 1348983253 211 VTDHIL-----HIE 219
Cdd:COG1118 200 LADRVVvmnqgRIE 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-223 |
6.77e-09 |
|
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: 56.26 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVL-FQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGElgadegslTRPSGWTVAHMAQEVKALDMPA 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE--------ELPTSGTIRVNGQDVSDLRGRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDEEYWQIQKQLAQpeqLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGfMEHQLRLDVSSFSGGWRMRLNLA 160
Cdd:cd03292 73 IPYLRRKIGVVFQDFRLLPD---RNVYENVAFALEVTGVPPREIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 161 RTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQEL 223
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDttwEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
307-504 |
7.62e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.17 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASK-ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ-----------RKASELL 374
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKgININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilfdgkpidysRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 --NIGYFAQ---HQMDAldgqASPMLQLS------RLADKQISEaTLRSFLGSFGFSGERmDTPCESFSGGERARLALAL 443
Cdd:PRK13636 81 reSVGMVFQdpdNQLFS----ASVYQDVSfgavnlKLPEDEVRK-RVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 444 IVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-180 |
8.58e-09 |
|
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: 55.96 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 5 DQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RPSGWTVAHMAQEVKAL-DMPA 80
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARGLLYLgHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDE--EYWQIQKQLAQPEQlsdsELAQlhgrfdeihgysapskaaqlmAGLGFMEHqlrLDVSSFSGGWRMRLN 158
Cdd:cd03231 84 IKTTLSVLEnlRFWHADHSDEQVEE----ALAR---------------------VGLNGFED---RPVAQLSAGQQRRVA 135
|
170 180
....*....|....*....|..
gi 1348983253 159 LARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALD 157
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-181 |
8.87e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR-RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSltrpsgwtVAHMAQEV-KALDMP 79
Cdd:PRK15056 7 IVVNDVTVTwRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK--------ISILGQPTrQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 ALDFVLSGDEEYWQIqkqlaqPEQLSDselAQLHGRFDEIHGYSAPSKAAQ-----LMAGLGFMEHQLRlDVSSFSGGWR 154
Cdd:PRK15056 79 LVAYVPQSEEVDWSF------PVLVED---VVMMGRYGHMGWLRRAKKRDRqivtaALARVDMVEFRHR-QIGELSGGQK 148
|
170 180
....*....|....*....|....*..
gi 1348983253 155 MRLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDV 175
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-504 |
1.01e-08 |
|
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: 57.37 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA---------LLNGQR----KASELLN-----IGYFAQHQMDALD--- 388
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgitsgeiLFDGEDllklSEKELRKirgreIQMIFQDPMTSLNpvm 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 389 --G-QASPMLQLSRLADKQISEATLRSFLGSFGFSG--ERMDT-PCEsFSGGERAR--LALALIVwqRPNVLILDEPTNH 460
Cdd:COG0444 104 tvGdQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRyPHE-LSGGMRQRvmIARALAL--EPKLLIADEPTTA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1348983253 461 LDLDMRH---ALSMALQD-FEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:COG0444 181 LDVTIQAqilNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
324-509 |
1.04e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 324 KSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL--------ALLNGQRKASELLN-IGYFAQHqmDALDGQAS-- 392
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgtILANNRKPTKQILKrTGFVTQD--DILYPHLTvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 ------PMLQLSRLADKQISEATLRSFLGSFGFsgermdTPCE------SF----SGGERARLALALIVWQRPNVLILDE 456
Cdd:PLN03211 159 etlvfcSLLRLPKSLTKQEKILVAESVISELGL------TKCEntiignSFirgiSGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 457 PTNHLDLDMRHALSMALQDF--EGAVVLVS-HE-RQLIASVCDDLLLVHAGRCTEFS 509
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLaqKGKTIVTSmHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
287-504 |
1.11e-08 |
|
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: 55.94 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 287 LLAPAHVDTPFTF---SFREPTKMSSPLLtldqaeigypgksiaSKISLQITPSSRIGLLGMNGAGKSTLIKSL------ 357
Cdd:cd03248 2 SLAPDHLKGIVKFqnvTFAYPTRPDTLVL---------------QDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 358 VGDLALLNGqrKASELLNIGYFaqHQMDALDGQaSPMLQLSRLAD-----------KQISEATLRSFLGSF------GFS 420
Cdd:cd03248 67 QGGQVLLDG--KPISQYEHKYL--HSKVSLVGQ-EPVLFARSLQDniayglqscsfECVKEAAQKAHAHSFiselasGYD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 421 GErMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVcDDLL 498
Cdd:cd03248 142 TE-VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVERA-DQIL 219
|
....*.
gi 1348983253 499 LVHAGR 504
Cdd:cd03248 220 VLDGGR 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
303-488 |
1.30e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.15 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 303 EPTKMSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQR 368
Cdd:PRK11607 11 KTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeqptagqimldgvDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 369 KASELLNIGYFAQHQMDALDGQASPMLQlSRLADKQISE--ATLRSFLGSFGFSGERmdtPcESFSGGERARLALALIVW 446
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASrvNEMLGLVHMQEFAKRK---P-HQLSGGQRQRVALARSLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1348983253 447 QRPNVLILDEPTNHLDLDMRHALSMALQDFEGAV----VLVSHERQ 488
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvtcVMVTHDQE 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.31e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 56.66 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RPSGWTVAH----MAQEv 73
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgEPLDPEDRRrigyLPEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 74 KAL--DMPALDFVLsgdeeYwqiqkqlaqpeqlsdseLAQLhgrfdeiHGYS---APSKAAQLMAGLGFMEHQLRLdVSS 148
Cdd:COG4152 80 RGLypKMKVGEQLV-----Y-----------------LARL-------KGLSkaeAKRRADEWLERLGLGDRANKK-VEE 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILIS-HDRDFLDAVTDHIL 216
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFSsHQMELVEELCDRIV 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
341-563 |
1.40e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 341 GLLGMNGAGKSTLIKSLVGDL------ALLNGQ---------RKasellNIGYFAQ----------HQmdALDGQAspml 395
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLpasegeAWLFGQpvdagdiatRR-----RVGYMSQafslygeltvRQ--NLELHA---- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 396 QLSRLADKQISEAtLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD---LDM--RHALS 470
Cdd:NF033858 365 RLFHLPAAEIAAR-VAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvaRDMfwRLLIE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 471 MALQDfeGAVVLVS-H-----ERqliasvCDDLLLVHAGR----------CTEFSGD-LQD-YAKWLREARQQQINAQTA 532
Cdd:NF033858 443 LSRED--GVTIFIStHfmneaER------CDRISLMHAGRvlasdtpaalVAARGAAtLEEaFIAYLEEAAGAAAAPAAA 514
|
250 260 270
....*....|....*....|....*....|...
gi 1348983253 533 LAQASASTNKTAAPAKVDK--EAQRKLAAQRRE 563
Cdd:NF033858 515 AAPAAAAAAPAAPAPAPRRrfSLRRLLAYARRE 547
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
330-535 |
1.61e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ-RKASELLNIGYFA--QHQMDALDGQASPMLQLSrLADKQIS 406
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKvDRNGEVSVIAISAglSGQLTGIENIEFKMLCMG-FKRKEIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 407 EATLRsfLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA---VVLV 483
Cdd:PRK13546 122 AMTPK--IIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFV 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 484 SHERQLIASVCDDLLLVHAGRCTEFsGDLQD----YAKWLREARQQQINAQTALAQ 535
Cdd:PRK13546 200 SHNLGQVRQFCTKIAWIEGGKLKDY-GELDDvlpkYEAFLNDFKKKSKAEQKEFRN 254
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-485 |
1.62e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.53 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 298 TFSFREPTKMSSPLLTLDQAEIGYPGKSIA--SKISLQITPSSRIGLLGMNGAGKSTLIKSLV-------GDLaLLNGQ- 367
Cdd:PRK11160 325 TFPTTSTAAADQVSLTLNNVSFTYPDQPQPvlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrawdpqqGEI-LLNGQp 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 368 ---------RKASELLN--IGYF----------AQHQmdALDGQASPMLQ---LSRLADkqiSEATLRSFLGSFGfsger 423
Cdd:PRK11160 404 iadyseaalRQAISVVSqrVHLFsatlrdnlllAAPN--ASDEALIEVLQqvgLEKLLE---DDKGLNAWLGEGG----- 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 424 mdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM-RHALSMALQDFEG-AVVLVSH 485
Cdd:PRK11160 474 -----RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITH 532
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-219 |
1.65e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLG-------ELGADEGSLTRPSGWTVAHMA--- 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfykptggTILLRGQHIEGLPGHQIARMGvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 71 --QEVKAL-DMPALDFVLsgdeeywqiqkqLAQPEQLSDSELAQLHG----RFDEihgYSAPSKAAQLMAGLGFMEHQLR 143
Cdd:PRK11300 85 tfQHVRLFrEMTVIENLL------------VAQHQQLKTGLFSGLLKtpafRRAE---SEALDRAATWLERVGLLEHANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 144 lDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL------DLDAILwleDWL-NAYEGTLILISHDRDFLDAVTDHIL 216
Cdd:PRK11300 150 -QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDELI---AELrNEHNVTVLLIEHDMKLVMGISDRIY 225
|
...
gi 1348983253 217 HIE 219
Cdd:PRK11300 226 VVN 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-204 |
1.68e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFaALLGELGADEGSLTRPSGWTVAHMAQEVKA-LDMPALDFVlsgdeeyWQIQKQLA 99
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLL-HLLGGLDTPTSGDVIFNGQPMSKLSSAAKAeLRNQKLGFI-------YQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 100 QPEQLSDSELAQLHGRfdeIHGYSAPSKAAQLMAGLGfMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:PRK11629 101 DFTALENVAMPLLIGK---KKPAEINSRALEMLAAVG-LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*....
gi 1348983253 180 DL---DAILWLEDWLNAYEGTLIL-ISHD 204
Cdd:PRK11629 177 DArnaDSIFQLLGELNRLQGTAFLvVTHD 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
323-462 |
1.76e-08 |
|
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: 54.81 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQ-------RKASELLNIGyfaqHQmDALDG 389
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpplagrVLLNGGpldfqrdSIARGLLYLG----HA-PGIKT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 390 QASPMLQLSRL----ADKQISEATLRSFLGSFGfsgermDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03231 87 TLSVLENLRFWhadhSDEQVEEALARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
312-485 |
1.82e-08 |
|
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: 55.17 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIA----SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKASELLNIGYFAQ 381
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 382 HQ-----MDALDGQASPmLQLSRLADKQISEATlRSFLGSFGFSGERMDTPCEsFSGGERARLALA--LIVwqRPNVLIL 454
Cdd:cd03293 81 QDallpwLTVLDNVALG-LELQGVPKAEARERA-EELLELVGLSGFENAYPHQ-LSGGMRQRVALAraLAV--DPDVLLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1348983253 455 DEPTNHLD----LDMRHALSMALQDFEGAVVLVSH 485
Cdd:cd03293 156 DEPFSALDaltrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
328-572 |
1.87e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 328 SKISLQITPSSRIGLLGMNGAGKSTLiKSLVGDLALLNGQ----RKASELLNIGYFAQHQMDALDGQASPMLQLSrLADK 403
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTL-SNLIAGVTMPNKGtvdiKGSAALIAISSGLNGQLTGIENIELKGLMMG-LTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 404 QISEATLRSFlgSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEptnhldldmrhALSMALQDFEG----- 478
Cdd:PRK13545 119 KIKEIIPEII--EFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE-----------ALSVGDQTFTKkcldk 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 479 ---------AVVLVSHERQLIASVCDDLLLVHAGRCTEFsGDLQD----YAKWLREARQQQINAQTALAQASASTNKTAA 545
Cdd:PRK13545 186 mnefkeqgkTIFFISHSLSQVKSFCTKALWLHYGQVKEY-GDIKEvvdhYDEFLKKYNQMSVEERKDFREEQISQFQHGL 264
|
250 260
....*....|....*....|....*..
gi 1348983253 546 PAKVDKEAQRKLAAQRREETRPLRKKI 572
Cdd:PRK13545 265 LQEDQTGRERKRKKGKKTSRKFKKKRV 291
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-203 |
1.90e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 7 VSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSL---TRPSgwTVAHMAQEVKALD-MPALd 82
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTA--TRGDRSRFMAYLGhLPGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 83 fvlsgdeeywqiQKQLAQPEQLsdSELAQLHGRfdeiHGYSAPSKAaqlMAGLGFMEHQLRLdVSSFSGGWRMRLNLART 162
Cdd:PRK13543 94 ------------KADLSTLENL--HFLCGLHGR----RAKQMPGSA---LAIVGLAGYEDTL-VRQLSAGQKKRLALARL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY---EGTLILISH 203
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
322-504 |
1.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASK----ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLallngqRKASELLNI-GYFAQHQ-----MDALDGQA 391
Cdd:PRK13641 14 PGTPMEKKgldnISFELEEGSFVALVGHTGSGKSTLMQHFNALL------KPSSGTITIaGYHITPEtgnknLKKLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 SPMLQLSR--------------------LADKQISEATLRsFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNV 451
Cdd:PRK13641 88 SLVFQFPEaqlfentvlkdvefgpknfgFSEDEAKEKALK-WLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 452 LILDEPTNHLDLDMRHALSMALQDFEGA---VVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-526 |
1.98e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.16 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA-----LLNGQrkasEL--LNIGYFAQHQmdALDGQASPML 395
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGI----ELreLDPESWRKHL--SWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 396 QLS-----RLADKQISEATL-----RSFLGSFGFSGER-MDTPCE----SFSGGERARLALALIVWQRPNVLILDEPTNH 460
Cdd:PRK11174 436 HGTlrdnvLLGNPDASDEQLqqaleNAWVSEFLPLLPQgLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 461 LDLDMRHALSMALQD--FEGAVVLVSHERQLIAS-----VCDDLLLVHAGRCTEFSGDLQDYAKWLREARQQQ 526
Cdd:PRK11174 516 LDAHSEQLVMQALNAasRRQTTLMVTHQLEDLAQwdqiwVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-216 |
2.06e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 23 QIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpSGWTVAHMAQEVKA-LDMPALDFvLSG-----DEEYWQIqk 96
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYIKPdYDGTVEDL-LRSitddlGSSYYKS-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 97 QLAQPEQLsdselaqlhgrfDEIhgysapskaaqlmaglgfMEHQlrldVSSFSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:PRK13409 436 EIIKPLQL------------ERL------------------LDKN----VKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 177 NHLDldailwLEDWLNA----------YEGTLILISHDRDFLDAVTDHIL 216
Cdd:PRK13409 482 AHLD------VEQRLAVakairriaeeREATALVVDHDIYMIDYISDRLM 525
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-203 |
2.42e-08 |
|
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: 57.06 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRG-GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT--------------RPSgwtV 66
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlngfslkdidrhtlRQF---I 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 67 AHMAQEVKALDMPALDFVLSGDEEywqiqkQLAQPEQLSDSELAQLHgrfDEIHGYSapskaaqlmagLGFmEHQLRLDV 146
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLLLGAKE------NVSQDEIWAACEIAEIK---DDIENMP-----------LGY-QTELSEEG 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 147 SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLdaIL---WLEDWLNAYEGTLILISH 203
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDT--ITekkIVNNLLNLQDKTIIFVAH 667
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
321-485 |
2.73e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.09 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQItPSSRI-GLLGMNGAGKSTLIkSLVGDLA-------LLNGQ-----------RKAS---------- 371
Cdd:COG4604 11 YGGKVVLDDVSLTI-PKGGItALIGPNGAGKSTLL-SMISRLLppdsgevLVDGLdvattpsrelaKRLAilrqenhins 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 372 -----ELLNIGYFAQHQmdaldgqaspmlqlSRL--ADKQISEATLRsFLGSFGFSGERMDTpcesFSGGERARLALALI 444
Cdd:COG4604 89 rltvrELVAFGRFPYSK--------------GRLtaEDREIIDEAIA-YLDLEDLADRYLDE----LSGGQRQRAFIAMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 445 VWQRPNVLILDEPTNhlDLDMRHALSM------ALQDFEGAVVLVSH 485
Cdd:COG4604 150 LAQDTDYVLLDEPLN--NLDMKHSVQMmkllrrLADELGKTVVIVLH 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
309-458 |
3.18e-08 |
|
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: 54.60 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 309 SPLLTLDQAEIGYpGKSIASK-ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ----RKASEL--LN 375
Cdd:COG0410 1 MPMLEVENLHAGY-GGIHVLHgVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPprsgsiRFDGEditgLPPHRIarLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 376 IGY-------FAQhqmdaldgqaspM-----LQL--SRLADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLAL 441
Cdd:COG0410 80 IGYvpegrriFPS------------LtveenLLLgaYARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAI 147
|
170
....*....|....*....
gi 1348983253 442 --ALIvwQRPNVLILDEPT 458
Cdd:COG0410 148 grALM--SRPKLLLLDEPS 164
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-180 |
3.27e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 5 DQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RPSGWT-VAHMAQ-EVKALDMP 79
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRdLYALSEaERRRLLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 ALDFV-----------------------LSGDEEYWQIQKQLAQpeQLSDSELAQlhGRFDEihgysAPSkaaqlmaglg 136
Cdd:PRK11701 90 EWGFVhqhprdglrmqvsaggnigerlmAVGARHYGDIRATAGD--WLERVEIDA--ARIDD-----LPT---------- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 137 fmehqlrldvsSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11701 151 -----------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-210 |
3.65e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 7 VSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELgadegsLTRPSGWTVahmaqevkalDMPALDFvls 86
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL------KGTPVAGCV----------DVPDNQF--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 87 gdeeywqiqkqlaqpeqlsDSELAQLhgrfDEIHGYSAPSKAAQLMAGLGFMEHQL-RLDVSSFSGGWRMRLNLARTLMS 165
Cdd:COG2401 97 -------------------GREASLI----DAIGRKGDFKDAVELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 166 RSDLLLLDEPTNHLDLD-----AILWLEDWLNAyEGTLILISHDRDFLDA 210
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQtakrvARNLQKLARRA-GITLVVATHHYDVIDD 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-211 |
4.22e-08 |
|
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: 53.68 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 7 VSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELG--ADEGSLTrpsgwtvahmAQEVKALDMPALDFV 84
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEIL----------FKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 85 LSGDEEYWQIqkqlaqPEqlsdselaqlhgrfdEIHGYSapskaaqlmaglgfMEHQLR-LDVSsFSGGWRMRLNLARTL 163
Cdd:cd03217 76 RLGIFLAFQY------PP---------------EIPGVK--------------NADFLRyVNEG-FSGGEKKRNEILQLL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 164 MSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGT-LILISHDRDFLDAV 211
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYI 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
330-509 |
4.68e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ----------------RKASELL-------------NIGYFA 380
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRimiddcdvakfgltdlRRVLSIIpqspvlfsgtvrfNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QHQmDALDGQAspmlqlsrLADKQISEATLRSflgSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNH 460
Cdd:PLN03232 1335 EHN-DADLWEA--------LERAHIKDVIDRN---PFGLDAEVSEGG-ENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 461 LDLDMRHALSMAL-QDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFS 509
Cdd:PLN03232 1402 VDVRTDSLIQRTIrEEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
340-504 |
5.19e-08 |
|
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: 54.20 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 340 IGLLGMNGAGKSTLIKSLVGDL---------ALLNGQ-RKASELL-NIGYFAQ------------------------HQM 384
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVegggttsgqILFNGQpRKPDQFQkCVAYVRQddillpgltvretltytailrlprKSS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 DALDGQASPMLQLSRLADKQISeatlrsflgsfgfsGERMdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLD 464
Cdd:cd03234 116 DAIRKKRVEDVLLRDLALTRIG--------------GNLV----KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 465 MRHALSMALQDF--EGAVVLVS-HE-RQLIASVCDDLLLVHAGR 504
Cdd:cd03234 178 TALNLVSTLSQLarRNRIVILTiHQpRSDLFRLFDRILLLSSGE 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
307-507 |
5.24e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPG----KSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLV------------GDLaLLNGQR-- 368
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILrllpsppvvypsGDI-RFHGESll 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 369 KASELL-------NIGYFAQHQMDAL------DGQASPMLQLSRLADKQISEATLRSFLGSFGF--SGERMDTPCESFSG 433
Cdd:PRK15134 80 HASEQTlrgvrgnKIAMIFQEPMVSLnplhtlEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 434 GERARLALALIVWQRPNVLILDEPTNHLDL-----------DMRHALSMALqdfegavVLVSHERQLIASVCDDLLLVHA 502
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilqllrELQQELNMGL-------LFITHNLSIVRKLADRVAVMQN 232
|
....*
gi 1348983253 503 GRCTE 507
Cdd:PRK15134 233 GRCVE 237
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
323-512 |
5.63e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 54.19 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA--------LLNGQR----KASELLNIGYFAQHQM------ 384
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyevtsgtiLFKGQDllelEPDERARAGLFLAFQYpeeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 --------DALDGQAS-------PMLQLSRLADK-----QISEATLRSFLGsfgfsgermdtpcESFSGGERAR---LAL 441
Cdd:TIGR01978 92 vsnleflrSALNARRSargeeplDLLDFEKLLKEklallDMDEEFLNRSVN-------------EGFSGGEKKRneiLQM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 442 ALIvwqRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASVCDDLLLV-HAGRCTEfSGDL 512
Cdd:TIGR01978 159 ALL---EPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVHVlLDGRIVK-SGDV 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
340-509 |
5.73e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 340 IGLLGMNGAGKSTLIKSLVGDLA------LLNGQ----RKASELLN--IGYFAQHQ----------------MDALDGQA 391
Cdd:PRK10762 281 LGVSGLMGAGRTELMKVLYGALPrtsgyvTLDGHevvtRSPQDGLAngIVYISEDRkrdglvlgmsvkenmsLTALRYFS 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 SPMLQLSRLADKQiseaTLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:PRK10762 361 RAGGSLKHADEQQ----AVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ 436
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1348983253 472 ALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGR-CTEFS 509
Cdd:PRK10762 437 LINQFkaEGlSIILVSSEMPEVLGMSDRILVMHEGRiSGEFT 478
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
322-521 |
5.74e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.82 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL---------VGDLALLNGQR-KASELLNI-GYFAQHQM------ 384
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrspkgvkGSGSVLLNGMPiDAKEMRAIsAYVQQDDLfiptlt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 385 --DALDGQAspMLQLSRLADKQISEATLRSFLGSFGF---------SGERMdtpcESFSGGERARLALALIVWQRPNVLI 453
Cdd:TIGR00955 116 vrEHLMFQA--HLRMPRRVTKKEKRERVDEVLQALGLrkcantrigVPGRV----KGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 454 LDEPTNHLDLDMRHALSMALQDF--EGAVVLVS-HE-RQLIASVCDDLLLVHAGRCTeFSGDLQDYAKWLRE 521
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLaqKGKTIICTiHQpSSELFELFDKIILMAEGRVA-YLGSPDQAVPFFSD 260
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-204 |
5.89e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.25 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALlgelgadegslTRpsgwtvahmaqevkaLDMPA 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCF-----------AR---------------LLTPQ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDEEYWQIQ-KQLAQ-----------PEQLSDSELAQ--------LHGRF---DEihgysapSKAAQLMAGLGF 137
Cdd:PRK11231 56 SGTVFLGDKPISMLSsRQLARrlallpqhhltPEGITVRELVAygrspwlsLWGRLsaeDN-------ARVNQAMEQTRI 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 138 MEHQLRLdVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLNAYEGTLILISHD 204
Cdd:PRK11231 129 NHLADRR-LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-507 |
6.23e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLnigyfaqhqmdaLDGQA------------------ 391
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVY------------LDGQDifkmdvielrrrvqmvfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 --SPM------------LQLSRLA-DKQISEATLRSFLGSFGFSGE---RMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK14247 90 ipNPIpnlsifenvalgLKLNRLVkSKKELQERVRWALEKAQLWDEvkdRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 454 LDEPTNHLDLDMR---HALSMALQDfEGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK14247 170 ADEPTANLDPENTakiESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
307-462 |
6.57e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.25 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPG-KSIASK-ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELL---------- 374
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaATYALKdVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 -NIGYFAQH----------QMD---ALDGQASPMLQLSRLADKQISEATLRSFLgsfgfsgermDTPCESFSGGERARLA 440
Cdd:PRK13635 81 rQVGMVFQNpdnqfvgatvQDDvafGLENIGVPREEMVERVDQALRQVGMEDFL----------NREPHRLSGGQKQRVA 150
|
170 180
....*....|....*....|..
gi 1348983253 441 LALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLD 172
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
330-514 |
7.15e-08 |
|
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: 53.88 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ---RKASELLNIGYFAQH-----QMDALDGQASPML 395
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpdsgkiLLNGKditNLPPEKRDISYVPQNyalfpHMTVYKNIAYGLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 396 QlsRLADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALA--LIVwqRPNVLILDEPTNHLDL----DMRHAL 469
Cdd:cd03299 98 K--RKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIAraLVV--NPKILLLDEPFSALDVrtkeKLREEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1348983253 470 SMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFsGDLQD 514
Cdd:cd03299 173 KKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEE 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
147-216 |
8.24e-08 |
|
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: 53.30 E-value: 8.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 147 SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLedwlnAYEG-TLILISHDRDFLDAVTDHIL 216
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelvgevLDVMKDL-----AEEGmTMVVVTHEMGFAREVADRVI 206
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-275 |
8.38e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.50 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALlgelgadeGSLTRPSGWTVAHMAQEVKALDMPALDFVLSgdEEYWQIQKQLAQ 100
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKPTSGTYRVAGQDVATLDADALAQLRR--EHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PEQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEhqlRLDV--SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNH 178
Cdd:PRK10535 98 LSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYqpSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 179 LD------LDAILwleDWLNAYEGTLILISHDRDfLDAVTDHILHIENQELTLYTGNYSTFEVtrserlaqqQQAFEKQV 252
Cdd:PRK10535 175 LDshsgeeVMAIL---HQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEKVNV---------AGGTEPVV 241
|
250 260
....*....|....*....|...
gi 1348983253 253 EARAHLQKFIDRFKAKATKARQA 275
Cdd:PRK10535 242 NTASGWRQFVSGFREALTMAWRA 264
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
331-504 |
9.22e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.24 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 331 SLQITPSSRIGLLGMNGAGKSTLIK------------SLVGDLALLNGQRKASELLN----IGY---FAQHQM--DALDG 389
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVKRlrkeIGLvfqFPEYQLfqETIEK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 390 Q-ASPMLQLSrlADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LD 464
Cdd:PRK13645 111 DiAFGPVNLG--ENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpkgeED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1348983253 465 MRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK13645 189 FINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-462 |
1.04e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.55 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQrkasellNIGYFAQHQ---------MDALDGQASPM 394
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPpdsgsiLIDGK-------DVTKLPEYKrakyigrvfQDPMMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 395 -----LQL-----------SRLADKQISEatLRSFLGSFGFSGE-RMDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:COG1101 98 tieenLALayrrgkrrglrRGLTKKRREL--FRELLATLGLGLEnRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
....*
gi 1348983253 458 TNHLD 462
Cdd:COG1101 176 TAALD 180
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
328-485 |
1.08e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 328 SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGdLA-------LLNGQ--RK-----ASELLNIGyfaqHQmDALDGQASP 393
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LArpdagevLWQGEpiRRqrdeyHQDLLYLG----HQ-PGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 394 M--LQ-LSRLADKQiSEATLRSFLGSFGFSGeRMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDldmRHALS 470
Cdd:PRK13538 92 LenLRfYQRLHGPG-DDEALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID---KQGVA 166
|
170 180
....*....|....*....|.
gi 1348983253 471 MALQDFE------GAVVLVSH 485
Cdd:PRK13538 167 RLEALLAqhaeqgGMVILTTH 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
307-485 |
1.19e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.39 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNG----QRKASELLNI------ 376
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhyRMRDGQLRDLyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 377 ----------GYFAQHQMDALDGQASpmlqlsrlADKQISE--------------ATLRSFLGSFGFSGERMDTPCESFS 432
Cdd:PRK11701 82 errrllrtewGFVHQHPRDGLRMQVS--------AGGNIGErlmavgarhygdirATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 433 GGERARLALALIVWQRPNVLILDEPTNHLD-------LDMRHALsmaLQDFEGAVVLVSH 485
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGL---VRELGLAVVIVTH 210
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
565-631 |
1.20e-07 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 49.00 E-value: 1.20e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 565 TRPLRKKIEQCESQIEKIQPRLASIEEQLADSSLYeaSRKEDLLKLMNEQTSLKATLEQAEETMLEL 631
Cdd:pfam16326 3 SYKEQRELEELEAEIEKLEEEIAELEAQLADPELY--SDYEKLQELSAELEELEAELEELYERWEEL 67
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
320-507 |
1.24e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 54.79 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 320 GYPGKSIA-SKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--DLA----LLNGQ-----RKASELLNIGYFAQHqmdal 387
Cdd:COG1132 348 SYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDPTsgriLIDGVdirdlTLESLRRQIGVVPQD----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 388 dgqaSPMLQLS-----RLADKQISEATLRS---------FLGSF--GFsgermDTPCE----SFSGGERARLALALIVWQ 447
Cdd:COG1132 423 ----TFLFSGTireniRYGRPDATDEEVEEaakaaqaheFIEALpdGY-----DTVVGergvNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 448 RPNVLILDEPTNHLDLDMRHALSMALQDF-EGA-VVLVSHeRqlIASV--CDDLLLVHAGRCTE 507
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLmKGRtTIVIAH-R--LSTIrnADRILVLDDGRIVE 554
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-203 |
1.27e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtRPSGWTVAHMAQEVKAlDM-- 78
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQGEPIRRQRDEYHQ-DLly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 ----PALDFVLSGDE--EYWQIQKQLAQPEQLSDSeLAQ--LHGRFDeihgysAPskAAQLMAGlgfmehQLRldvssfs 150
Cdd:PRK13538 79 lghqPGIKTELTALEnlRFYQRLHGPGDDEALWEA-LAQvgLAGFED------VP--VRQLSAG------QQR------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 151 ggwrmRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY---EGTLILISH 203
Cdd:PRK13538 137 -----RVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
1.28e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.83 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLfqKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSL---------TRPSGWTVAHMAQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltaLPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 72 E--------VK---ALDM-PALdfvlsgdeeywqiqkqlaqpeQLSDSELAQLHgrfdeihgysapsKAAQLMaGLGFME 139
Cdd:COG3840 79 EnnlfphltVAqniGLGLrPGL---------------------KLTAEQRAQVE-------------QALERV-GLAGLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 140 ----HQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLNAYEGTLILISHDRDflDA- 210
Cdd:COG3840 124 drlpGQL-------SGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPE--DAa 194
|
250
....*....|.
gi 1348983253 211 -VTDHILHIEN 220
Cdd:COG3840 195 rIADRVLLVAD 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
312-504 |
1.80e-07 |
|
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: 52.62 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG-------DLaLLNGQRKASELLN---IGYFAQ 381
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfetptsgEI-LLDGKDITNLPPHkrpVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 382 H-----QMDALDGQASPmLQLSRLaDKQISEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDE 456
Cdd:cd03300 80 NyalfpHLTVFENIAFG-LRLKKL-PKAEIKERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 457 PTNHLDLDMRHALS---MALQDFEG-AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03300 157 PLGALDLKLRKDMQlelKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
331-504 |
1.83e-07 |
|
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: 52.11 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 331 SLQITPSSRIGLLGMNGAGKSTLIKSLVG-DLA-----LLNGQ---------RKASELL---NIgyFAQHQMDALDGQA- 391
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPqsgrvLINGVdvtaappadRPVSMLFqenNL--FAHLTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 392 SPMLQLSRLADKQISEAtlrsfLGSFGFSGERMDTPcESFSGGERARLALA-LIVWQRPnVLILDEPTNHLDLDMRHALS 470
Cdd:cd03298 96 SPGLKLTAEDRQAIEVA-----LARVGLAGLEKRLP-GELSGGERQRVALArVLVRDKP-VLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1348983253 471 MALQDF----EGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03298 169 DLVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
307-462 |
1.85e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.86 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL--VGDL---------ALLNGQRKAS---- 371
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLnpevtitgsIVYNGHNIYSprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 372 --ELLN-IGYFAQhqmdaldgQASPM-----------LQLSRLADKQI-SEATLRSFLGS--FGFSGERMDTPCESFSGG 434
Cdd:PRK14239 81 tvDLRKeIGMVFQ--------QPNPFpmsiyenvvygLRLKGIKDKQVlDEAVEKSLKGAsiWDEVKDRLHDSALGLSGG 152
|
170 180
....*....|....*....|....*...
gi 1348983253 435 ERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-203 |
1.93e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSL---RRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqevkaldm 78
Cdd:TIGR00958 479 IEFQDVSFsypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL------------------- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 paLDFVLSGDEEYWQIQKQLAQPEQlsdsELAQLHGRFDEIHGY----------SAPSKAAQLMAGLGFMEHQLRLDV-- 146
Cdd:TIGR00958 540 --LDGVPLVQYDHHYLHRQVALVGQ----EPVLFSGSVRENIAYgltdtpdeeiMAAAKAANAHDFIMEFPNGYDTEVge 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 147 --SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLILISH 203
Cdd:TIGR00958 614 kgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
320-507 |
2.05e-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: 52.23 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 320 GY-PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLV-------GDLaLLNGQ----------RKA-------SELL 374
Cdd:cd03253 9 AYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFrfydvssGSI-LIDGQdirevtldslRRAigvvpqdTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 N--IGY-FAQHQMDALDGQaspMLQLSRLAdkQISEATLRSflgSFGFS---GER--MdtpcesFSGGERARLALALIVW 446
Cdd:cd03253 88 NdtIGYnIRYGRPDATDEE---VIEAAKAA--QIHDKIMRF---PDGYDtivGERglK------LSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 447 QRPNVLILDEPTNHLDLDMRHALSMALQD-FEG-AVVLVSHERQLIASvCDDLLLVHAGRCTE 507
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-249 |
2.44e-07 |
|
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: 54.18 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSgwTVAHMAQEVKALDMPALDFVLSGdeeywqiqKQLAQ 100
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQQAWIQNDSLRENILFG--------KALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PEqlsdselaqlhgrfdeihgYSAPSKAAQLMAGLGFMEHQLRLDVS----SFSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:TIGR00957 728 KY-------------------YQQVLEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 177 NHLDLDAILWLEDWLNAYEGTL-----ILISHDRDFLDAVtDHILHIEN---------QELTLYTGNYSTFEVTRSErlA 242
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYLPQV-DVIIVMSGgkisemgsyQELLQRDGAFAEFLRTYAP--D 865
|
....*..
gi 1348983253 243 QQQQAFE 249
Cdd:TIGR00957 866 EQQGHLE 872
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
331-489 |
2.49e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.89 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 331 SLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNG---------QRKASELL-------------NIGYfaqh 382
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTpasgslTLNGqdhtttppsRRPVSMLFqennlfshltvaqNIGL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 383 qmdALDgqasPMLqlsRLADKQisEATLRSFLGSFGFSG--ERMdtPCEsFSGGERARLALA-LIVWQRPnVLILDEPTN 459
Cdd:PRK10771 95 ---GLN----PGL---KLNAAQ--REKLHAIARQMGIEDllARL--PGQ-LSGGQRQRVALArCLVREQP-ILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|
gi 1348983253 460 HLDLDMRHALSMALQDfegavvlVSHERQL 489
Cdd:PRK10771 159 ALDPALRQEMLTLVSQ-------VCQERQL 181
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-223 |
2.58e-07 |
|
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: 52.50 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALDMPALDFVLSGDEEYWQIQKQLAQ 100
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLG--------LEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PEQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:TIGR02769 103 PRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 181 L---DAILWLEDWLNAYEGT-LILISHDRDFLDAVTDHILHIENQEL 223
Cdd:TIGR02769 183 MvlqAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-204 |
2.69e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 24 IHPGWKVGLTGVNGAGKSTLFAALlgeLGADEGSLTRPS--GWTVAHMAQEVKA-LDMPALDFVLsgdeeywqiQKQLAQ 100
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAIL---AGLDDGSSGEVSlvGQPLHQMDEEARAkLRAKHVGFVF---------QSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PeQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEhqlRLD--VSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNH 178
Cdd:PRK10584 101 P-TLNALENVELPALLRGESSRQSRNGAKALLEQLGLGK---RLDhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|
gi 1348983253 179 LDL---DAILWLEDWLNA-YEGTLILISHD 204
Cdd:PRK10584 177 LDRqtgDKIADLLFSLNReHGTTLILVTHD 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
321-526 |
2.71e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL------------VGDLAL-----LNGQRKASELL--NIGYFAQ 381
Cdd:PRK11264 13 FHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIdtarsLSQQKGLIRQLrqHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 382 H-----QMDALDGQASPMLQLSRLAdKQISEATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDE 456
Cdd:PRK11264 93 NfnlfpHRTVLENIIEGPVIVKGEP-KEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 457 PTNHLDLDM-RHALSM--ALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEfsgdlQDYAKWLREARQQQ 526
Cdd:PRK11264 171 PTSALDPELvGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE-----QGPAKALFADPQQP 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-206 |
3.00e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.92 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQEVKALDMPALDFVLSgdeEYWQIQKQLA- 99
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQRPINMMFQSYALF---PHMTVEQNIAf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 100 --QPEQLSDSELAQlhgRFDEihgysapskaaqlMAGLGFMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTN 177
Cdd:PRK11607 115 glKQDKLPKAEIAS---RVNE-------------MLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 178 HLD--LDAILWLE--DWLNAYEGTLILISHDRD 206
Cdd:PRK11607 179 ALDkkLRDRMQLEvvDILERVGVTCVMVTHDQE 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-180 |
3.04e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPG-WKVgLTGVNGAGKSTLF---AALL----GEL---GADEGSLTrPSGW--TVA 67
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGeFKL-ITGPSGCGKSTLLkivASLIsptsGTLlfeGEDISTLK-PEIYrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 68 HMAQevkaldMPALdFvlsGDEEY------WQIQKQLAQPEQLSDSeLAQLhgrfdeihgysapskaaqlmaglGFMEHQ 141
Cdd:PRK10247 85 YCAQ------TPTL-F---GDTVYdnlifpWQIRNQQPDPAIFLDD-LERF-----------------------ALPDTI 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 1348983253 142 LRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK10247 131 LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
321-507 |
3.05e-07 |
|
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: 53.57 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIA--SKISLQITPSSRIGLLGMNGAGKSTLIKSL-------VGDLaLLNGQRKASELL-----NIGYFAQHQMdA 386
Cdd:TIGR02203 340 YPGRDRPalDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGQI-LLDGHDLADYTLaslrrQVALVSQDVV-L 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 LDGQASPMLQLSRLAD---KQISEATLRSFLGSF-GFSGERMDTPCES----FSGGERARLALALIVWQRPNVLILDEPT 458
Cdd:TIGR02203 418 FNDTIANNIAYGRTEQadrAEIERALAAAYAQDFvDKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 459 NHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:TIGR02203 498 SALDNESERLVQAALERLmQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
308-504 |
3.31e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 308 SSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ----RKASELLNIG 377
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQpdagsiLIDGQemrfASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 378 YFAQHQMDALDGQASPM--LQLSRLADKQ--ISEATLRSFLGS-FGFSGERMD--TPCESFSGGERARLALALIVWQRPN 450
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAenLYLGQLPHKGgiVNRRLLNYEAREqLEHLGVDIDpdTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 451 VLILDEPTNHL---DLDMRHALSMALQDfEGAVVL-VSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK11288 161 VIAFDEPTSSLsarEIEQLFRVIRELRA-EGRVILyVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
329-508 |
3.41e-07 |
|
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: 51.34 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 329 KISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQrkasellnIgyfaqhQMDALDGQASPMLQL-SRLA----DK 403
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGS--------I------LIDGVDISKIGLHDLrSRISiipqDP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 404 QISEATLRSFLGSFG-FSGERM--------------------DTPCES----FSGGERARLALALIVWQRPNVLILDEPT 458
Cdd:cd03244 88 VLFSGTIRSNLDPFGeYSDEELwqalervglkefveslpgglDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 459 NHLDLDMRHALSMALQD-FEGAVVL-VSHERQLIASvCDDLLLVHAGRCTEF 508
Cdd:cd03244 168 ASVDPETDALIQKTIREaFKDCTVLtIAHRLDTIID-SDRILVLDKGRVVEF 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-204 |
3.48e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.40 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtVAHM--AQEVKAL----------------DMPALD 82
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR------VLGYvpFKRRKEFarrigvvfgqrsqlwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 83 -FVLsgdeeywqiqkqLAQPEQLSDSELAQLHGRFDEIhgysapskaaqlmagLGfMEHQLRLDVSSFSGGWRMRLNLAR 161
Cdd:COG4586 116 sFRL------------LKAIYRIPDAEYKKRLDELVEL---------------LD-LGELLDTPVRQLSLGQRMRCELAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 162 TLMSRSDLLLLDEPTNHLDL---DAILWLEDWLNAYEG-TLILISHD 204
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNRERGtTILLTSHD 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
307-500 |
3.92e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.81 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGY-PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ--------RKASELLNIG 377
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgqptRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 378 YFAQ-HQMD----------ALDGQASPM--LQLSRLADKQISEATLrsflgsfgfsgERMDT------PCESFSGGERAR 438
Cdd:PRK15056 82 YVPQsEEVDwsfpvlvedvVMMGRYGHMgwLRRAKKRDRQIVTAAL-----------ARVDMvefrhrQIGELSGGQKKR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 439 LALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQDfEGAVVLVS-HERQLIASVCDDLLLV 500
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEAriiSLLRELRD-EGKTMLVStHNLGSVTEFCDYTVMV 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
278-517 |
4.15e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.19 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 278 RIKQLEKMQLLAPAHVDTPFTF---SFREPTKMSSPLL-----TLdqaeigYPGKSIAskislqitpssrigLLGMNGAG 349
Cdd:TIGR00958 460 RKPNIPLTGTLAPLNLEGLIEFqdvSFSYPNRPDVPVLkgltfTL------HPGEVVA--------------LVGPSGSG 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 350 KSTLIKSL------VGDLALLNGQRkaseLLNIGYFAQHQMDALDGQaSPML-----------QLSRLADKQISEATLRS 412
Cdd:TIGR00958 520 KSTVAALLqnlyqpTGGQVLLDGVP----LVQYDHHYLHRQVALVGQ-EPVLfsgsvreniayGLTDTPDEEIMAAAKAA 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 413 FLGSFGFSGER-MDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHER 487
Cdd:TIGR00958 595 NAHDFIMEFPNgYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRL 674
|
250 260 270
....*....|....*....|....*....|
gi 1348983253 488 QLIASvCDDLLLVHAGRCTEFSGDLQDYAK 517
Cdd:TIGR00958 675 STVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-206 |
4.25e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 51.94 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtVAHMaqevkaldmpaldfVLSgDEEYWQIQKQLAQ 100
Cdd:PRK13635 27 SFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT------VGGM--------------VLS-EETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PEQLSDSELAQLHGRFD-----EIHGYSAPS------KAAQLMAGLGFMEHQlrldVSSFSGGWRMRLNLARTLMSRSDL 169
Cdd:PRK13635 86 VFQNPDNQFVGATVQDDvafglENIGVPREEmvervdQALRQVGMEDFLNRE----PHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 170 LLLDEPTNHLD-------LDAILWLEDWLNAyegTLILISHDRD 206
Cdd:PRK13635 162 IILDEATSMLDprgrrevLETVRQLKEQKGI---TVLSITHDLD 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
128-219 |
4.26e-07 |
|
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: 51.14 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 128 AAQLMAGLGfMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLNAYEGTLILISH 203
Cdd:cd03297 112 VDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTH 190
|
90
....*....|....*.
gi 1348983253 204 DRDFLDAVTDHILHIE 219
Cdd:cd03297 191 DLSEAEYLADRIVVME 206
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
323-490 |
5.56e-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: 52.83 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHqmdaldgqasPMLQLSRLAD 402
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQR----------PYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 403 -------------KQISEATLRSFL------------GSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:TIGR00954 534 qiiypdssedmkrRGLSDKDLEQILdnvqlthilereGGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 458 TNHLDLDMRHALSMALQDFEGAVVLVSHERQLI 490
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
344-492 |
5.79e-07 |
|
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: 50.68 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 344 GMNGAGKSTLIK----SLVGDLAL-LNGQRKASELLNIGyfaqhqmdALDGQASpmLQLSRLADKQIsEAT--LRSFLGS 416
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELPPnSKGGAHDPKLIREG--------EVRAQVK--LAFENANGKKY-TITrsLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 417 FGFSGERMDTPCE----SFSGGERA------RLALALIVWQRPNVLILDEPTNHLDLD-MRHALSMALQDFEGA----VV 481
Cdd:cd03240 98 IFCHQGESNWPLLdmrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQknfqLI 177
|
170
....*....|.
gi 1348983253 482 LVSHERQLIAS 492
Cdd:cd03240 178 VITHDEELVDA 188
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
308-507 |
6.44e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 308 SSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELL------------- 374
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLlggrsifnyrdvl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 ----NIGYFAQHQ-------MDALDGQASPMLQLSRLADKQISEATLRSfLGSFGFSGERMDTPCESFSGGERARLALAL 443
Cdd:PRK14271 98 efrrRVGMLFQRPnpfpmsiMDNVLAGVRAHKLVPRKEFRGVAQARLTE-VGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-217 |
7.07e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLfAALL--------GELGADEGSLTRPSGWTVAHMAQEVKaldmpaLDFvlsgDEEY- 91
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTL-ARLLtmietptgGELYYQGQDLLKADPEAQKLLRQKIQ------IVF----QNPYg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 92 -----WQIQKQLAQP----EQLSDSELAQlhgrfdeihgysapsKAAQLMAGLGFM-EHQLRLDvSSFSGGWRMRLNLAR 161
Cdd:PRK11308 104 slnprKKVGQILEEPllinTSLSAAERRE---------------KALAMMAKVGLRpEHYDRYP-HMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 162 TLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLN-AYegtlILISHDRdfldAVTDHILH 217
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDvsvqaqvLNLMMDLQQELGlSY----VFISHDL----SVVEHIAD 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-186 |
7.11e-07 |
|
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: 52.71 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 24 IHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEVKAL----DMPALDFVLSGDEEYWQIQKQLA 99
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgycpQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 100 QPEQlsdselaqlhgRFDEIHGYSAPSkaaqlmagLGFMEHQLRLdVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:TIGR01257 2042 VPAE-----------EIEKVANWSIQS--------LGLSLYADRL-AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
....*....
gi 1348983253 180 DLDA--ILW 186
Cdd:TIGR01257 2102 DPQArrMLW 2110
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-228 |
8.70e-07 |
|
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: 50.35 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 14 RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELgaDEGSLTrpSGwTVAHMAQEVKALDM-------PALDFVLS 86
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTT--SG-QILFNGQPRKPDQFqkcvayvRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 87 G--DEEYWQIQKQLAQPEQLSDSELAQLhgrfDEIHGYSApskAAQLMAGlgfmeHQLrldVSSFSGGWRMRLNLARTLM 164
Cdd:cd03234 95 GltVRETLTYTAILRLPRKSSDAIRKKR----VEDVLLRD---LALTRIG-----GNL---VKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 165 SRSDLLLLDEPTNHLD----LDAILWLEDWlnAYEGTLILIS-HD-RDFLDAVTDHILHIENQELtLYTG 228
Cdd:cd03234 160 WDPKVLILDEPTSGLDsftaLNLVSTLSQL--ARRNRIVILTiHQpRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
307-485 |
9.17e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 50.86 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKS----IASKISLQITPSSRIGLLGMNGAGKSTLIKsLVGDL-------ALLNGQRKASELLN 375
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLR-LIAGLekptsgeVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 376 IGY-FAQHQ----MDALD----GqaspmLQLSRLADKQIsEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALA--LI 444
Cdd:COG1116 82 RGVvFQEPAllpwLTVLDnvalG-----LELRGVPKAER-RERARELLELVGLAGFEDAYPHQ-LSGGMRQRVAIAraLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1348983253 445 VwqRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSH 485
Cdd:COG1116 155 N--DPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTH 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-203 |
9.26e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.09 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR-RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---------RPSGW--TVAHM 69
Cdd:COG1132 340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLESLrrQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 70 AQEVkaldmpaldFVLSG--------------DEEYWQIqkqlaqpeqlsdSELAQLHgrfDEI----HGYsapskaaql 131
Cdd:COG1132 420 PQDT---------FLFSGtirenirygrpdatDEEVEEA------------AKAAQAH---EFIealpDGY--------- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 132 maglgfmEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAIlwledwLNAYEG-TLILISH 203
Cdd:COG1132 467 -------DTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEAL------ERLMKGrTTIVIAH 533
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
132-242 |
9.31e-07 |
|
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: 50.41 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 132 MAGLGFMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDWLNAYEGTLILISHDRDF 207
Cdd:cd03299 113 IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEE 192
|
90 100 110
....*....|....*....|....*....|....*
gi 1348983253 208 LDAVTDHILHIENQELTLYTGNYSTFEVTRSERLA 242
Cdd:cd03299 193 AWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
323-485 |
9.89e-07 |
|
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: 49.66 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ-RKASELLNIGYFAQHQ-------MDALDGQASPM 394
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEvRWNGTPLAEQRDEPHEnilylghLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 395 LQLSRL-ADKQISEATLRSFLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILDEPTNHLD---LDMRHAL 469
Cdd:TIGR01189 92 ENLHFWaAIHGGAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALArLWLSRRP-LWILDEPTTALDkagVALLAGL 169
|
170
....*....|....*.
gi 1348983253 470 SMALQDFEGAVVLVSH 485
Cdd:TIGR01189 170 LRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
311-464 |
1.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYP-GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL-----------------VGDLALLNGQRKAse 372
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLngllrpqkgkvlvsgidTGDFSKLQGIRKL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 373 llnIGYFAQHQMDALDGQAS-------------PMLQLSRLADKQISEATLRSFlgsfgfsgeRMDTPcESFSGGERARL 439
Cdd:PRK13644 79 ---VGIVFQNPETQFVGRTVeedlafgpenlclPPIEIRKRVDRALAEIGLEKY---------RHRSP-KTLSGGQGQCV 145
|
170 180
....*....|....*....|....*
gi 1348983253 440 ALALIVWQRPNVLILDEPTNHLDLD 464
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPD 170
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-176 |
1.19e-06 |
|
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: 49.74 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALdmPALDFVLSGdeeywqiqkqLAQ 100
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMG--------LLPPRSGSIRFDGRDITGL--PPHERARAG----------IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 -PE------QLSDSE---LAQLHGRFDEIHgySAPSKAAQLMAGLGFMEHQLrldVSSFSGGWRMRLNLARTLMSRSDLL 170
Cdd:cd03224 80 vPEgrrifpELTVEEnllLGAYARRRAKRK--ARLERVYELFPRLKERRKQL---AGTLSGGEQQMLAIARALMSRPKLL 154
|
....*.
gi 1348983253 171 LLDEPT 176
Cdd:cd03224 155 LLDEPS 160
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
336-493 |
1.46e-06 |
|
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: 48.14 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 336 PSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKAsellnigyfaqhqmdaLDGQASPMLQLSRLADKQISEATLrsflg 415
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------IDGEDILEEVLDQLLLIIVGGKKA----- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 416 sfgfsgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASV 493
Cdd:smart00382 60 --------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-175 |
1.50e-06 |
|
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: 49.85 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 5 DQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALDMpaldfv 84
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG--------LVKPDSGKILLDGQDITKLPM------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 85 lsgdeeywqiqKQLAqpeQLSDSELAQLHGRFD------------EIHGYS---APSKAAQLMAGLGfMEHQLRLDVSSF 149
Cdd:cd03218 70 -----------HKRA---RLGIGYLPQEASIFRkltveenilavlEIRGLSkkeREEKLEELLEEFH-ITHLRKSKASSL 134
|
170 180
....*....|....*....|....*.
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEP 175
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEP 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-224 |
1.60e-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: 50.50 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 30 VGLTGVNGAGKSTLFAALLGELGADEGSLtrpsgwtvaHMAQEV-----KALDMP----ALDFV-----------LSGDE 89
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEI---------VLNGRTlfdsrKGIFLPpekrRIGYVfqearlfphlsVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 90 EYwqiqkqlaqpeQLSDSELAQLHGRFDEIhgysapskaAQLMAglgfMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDL 169
Cdd:TIGR02142 97 RY-----------GMKRARPSERRISFERV---------IELLG----IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 170 LLLDEPTNHLDL---DAIL-WLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELT 224
Cdd:TIGR02142 153 LLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
310-495 |
1.66e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.04 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 310 PLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLvGDLALLNGQRKASEllNIGYFAQH------Q 383
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG--RVEFFNQNiyerrvN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 384 MDALDGQAS---------------------------PMLQLSRLADKQISEATLRSFLGSfgfsgeRMDTPCESFSGGER 436
Cdd:PRK14258 83 LNRLRRQVSmvhpkpnlfpmsvydnvaygvkivgwrPKLEIDDIVESALKDADLWDEIKH------KIHKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 437 ARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCD 495
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
322-490 |
1.68e-06 |
|
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: 49.25 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQMDALDGQASPMLQLSRLA 401
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 402 DKQISEATlrsflgSFG--FSGERMDTPCES------------------------FSGGERARLALALIVWQRPNVLILD 455
Cdd:cd03290 92 NATVEENI------TFGspFNKQRYKAVTDAcslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1348983253 456 EPTNHLDLDMRHALSMA-----LQDFEGAVVLVSHERQLI 490
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-252 |
1.83e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALL------GELGADEGSLTRPSGWTVAHM----AQEVKAL-DMPALdfvlsgde 89
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAgllpgsGSIQFAGQPLEAWSAAELARHraylSQQQTPPfAMPVF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 90 EYWqiqkQLAQPEQlsdSELAQLHGRFDEIhgysapSKAAQLMAGLGFMEHQLrldvssfSGG-W-RMR-----LNLART 162
Cdd:PRK03695 88 QYL----TLHQPDK---TRTEAVASALNEV------AEALGLDDKLGRSVNQL-------SGGeWqRVRlaavvLQVWPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYE---GTLILISHDrdfldavTDHILHIENQELTLYTGNY----STFEV 235
Cdd:PRK03695 148 INPAGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD-------LNHTLRHADRVWLLKQGKLlasgRRDEV 220
|
250
....*....|....*..
gi 1348983253 236 TRSERLAqqqQAFEKQV 252
Cdd:PRK03695 221 LTPENLA---QVFGVNF 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
322-507 |
1.99e-06 |
|
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: 49.15 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 322 PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKslvgdlaLLNGqrkasellnigyFAQHQ-----MDALDGqaspmlq 396
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLIN-------LLMR------------FYDPQkgqilIDGIDI------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 397 lsrladKQISEATLRSFLG-----SFGFSGE-----RMDTPC----------------------------------ESFS 432
Cdd:cd03254 68 ------RDISRKSLRSMIGvvlqdTFLFSGTimeniRLGRPNatdeevieaakeagahdfimklpngydtvlgengGNLS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 433 GGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:cd03254 142 QGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-223 |
2.06e-06 |
|
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: 48.58 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 9 LRRGGRvlFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVahmaqevkaldmpaldfvlsgd 88
Cdd:cd03215 10 LSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--------LRPPASGEI---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 89 eeywqiqkqlaqpeqlsdselaQLHGRfdEIHGYSaPSKAAQlmAGLGF-----MEHQLRLDVS---------SFSGGWR 154
Cdd:cd03215 58 ----------------------TLDGK--PVTRRS-PRDAIR--AGIAYvpedrKREGLVLDLSvaenialssLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGT-LILISHDRDFLDAVTDHILHIENQEL 223
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadAGKaVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
309-496 |
2.17e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 309 SPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLAL------LNGQR------KASELLNI 376
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRdagsilYLGKEvtfngpKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 377 GYFaqHQmdaldgqaspmlQLSRLADKQISEATL--RSFLGSFG-FSGERM-----------------DTPCESFSGGER 436
Cdd:PRK10762 82 GII--HQ------------ELNLIPQLTIAENIFlgREFVNRFGrIDWKKMyaeadkllarlnlrfssDKLVGELSIGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 437 ARLALALIVWQRPNVLILDEPTNHL-DLDMRHALSM--ALQDFEGAVVLVSHERQLIASVCDD 496
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVirELKSQGRGIVYISHRLKEIFEICDD 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-214 |
2.30e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.12 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 13 GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahMAQEVKALdMPALDFVLSGDeEYW 92
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---------IDDEDISL-LPLHARARRGI-GYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 93 QIQKQLAQPEQLSDSELAQLHGRfDEIHGYSAPSKAAQLMAglGFMEHQLRLDV-SSFSGGWRMRLNLARTLMSRSDLLL 171
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIR-DDLSAEQREDRANELME--EFHIEHLRDSMgQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1348983253 172 LDEPTNHLDLDAILWLEDwlnayegtliLISHDRDFLDAV--TDH 214
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKR----------IIEHLRDSGLGVliTDH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
323-566 |
2.49e-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: 51.06 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLV------GDLAL---------LNGQRKASELL--NIGYFAQHQMD 385
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllsteGEIQIdgvswnsvtLQTWRKAFGVIpqKVFIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 ALDGQAspmlqlsRLADKQI----SEATLRSFLGSFgfsGERMDTPCES----FSGGERARLALALIVWQRPNVLILDEP 457
Cdd:TIGR01271 1311 NLDPYE-------QWSDEEIwkvaEEVGLKSVIEQF---PDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 458 TNHLDLDMRHALSMAL-QDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTEFSGdLQdyaKWLREA---RQQQINAQTAL 533
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLkQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS-IQ---KLLNETslfKQAMSAADRLK 1456
|
250 260 270
....*....|....*....|....*....|...
gi 1348983253 534 AQASASTNKTAAPAKVDKEAQRKLAAQRREETR 566
Cdd:TIGR01271 1457 LFPLHRRNSSKRKPQPKITALREEAEEEVQNTR 1489
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
329-504 |
2.50e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.35 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 329 KISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNG----------QRKASELLN-IGYFAQHQMDAL-------DGQ 390
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrvkvmgrevnAENEKWVRSkVGLVFQDPDDQVfsstvwdDVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 391 ASPMLQlsRLADKQISEATlRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:PRK13647 103 FGPVNM--GLDKDEVERRV-EEALKAVRMWDFR-DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1348983253 471 MALQDF--EGAVVLVS-HERQLIASVCDDLLLVHAGR 504
Cdd:PRK13647 179 EILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGR 215
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-215 |
2.72e-06 |
|
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: 49.29 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 26 PGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWT--VAHMA-------------QEVKALDMPA-LDfvlsgde 89
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeiLDEFRgselqnyftklleGDVKVIVKPQyVD------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 90 eywQIQKQLaqpeqlsDSELAQLHGRFDEIHgysapsKAAQLMAGLGfMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDL 169
Cdd:cd03236 98 ---LIPKAV-------KGKVGELLKKKDERG------KLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 170 LLLDEPTNHLDLD-----AILWLEdwLNAYEGTLILISHDRDFLDAVTDHI 215
Cdd:cd03236 161 YFFDEPSSYLDIKqrlnaARLIRE--LAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
330-507 |
2.76e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.39 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELL---------------NIGYFAQHQMDAL--DGQAS 392
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrkRIGMVFQFPESQLfeDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 PMLQLSRLADKQISEATLRSF--LGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:PRK13646 106 EIIFGPKNFKMNLDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVM 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1348983253 471 MALQDFE----GAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK13646 186 RLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
330-458 |
3.02e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ-------RKASElLNIGYFAQHQMD----------- 385
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiLIDGKpvrirspRDAIA-LGIGMVHQHFMLvpnltvaeniv 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 386 -ALDGQASPMLQLSRLADKqiseatLRSFLGSFGFSGErMDTPCESFSGGERARL----ALalivWQRPNVLILDEPT 458
Cdd:COG3845 103 lGLEPTKGGRLDRKAARAR------IRELSERYGLDVD-PDAKVEDLSVGEQQRVeilkAL----YRGARILILDEPT 169
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-182 |
3.19e-06 |
|
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: 48.56 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSgwtvahmaQEVKALDMPALDFVLSgdeeywqIQKQlaQ 100
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--------IDISTIPLEDLRSSLT-------IIPQ--D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PEQLSDSELAQLHgRFDEihgYSapskAAQLMAGLGFMEHQLRLdvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03369 91 PTLFSGTIRSNLD-PFDE---YS----DEEIYGALRVSEGGLNL-----SQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
..
gi 1348983253 181 LD 182
Cdd:cd03369 158 YA 159
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-175 |
3.19e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.87 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 12 GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGS-------LTR-----------------PS---GW 64
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRifldgedITHlpmhkrarlgigylpqeASifrKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 65 TVahmAQEVKAldmpaldfVLsgdeEYWQIQKqlAQPEQLSDSELAQLHgrfdeIhGYSAPSKAAQLmaglgfmehqlrl 144
Cdd:COG1137 94 TV---EDNILA--------VL----ELRKLSK--KEREERLEELLEEFG-----I-THLRKSKAYSL------------- 137
|
170 180 190
....*....|....*....|....*....|.
gi 1348983253 145 dvssfSGGWRMRLNLARTLMSRSDLLLLDEP 175
Cdd:COG1137 138 -----SGGERRRVEIARALATNPKFILLDEP 163
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-181 |
3.67e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.93 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGwkvGLT---GVNGAGKSTLFAALLGELGADEGSLtrpsgwTVAHMaqEVKALD 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKG---GITaliGPNGAGKSTLLSMISRLLPPDSGEV------LVDGL--DVATTP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 78 MPALDFVLSgdeeywqIQKQ-LAQPEQLSDSELAQLhGRF----------DEIHgysaPSKAAQLMaGLGFMEHQlRLDv 146
Cdd:COG4604 70 SRELAKRLA-------ILRQeNHINSRLTVRELVAF-GRFpyskgrltaeDREI----IDEAIAYL-DLEDLADR-YLD- 134
|
170 180 190
....*....|....*....|....*....|....*
gi 1348983253 147 sSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:COG4604 135 -ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
312-504 |
3.73e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 312 LTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLikslvgdLALLNGQRKAS--ELL-NIGYFAQHQMDAld 388
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL-------LRLLAGLETPSagELLaGTAPLAEAREDT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 389 gqaSPMLQLSRLA--DKQISEATL----------RSFLGSFGFSGERMDTPCeSFSGGERARLALALIVWQRPNVLILDE 456
Cdd:PRK11247 84 ---RLMFQDARLLpwKKVIDNVGLglkgqwrdaaLQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 457 PTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-180 |
3.81e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.93 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 14 RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQEVKALDM------PaldfvLSG 87
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI-DGKDVTKLPEYKRAKYIgrvfqdP-----MMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 88 DEEYWQIQKQLAqpeqlsdseLAQLHGRF---------DEIHGYSApsKAAQLmaGLGfMEHQLRLDVSSFSGGWRMRLN 158
Cdd:COG1101 93 TAPSMTIEENLA---------LAYRRGKRrglrrgltkKRRELFRE--LLATL--GLG-LENRLDTKVGLLSGGQRQALS 158
|
170 180
....*....|....*....|..
gi 1348983253 159 LARTLMSRSDLLLLDEPTNHLD 180
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
323-504 |
3.85e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG-----DLALLNGQRKASELLN---------IGY-FAQHQ--MD 385
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGierpsAGKIWFSGHDITRLKNrevpflrrqIGMiFQDHHllMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 --ALDGQASPMLQLSRLAD---KQISEAtlrsfLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNH 460
Cdd:PRK10908 94 rtVYDNVAIPLIIAGASGDdirRRVSAA-----LDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 461 LDLDMRHALSMALQDFE--GAVVLV-SHERQLIASVCDDLLLVHAGR 504
Cdd:PRK10908 168 LDDALSEGILRLFEEFNrvGVTVLMaTHDIGLISRRSYRMLTLSDGH 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
307-489 |
4.01e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.66 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIAS----KISLQITPSSRIGLLGMNGAGKSTLIKsLVGDL-------ALLNGQ-------R 368
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTdvlhNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLdtptsgdVIFNGQpmsklssA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 369 KASELLN--IGYFAQ-HQM----DALDGQASPMLqLSRLADKQISEaTLRSFLGSFGFSGERMDTPCEsFSGGERARLAL 441
Cdd:PRK11629 80 AKAELRNqkLGFIYQfHHLlpdfTALENVAMPLL-IGKKKPAEINS-RALEMLAAVGLEHRANHRPSE-LSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 442 ALIVWQRPNVLILDEPTNHLDL---DMRHALSMALQDFEG-AVVLVSHERQL 489
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGtAFLVVTHDLQL 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
432-513 |
4.11e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMR----HALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
....*.
gi 1348983253 508 fSGDLQ 513
Cdd:PRK10261 250 -TGSVE 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-254 |
4.25e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.86 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 22 MQIHPGWKVGLTGVNGAGKSTLFAALLGELGAD----------------EGSLTRPSGWTVAHMA---QEVKALD-MPAL 81
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqrEGRLARDIRKSRANTGyifQQFNLVNrLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 82 DFVLSG---DEEYWQIQKQLAQPEQlsdselaqlhgrfdeihgysaPSKAAQLMAGLGfMEHQLRLDVSSFSGGWRMRLN 158
Cdd:PRK09984 105 ENVLIGalgSTPFWRTCFSWFTREQ---------------------KQRALQALTRVG-MVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL---NAYEG-TLILISHDRDFLDAVTDHILHIEnQELTLYTGNYSTFE 234
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLrdiNQNDGiTVVVTLHQVDYALRYCERIVALR-QGHVFYDGSSQQFD 241
|
250 260
....*....|....*....|
gi 1348983253 235 VTRSERLAQQQQAFEKQVEA 254
Cdd:PRK09984 242 NERFDHLYRSINRVEENAKA 261
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
150-225 |
4.27e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.52 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---------LDAILWLEdwlnaYEGTLILISHDRDFLDAVTDHILHIEN 220
Cdd:PRK11247 135 SGGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdLIESLWQQ-----HGFTVLLVTHDVSEAVAMADRVLLIEE 209
|
....*
gi 1348983253 221 QELTL 225
Cdd:PRK11247 210 GKIGL 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
307-526 |
4.58e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.43 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSL-------VGDLALLN----------GQRK 369
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGqtinlvrdkdGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 370 ASE-----LLN--IGYFAQH-----QMDALDGQASPMLQLSRLADKQISEATLRsFLGSFGFSGERMDTPCESFSGGERA 437
Cdd:PRK10619 81 VADknqlrLLRtrLTMVFQHfnlwsHMTVLENVMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 438 RLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDDLLLVHAGRCTEfSGDLQD 514
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLHQGKIEE-EGAPEQ 238
|
250
....*....|..
gi 1348983253 515 YAKWLREARQQQ 526
Cdd:PRK10619 239 LFGNPQSPRLQQ 250
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
340-486 |
5.64e-06 |
|
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: 48.13 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 340 IGLLGMNGAGKSTLIKSLVGDLA--------------LLNGQRkASELLNigYFAQhqmdALDGQASPML------QLSR 399
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKpnlgkfddppdwdeILDEFR-GSELQN--YFTK----LLEGDVKVIVkpqyvdLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 400 LADKQISEATLRSF-LGSFGFSGERM------DTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRhaLSMA 472
Cdd:cd03236 102 AVKGKVGELLKKKDeRGKLDELVDQLelrhvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR--LNAA 179
|
170
....*....|....*....
gi 1348983253 473 -----LQDFEGAVVLVSHE 486
Cdd:cd03236 180 rlireLAEDDNYVLVVEHD 198
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
307-507 |
6.08e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.33 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGY-PGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ-----RKASELlniGYFA 380
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEirldgRPLSSL---SHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QHQMDALDGQASPMLQLSRLAD----KQISEATLRSFL--------------GSFGFSGERMDTpcesFSGGERARLALA 442
Cdd:PRK10790 413 LRQGVAMVQQDPVVLADTFLANvtlgRDISEEQVWQALetvqlaelarslpdGLYTPLGEQGNN----LSVGQKQLLALA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 443 LIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVcDDLLLVHAGRCTE 507
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEA-DTILVLHRGQAVE 554
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-226 |
6.16e-06 |
|
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: 47.91 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 9 LRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGwtvahmaqEVKALDMPALDFvlsgd 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RG--------RVSSLLGLGGGF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 89 eeywqiqkqlaQPEQ--------------LSDSELAQlhgRFDEIHGYSapskaaqlmaGLG-FMEhqlrLDVSSFSGGW 153
Cdd:cd03220 96 -----------NPELtgreniylngrllgLSRKEIDE---KIDEIIEFS----------ELGdFID----LPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 154 RMRLNLARTLMSRSDLLLLDEPT----NHLDLDAILWLEDWLNAyEGTLILISHDRDFLDAVTDHILHIENQELTLY 226
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-570 |
6.44e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 342 LLGMNGAGKSTLIKSLVGDLALLNGQRKASEllNIGYFAQHQ--MDA--------LDGQASPMLQ----LSRL-ADKQIS 406
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQAwiMNAtvrgnilfFDEEDAARLAdavrVSQLeADLAQL 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 407 EATLRSFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDldmRHALSMALQD-FEGAV----- 480
Cdd:PTZ00243 769 GGGLETEIGEKGVN----------LSGGQKARVSLARAVYANRDVYLLDDPLSALD---AHVGERVVEEcFLGALagktr 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 481 VLVSHERQLIASVcdDLLLVHAGRCTEFSGDLQDYA-----KWLREARQQQINAQTALAQASASTNKTAAPAKVDKEAQR 555
Cdd:PTZ00243 836 VLATHQVHVVPRA--DYVVALGDGRVEFSGSSADFMrtslyATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPV 913
|
250
....*....|....*
gi 1348983253 556 KLAAQRREETRPLRK 570
Cdd:PTZ00243 914 AKQEGNAEGGDGAAL 928
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-212 |
6.50e-06 |
|
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: 47.87 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRG--GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSL--------TRPSGW---TVAH 68
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaLADPAWlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 69 MAQEVKALDMPALDFVLSGDEeywqiqkqlaQPEQLSDSELAQLHGRFDEIhgysapskaAQLMAGLGFMehqLRLDVSS 148
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADP----------GMSMERVIEAAKLAGAHDFI---------SELPEGYDTI---VGEQGAG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDldailwledwlnaYEGTLILISHDRDFLDAVT 212
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALD-------------YESEHAIMRNMHDICAGRT 189
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
307-469 |
7.07e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.21 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKS--IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ----------------R 368
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifynnqaitddnfeklR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 369 KasellNIGYFAQH----------QMD---ALDGQASPMLQLSRLADKQISEATLRsflgsfgfsgERMDTPCESFSGGE 435
Cdd:PRK13648 83 K-----HIGIVFQNpdnqfvgsivKYDvafGLENHAVPYDEMHRRVSEALKQVDML----------ERADYEPNALSGGQ 147
|
170 180 190
....*....|....*....|....*....|....
gi 1348983253 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHAL 469
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-223 |
8.56e-06 |
|
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: 47.47 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSL---RRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALL-------GELGADEGSLT----RPSGWTVA 67
Cdd:cd03248 12 VKFQNVTFaypTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqgGQVLLDGKPISqyehKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 68 HMAQEvkaldmPaldfVLSGDEEYWQIQKQLAQPEQLSDSELAQLHGRFDEI----HGYS--APSKAAQLmaglgfmehq 141
Cdd:cd03248 92 LVGQE------P----VLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFIselaSGYDteVGEKGSQL---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 142 lrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLE----DWLNAYegTLILISHDrdfLDAV--TDHI 215
Cdd:cd03248 152 --------SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQqalyDWPERR--TVLVIAHR---LSTVerADQI 218
|
....*...
gi 1348983253 216 LHIENQEL 223
Cdd:cd03248 219 LVLDGGRI 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-182 |
9.22e-06 |
|
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: 49.17 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR--RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtRPSGWTVAHMA---QEVKAL 76
Cdd:TIGR00957 1285 VEFRNYCLRyrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-IIDGLNIAKIGlhdLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DMPALDFVLSGdeeywQIQKQLAQPEQLSDS------ELAQLHGRFDeihgySAPSKaaqlmaglgfMEHQLRLDVSSFS 150
Cdd:TIGR00957 1364 IIPQDPVLFSG-----SLRMNLDPFSQYSDEevwwalELAHLKTFVS-----ALPDK----------LDHECAEGGENLS 1423
|
170 180 190
....*....|....*....|....*....|..
gi 1348983253 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD 182
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-565 |
9.72e-06 |
|
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: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLV------GDLAL---------LNGQRKASELL--NIGYFAQHQMD 385
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIdgvswnsvpLQKWRKAFGVIpqKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 ALD--GQASPMlQLSRLADKQISEATLRSFLGSFGFSGErmDTPCeSFSGGERARLALALIVWQRPNVLILDEPTNHLDL 463
Cdd:cd03289 96 NLDpyGKWSDE-EIWKVAEEVGLKSVIEQFPGQLDFVLV--DGGC-VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 464 DMRHALSMAL-QDFEGAVVLVSHERQLIASVCDDLLLVHAGRCtefsgdlqdyakWLREARQQQINAQTALAQASASTNK 542
Cdd:cd03289 172 ITYQVIRKTLkQAFADCTVILSEHRIEAMLECQRFLVIEENKV------------RQYDSIQKLLNEKSHFKQAISPSDR 239
|
250 260
....*....|....*....|....*..
gi 1348983253 543 TAA-PAKVDKEAQRKLAAQ---RREET 565
Cdd:cd03289 240 LKLfPRRNSSKSKRKPRPQiqaLQEET 266
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
321-504 |
1.04e-05 |
|
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: 46.86 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG-----DLALLNGQRKASEL----LNIGYFAQH-----QMDA 386
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleeptSGRIYIGGRDVTDLppkdRDIAMVFQNyalypHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 LDGQASPmLQLsRLADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD---- 462
Cdd:cd03301 90 YDNIAFG-LKL-RKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklr 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1348983253 463 LDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-512 |
1.04e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtRPSGWTVAHMAqevkaldmPA 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-EIGGNPCARLT--------PA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSgdeEYWQIQKQLAQPeQLSDSE--LAQLHGRFDeihgysAPSKAAQLMAGLGFmehQLRLDVSSFSggwrmrLN 158
Cdd:PRK15439 82 KAHQLG---IYLVPQEPLLFP-NLSVKEniLFGLPKRQA------SMQKMKQLLAALGC---QLDLDSSAGS------LE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 159 LA--------RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGT---LILISHDRDFLDAVTDHILHIENQELTLY- 226
Cdd:PRK15439 143 VAdrqiveilRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHKLPEIRQLADRISVMRDGTIALSg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 227 -TGNYSTFEVTrserlaqqqQAFEKqvearahlqkfidrfKAKATKARQAQsrikqleKMQLLAPAHvdtpftfsfREPT 305
Cdd:PRK15439 223 kTADLSTDDII---------QAITP---------------AAREKSLSASQ-------KLWLELPGN---------RRQQ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 306 KMSSPLLTLDQaeigYPGKSIASkISLQITPSSRIGLLGMNGAGKSTLIKSLVGdlalLNGQRKASELLNigyfaQHQMD 385
Cdd:PRK15439 263 AAGAPVLTVED----LTGEGFRN-ISLEVRAGEILGLAGVVGAGRTELAETLYG----LRPARGGRIMLN-----GKEIN 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 ALDGQASPMLQLSRLA-DKQIS-----------------------------EATLRSFLGSFGFSGERMDTPCESFSGGE 435
Cdd:PRK15439 329 ALSTAQRLARGLVYLPeDRQSSglyldaplawnvcalthnrrgfwikpareNAVLERYRRALNIKFNHAEQAARTLSGGN 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHAL-----SMALQDFegAVVLVSHERQLIASVCDDLLLVHAGrctEFSG 510
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIyqlirSIAAQNV--AVLFISSDLEEIEQMADRVLVMHQG---EISG 483
|
..
gi 1348983253 511 DL 512
Cdd:PRK15439 484 AL 485
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
308-495 |
1.06e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.48 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 308 SSPLLTLDQAEIGYPGkSIA-SKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQR------KASELL 374
Cdd:COG1129 1 AEPLLEMRGISKSFGG-VKAlDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQpdsgeiLLDGEPvrfrspRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 NIGYFAQHqmdaldgqasPML--QLS---------------RLADKQISEATlRSFLGSFGFSgERMDTPCESFSGGER- 436
Cdd:COG1129 80 GIAIIHQE----------LNLvpNLSvaeniflgreprrggLIDWRAMRRRA-RELLARLGLD-IDPDTPVGDLSVAQQq 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 437 ----ARlALAlivwQRPNVLILDEPTNHLDLD--------MRHalsmaLQDfEG-AVVLVSH---ErqlIASVCD 495
Cdd:COG1129 148 lveiAR-ALS----RDARVLILDEPTASLTEReverlfriIRR-----LKA-QGvAIIYISHrldE---VFEIAD 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
141-239 |
1.09e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 141 QLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILISHDRDFLDAVTDHILHI 218
Cdd:PRK14246 146 RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFL 225
|
90 100
....*....|....*....|.
gi 1348983253 219 ENQELTLYTGNYSTFEVTRSE 239
Cdd:PRK14246 226 YNGELVEWGSSNEIFTSPKNE 246
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
330-504 |
1.13e-05 |
|
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: 46.27 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQ----RKASELLN--IGYFAQ-HQMDALdgqaspMLQ 396
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPpasgeiTLDGKpvtrRSPRDAIRagIAYVPEdRKREGL------VLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 397 LSrladkqISE-ATLRSFLgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR---HALSMA 472
Cdd:cd03215 93 LS------VAEnIALSSLL-----------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKaeiYRLIRE 149
|
170 180 190
....*....|....*....|....*....|..
gi 1348983253 473 LQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:cd03215 150 LADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-215 |
1.18e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.80 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 10 RRGGRVlfqKA----SMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALDMPALdfvl 85
Cdd:COG4608 26 RTVGVV---KAvdgvSFDIRRGETLGLVGESGCGKSTLGRLLLR--------LEEPTSGEILFDGQDITGLSGREL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 86 sgdeeywqiqKQLAQPEQL--SDSeLAQLHGRFD---------EIHGYSAPS----KAAQLMA--GLG--FME---HQlr 143
Cdd:COG4608 91 ----------RPLRRRMQMvfQDP-YASLNPRMTvgdiiaeplRIHGLASKAerreRVAELLElvGLRpeHADrypHE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 144 ldvssFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---------LdailwLEDwLNAYEG-TLILISHDrdfLdAVTD 213
Cdd:COG4608 158 -----FSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaqvlnL-----LED-LQDELGlTYLFISHD---L-SVVR 222
|
..
gi 1348983253 214 HI 215
Cdd:COG4608 223 HI 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
307-458 |
1.19e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDlallngqRKASEllniGYFAQHQMDA 386
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-------PRATS----GRIVFDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 387 LDGQASPMLQ------------LSRL------------ADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALA 442
Cdd:PRK11614 70 TDWQTAKIMReavaivpegrrvFSRMtveenlamggffAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIG 149
|
170
....*....|....*.
gi 1348983253 443 LIVWQRPNVLILDEPT 458
Cdd:PRK11614 150 RALMSQPRLLLLDEPS 165
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-220 |
1.35e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 47.01 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAAL-------LGELGADEGSLTRPSGwTVAHMAQEV 73
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVNDPKV-DERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 74 KAL--------DMPALDFVLSGdeeywqiqkqlaqPEQLSDSELAQlhgrfdeihgysAPSKAAQLMAGLGFMEHQLRLD 145
Cdd:PRK09493 80 GMVfqqfylfpHLTALENVMFG-------------PLRVRGASKEE------------AEKQARELLAKVGLAERAHHYP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 146 vSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLnAYEG-TLILISHDRDFLDAVTDHILHIEN 220
Cdd:PRK09493 135 -SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDL-AEEGmTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
318-503 |
1.46e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 47.77 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 318 EIGYPGKS-----IASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG--------------DLALLNGQRKasellNIGY 378
Cdd:PRK10851 4 EIANIKKSfgrtqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsghirfhgtDVSRLHARDR-----KVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 379 FAQH-----QMDALDGQA----------SP--------------MLQLSRLADKQISEatlrsflgsfgfsgermdtpce 429
Cdd:PRK10851 79 VFQHyalfrHMTVFDNIAfgltvlprreRPnaaaikakvtqlleMVQLAHLADRYPAQ---------------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 430 sFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDDLLLVHAG 503
Cdd:PRK10851 137 -LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-216 |
1.46e-05 |
|
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: 48.21 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGG--RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTV----AHMAQevka 75
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG--------VWPPTAGSVrldgADLSQ---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 76 ldmpaldfvlsgdeeyWQiqkqlaqPEQLS--------DSEL-----AQLHGRFDEIHgysaPSK---AAQLmAGLgfme 139
Cdd:COG4618 399 ----------------WD-------REELGrhigylpqDVELfdgtiAENIARFGDAD----PEKvvaAAKL-AGV---- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 140 HQ--LRL----------DVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDwlnayEG-TLI 199
Cdd:COG4618 447 HEmiLRLpdgydtrigeGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIRALKA-----RGaTVV 521
|
250
....*....|....*..
gi 1348983253 200 LISHDRDFLdAVTDHIL 216
Cdd:COG4618 522 VITHRPSLL-AAVDKLL 537
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
311-503 |
1.63e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 311 LLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA------LLNGQRKASELLNIGYFAQHQ- 383
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 384 ----MDALDGQASPmLQLSRLADKQiSEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:PRK11248 81 llpwRNVQDNVAFG-LQLAGVEKMQ-RLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1348983253 460 HLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDDLLLVHAG 503
Cdd:PRK11248 158 ALDAFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
330-503 |
1.67e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.01 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVG------DLALLNGQRKASELL-----NIGYFAQHQMD------------- 385
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGlfeefeGKVKIDGELLTAENVwnlrrKIGMVFQNPDNqfvgatveddvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 386 ALDGQASPMLQLSRLADKQISEATLRSFlgsfgfsgeRMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDF---------KTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1348983253 466 RHALSMALQDFEG----AVVLVSHERQLIASvCDDLLLVHAG 503
Cdd:PRK13642 176 RQEIMRVIHEIKEkyqlTVLSITHDLDEAAS-SDRILVMKAG 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-180 |
1.67e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.78 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKA----SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQE---V 73
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPAlqdvSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL-DGVPVTGPGADrgvV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 74 ---KALdMPALDfvlsgdeeywqIQKQLAQPEQLSDSELAQLHGRfdeihgysapskAAQLMAGLGfMEHQLRLDVSSFS 150
Cdd:COG4525 82 fqkDAL-LPWLN-----------VLDNVAFGLRLRGVPKAERRAR------------AEELLALVG-LADFARRRIWQLS 136
|
170 180 190
....*....|....*....|....*....|
gi 1348983253 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
330-503 |
1.93e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.94 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASELLNIGYFAQHQMDALDGQASPMLQLsrlADKQISEAT 409
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQF---PEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 410 L----------------------RSFLGSFGFSGERMD-TPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLD---- 462
Cdd:PRK13634 103 VekdicfgpmnfgvseedakqkaREMIELVGLPEELLArSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgr 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1348983253 463 ---LDMRHALSmalQDFEGAVVLVSHERQLIASVCDDLLLVHAG 503
Cdd:PRK13634 182 kemMEMFYKLH---KEKGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
330-504 |
2.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.66 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVG-----------DLALLNGQRKASELLNIgyfAQHQMDALDGQASPMLQLS 398
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlhvptqgsvrvDDTLITSTSKNKDIKQI---RKKVGLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 399 RLAD-----------KQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH 467
Cdd:PRK13649 103 VLKDvafgpqnfgvsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1348983253 468 ALsMALqdFEG------AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK13649 183 EL-MTL--FKKlhqsgmTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-181 |
2.11e-05 |
|
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: 46.77 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 16 LFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtRPSGwTVAHMAQevKALDMPA-----LDFVLSGDEE 90
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-KHSG-RISFSSQ--FSWIMPGtikenIIFGVSYDEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 91 YWQIQKQLAQPEQlsdsELAQLhgrfdeihgysaPSKAAQLMAGLGFmehqlrldvsSFSGGWRMRLNLARTLMSRSDLL 170
Cdd:cd03291 128 RYKSVVKACQLEE----DITKF------------PEKDNTVLGEGGI----------TLSGGQRARISLARAVYKDADLY 181
|
170
....*....|.
gi 1348983253 171 LLDEPTNHLDL 181
Cdd:cd03291 182 LLDSPFGYLDV 192
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
423-507 |
2.24e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 423 RMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQDFEG-AVVLVSHERQLIASVCDDLL 498
Cdd:PRK11022 146 RLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQiieLLLELQQKENmALVLITHDLALVAEAAHKII 225
|
....*....
gi 1348983253 499 LVHAGRCTE 507
Cdd:PRK11022 226 VMYAGQVVE 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
140-507 |
2.26e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 140 HQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLNA-YEGTLILISHDRDFLDAVTDHI 215
Cdd:PRK10261 167 HQL-------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 216 LhienqelTLYTGNystfevtrserlAQQQQAFEKQVEARAHlqkfidrfkaKATKARQAQsrIKQLEKMQLLapahvDT 295
Cdd:PRK10261 240 L-------VMYQGE------------AVETGSVEQIFHAPQH----------PYTRALLAA--VPQLGAMKGL-----DY 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 296 PFTF---SFREPTKMSS-----------PLLTLDQAEIGYPGKS-----------IASKISLQITPSSRIGLLGMNGAGK 350
Cdd:PRK10261 284 PRRFpliSLEHPAKQEPpieqdtvvdgePILQVRNLVTRFPLRSgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 351 ST-------LIKSLVGDLaLLNGQR----KASELL----NIGYFAQHQMDALDGQA----SPM--LQLSRLADKQISEAT 409
Cdd:PRK10261 364 STtgrallrLVESQGGEI-IFNGQRidtlSPGKLQalrrDIQFIFQDPYASLDPRQtvgdSIMepLRVHGLLPGKAAAAR 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 410 LRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQ-DFEGAVVLVSH 485
Cdd:PRK10261 443 VAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQiinLLLDLQrDFGIAYLFISH 522
|
410 420
....*....|....*....|..
gi 1348983253 486 ERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK10261 523 DMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
320-462 |
2.79e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.26 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 320 GYPGKSIA-SKISLQITPSSRIGLLGMNGAGKSTLI--------------------------KSLVGDLA-------LLN 365
Cdd:PRK13657 343 SYDNSRQGvEDVSFEAKPGQTVAIVGPTGAGKSTLInllqrvfdpqsgrilidgtdirtvtrASLRRNIAvvfqdagLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 366 gqRKASELLNIGyfaqhQMDALDGQaspMLQLSRLAdkQISEATLRSFLGSFGFSGERmdtpCESFSGGERARLALALIV 445
Cdd:PRK13657 423 --RSIEDNIRVG-----RPDATDEE---MRAAAERA--QAHDFIERKPDGYDTVVGER----GRQLSGGERQRLAIARAL 486
|
170
....*....|....*..
gi 1348983253 446 WQRPNVLILDEPTNHLD 462
Cdd:PRK13657 487 LKDPPILILDEATSALD 503
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-218 |
2.97e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 46.10 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELG--ADEGSLTRpSGWTVAHMAQEVKA-----------LDMP---ALDFV 84
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILF-KGQDLLELEPDERAraglflafqypEEIPgvsNLEFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 85 LSGDEeywqIQKQLAQPEQLSDSELAQLhgrfdeihgysapskAAQLMAGLGFMEHQLRLDVS-SFSGGWRMRLNLARTL 163
Cdd:TIGR01978 99 RSALN----ARRSARGEEPLDLLDFEKL---------------LKEKLALLDMDEEFLNRSVNeGFSGGEKKRNEILQMA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 164 MSRSDLLLLDEPTNHLDLDAILWLEDWLNAY---EGTLILISHDRDFLDAVTDHILHI 218
Cdd:TIGR01978 160 LLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-204 |
3.46e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 9 LRR--GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALL------GELGADEGSL---TRPSGWTVAHMAQEV---- 73
Cdd:PRK15134 292 LKRtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIWFDGQPLhnlNRRQLLPVRHRIQVVfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 74 -KALDmPALDfVLSGDEEYWQI-QKQL--AQPEQlsdselaqlhgrfdeihgysapsKAAQLMAGLGFMEHQLRLDVSSF 149
Cdd:PRK15134 372 nSSLN-PRLN-VLQIIEEGLRVhQPTLsaAQREQ-----------------------QVIAVMEEVGLDPETRHRYPAEF 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWL-NAYEGTLILISHD 204
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILALLKSLqQKHQLAYLFISHD 485
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-180 |
3.51e-05 |
|
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: 45.23 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 8 SLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELgadegsltrpsgwTVAHMAQEVKALDMPaldfvlSG 87
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-------------TGLGVSGEVLINGRP------LD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 88 DEEYwqiQKQLAQPEQlSDSELAQLHGRfdEIHGYSApskaaqlmaglgfmehQLRldvsSFSGGWRMRLNLARTLMSRS 167
Cdd:cd03213 77 KRSF---RKIIGYVPQ-DDILHPTLTVR--ETLMFAA----------------KLR----GLSGGERKRVSIALELVSNP 130
|
170
....*....|...
gi 1348983253 168 DLLLLDEPTNHLD 180
Cdd:cd03213 131 SLLFLDEPTSGLD 143
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-507 |
3.56e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrpsgwtvahmaqeVKALDMPA 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-------------INNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDFVLSGDEEYWQIQKQLAQPEQLSDSE---LAQLHGR----FDEIHGYSAPSKAAQLMAGLGfMEHQLRLDVSSFSGGW 153
Cdd:PRK09700 72 LDHKLAAQLGIGIIYQELSVIDELTVLEnlyIGRHLTKkvcgVNIIDWREMRVRAAMMLLRVG-LKVDLDEKVANLSISH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 154 RMRLNLARTLMSRSDLLLLDEPTNHL---DLDAILWLEDWLNAyEGTLIL-ISHDRDFLDAVTDHILHIENQElTLYTGN 229
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISHKLAEIRRICDRYTVMKDGS-SVCSGM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 230 YSTFEVTRSERLAQQQQafekqvearahLQkfiDRFKAKATKARQaqsrikqlekmqllapahVDTPFTFSFREPTkmss 309
Cdd:PRK09700 229 VSDVSNDDIVRLMVGRE-----------LQ---NRFNAMKENVSN------------------LAHETVFEVRNVT---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 310 plltldqaeiGYPGKSIaSKISLQITPSSRIGLLGMNGAGKSTLIKSLVG------DLALLNGQR--KASELL----NIG 377
Cdd:PRK09700 273 ----------SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkragGEIRLNGKDisPRSPLDavkkGMA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 378 YFAQHQMD---------ALDGQASPMLQLSRLA----------DKQISEAtlrsflgsfgfSGERMDTPCES-------F 431
Cdd:PRK09700 342 YITESRRDngffpnfsiAQNMAISRSLKDGGYKgamglfhevdEQRTAEN-----------QRELLALKCHSvnqniteL 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKaeiYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
323-462 |
3.57e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNG----QRKASELLNIG---YFAQHQmDALDGQASPML 395
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtiklDGGDIDDPDVAeacHYLGHR-NAMKPALTVAE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 396 QLSRLA------DKQISEAtlrsfLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILDEPTNHLD 462
Cdd:PRK13539 93 NLEFWAaflggeELDIAAA-----LEAVGLAP-LAHLPFGYLSAGQKRRVALArLLVSNRP-IWILDEPTAALD 159
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
307-514 |
3.63e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG------DLALLNGQ------RKASELL 374
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiheptkGTITINNInynkldHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 NIGYFAQhqmdaldgQASPMLQLSRLADKQISEATLRSFLG----SFGFSGER-------------MDTPCESFSGGERA 437
Cdd:PRK09700 81 GIGIIYQ--------ELSVIDELTVLENLYIGRHLTKKVCGvniiDWREMRVRaammllrvglkvdLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 438 RLALALIVWQRPNVLILDEPTNHL---DLDMRHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGRCTeFSGDLQD 514
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV-CSGMVSD 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-254 |
4.13e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRR--GGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrPSGWTVAH--MAQEVKAL 76
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM-IDDCDVAKfgLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 77 DM-PALDFVLSGDEEYwqiqkqlaQPEQLSDSELAQLHGRFDEIHGYSAPSKAAqlmagLGfMEHQLRLDVSSFSGGWRM 155
Cdd:PLN03232 1313 SIiPQSPVLFSGTVRF--------NIDPFSEHNDADLWEALERAHIKDVIDRNP-----FG-LDAEVSEGGENFSVGQRQ 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 156 RLNLARTLMSRSDLLLLDEPTNHLDL--DAILWLEDWLNAYEGTLILISHDRD-FLDAvtDHILHIENQELTLYTgnyst 232
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVrtDSLIQRTIREEFKSCTMLVIAHRLNtIIDC--DKILVLSSGQVLEYD----- 1451
|
250 260
....*....|....*....|..
gi 1348983253 233 fevTRSERLAQQQQAFEKQVEA 254
Cdd:PLN03232 1452 ---SPQELLSRDTSAFFRMVHS 1470
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-204 |
4.30e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.83 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 10 RRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVKALDMPA--------- 80
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG--------LESPSQGNVSWRGEPLAKLNRAQrkafrrdiq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDF--VLSGDEEYWQIQKQLAQPEQ--LSDSELAQLHgrfdeihgysapsKAAQLMAGLGFMEHQLRLDVSSFSGGWRMR 156
Cdd:PRK10419 93 MVFqdSISAVNPRKTVREIIREPLRhlLSLDKAERLA-------------RASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 157 LNLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDwLNAYEGT-LILISHD 204
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKK-LQQQFGTaCLFITHD 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-181 |
4.47e-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: 46.83 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpsgwtvahmaqevkaldmpaldfvlSGDEEYwQIQKQLAQ 100
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH-------------------------SGRISF-SPQTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PEQLSDSELAQLhgRFDEIHgYSAPSKAAQLMAGLGFMEHQLRLDVS----SFSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:TIGR01271 500 PGTIKDNIIFGL--SYDEYR-YTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPF 576
|
....*
gi 1348983253 177 NHLDL 181
Cdd:TIGR01271 577 THLDV 581
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-204 |
4.57e-05 |
|
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: 45.81 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWT----------VAHM-AQEVKAL----------D-M 78
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILG--------LLPPPGITsgeilfdgedLLKLsEKELRKIrgreiqmifqDpM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 PALDFVLSgdeeywqIQKQLAqpeqlsdsELAQLHGRFDEIhgySAPSKAAQLMAGLGFMEHQLRLDV--SSFSGGWRMR 156
Cdd:COG0444 97 TSLNPVMT-------VGDQIA--------EPLRIHGGLSKA---EARERAIELLERVGLPDPERRLDRypHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 157 LNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLNAyegTLILISHD 204
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDvtiqaqiLNLLKDLQRELGL---AILFITHD 210
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
340-501 |
4.72e-05 |
|
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: 44.49 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 340 IGLLGMNGAGKSTLIKSLVGDLaLLNGQRKASELLNIGYFAQHQmdaldgqaspmlqlsrladkqiseatlrsflgsfgf 419
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQL-IPNGDNDEWDGITPVYKPQYI------------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 420 sgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCD 495
Cdd:cd03222 71 ----------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSD 140
|
....*.
gi 1348983253 496 DLLLVH 501
Cdd:cd03222 141 RIHVFE 146
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-204 |
5.01e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.36 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 5 DQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRPSGWTVAHMAQEV-KALDMPALDF 83
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 84 VLSGDEEYWQIQKQLAQPEQlsdsELAQLHGRFDEihgySAPSKAAQLMAglgfMEHQLRLDVSSFSGGWRMRLNLARTL 163
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQ----PLFTRWRKEDE----EAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1348983253 164 MSRSDLLLLDEPTNHLDLDA---ILWLEDWLNAYEG-TLILISHD 204
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHqidLLELLSELNREKGyTLAAVLHD 203
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
149-216 |
5.09e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 5.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWL-NAYEGTLILISHDRDFLDAVTDHIL 216
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELkREFNTAIIMITHDLGVVAGICDKVL 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
124-243 |
5.16e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 45.00 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 124 APSKAAQLMAglgfmehQLRLDVSS------FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILwledW 190
Cdd:COG4161 118 AREKAMKLLA-------RLRLTDKAdrfplhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqvVEIIR----E 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 191 LNAYEGTLILISHDRDFLDAVTDHILHIENQELTLYtGNYSTFEVTRSERLAQ 243
Cdd:COG4161 187 LSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTEAFAH 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
307-504 |
5.45e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.71 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG----DLA--LLNGQRKA---------- 370
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfetpDSGriMLDGQDIThvpaenrhvn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 371 ----SELL--------NIGYFAQHQ-----------MDALDgqaspMLQLSRLADKQISEatlrsflgsfgfsgermdtp 427
Cdd:PRK09452 90 tvfqSYALfphmtvfeNVAFGLRMQktpaaeitprvMEALR-----MVQLEEFAQRKPHQ-------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 428 cesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM---ALQDFEG-AVVLVSHERQLIASVCDDLLLVHAG 503
Cdd:PRK09452 145 ---LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHDQEEALTMSDRIVVMRDG 221
|
.
gi 1348983253 504 R 504
Cdd:PRK09452 222 R 222
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
429-492 |
5.63e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 5.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 429 ESFSGGERARLALAL--IVWQRPN----VLILDEPTNHLDLDMRHALS----MALQDFEG--AVVLVSHERQLIAS 492
Cdd:PRK01156 800 DSLSGGEKTAVAFALrvAVAQFLNndksLLIMDEPTAFLDEDRRTNLKdiieYSLKDSSDipQVIMISHHRELLSV 875
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
305-490 |
5.70e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 305 TKMSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLA--LLNG----------QRKASE 372
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGdilfkgesilDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 373 LLNIGYFAQHQ----------MDALdgqaspMLQL-SRLADKQISEATLRSFlgsFGFSGERMD----TPC-------ES 430
Cdd:CHL00131 81 RAHLGIFLAFQypieipgvsnADFL------RLAYnSKRKFQGLPELDPLEF---LEIINEKLKlvgmDPSflsrnvnEG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 431 FSGGERAR---LALALIvwqRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLI 490
Cdd:CHL00131 152 FSGGEKKRneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLL 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-203 |
5.89e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.97 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR--RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RP-SGWT----VAHMA- 70
Cdd:PRK11160 339 LTLNNVSFTypDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPiADYSeaalRQAISv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 71 --QEVkaldmpaldFVLSGD-EEYWQIQKQLAQPEQLSDSeLAQ--LHGRFDEIHGysapskaaqLMAGLGFMEHQLrld 145
Cdd:PRK11160 419 vsQRV---------HLFSATlRDNLLLAAPNASDEALIEV-LQQvgLEKLLEDDKG---------LNAWLGEGGRQL--- 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 146 vssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLedwLNAY--EGTLILISH 203
Cdd:PRK11160 477 ----SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILEL---LAEHaqNKTVLMITH 532
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
124-243 |
6.10e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.96 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 124 APSKAAQLMAGLGFMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLNAYEGTLIL 200
Cdd:PRK10619 128 ARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVV 207
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1348983253 201 ISHDRDFLDAVTDHILHIENQELTLYTGNYSTFEVTRSERLAQ 243
Cdd:PRK10619 208 VTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-180 |
6.81e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 14 RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtrpsgW---TVAHMAQEVKALDMPALDFVLSGDEE 90
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----WaerSIAYVPQQAWIMNATVRGNILFFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 91 ywqiqkqlaQPEQLSDS-ELAQLHgrfdeihgysapSKAAQLMAGLgfmEHQLRLDVSSFSGGWRMRLNLARTLMSRSDL 169
Cdd:PTZ00243 748 ---------DAARLADAvRVSQLE------------ADLAQLGGGL---ETEIGEKGVNLSGGQKARVSLARAVYANRDV 803
|
170
....*....|.
gi 1348983253 170 LLLDEPTNHLD 180
Cdd:PTZ00243 804 YLLDDPLSALD 814
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-226 |
7.67e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGwTVAHMaqevkaLDMpALDFvlsgdeeywqiqkqlaQ 100
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NG-RVSAL------LEL-GAGF----------------H 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 101 PEqLSDSELAQLHGRfdeIHGYSaPSKAAQLM------AGLG-FMEHQLRldvsSFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:COG1134 101 PE-LTGRENIYLNGR---LLGLS-RKEIDEKFdeivefAELGdFIDQPVK----TYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 174 EptnhldldailWL-----------EDWLNAY---EGTLILISHDRDFLDAVTDHILHIENQELTLY 226
Cdd:COG1134 172 E-----------VLavgdaafqkkcLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
330-486 |
7.96e-05 |
|
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: 44.38 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIkSLVGDLAL-------LNGQ---RKASELLNI--GYFAQHQMDALDGQASPMLQL 397
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLL-NLISGLAQptsggviLEGKqitEPGPDRMVVfqNYSLLPWLTVRENIALAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 SRLADKQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL---- 473
Cdd:TIGR01184 83 LPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiw 161
|
170
....*....|...
gi 1348983253 474 QDFEGAVVLVSHE 486
Cdd:TIGR01184 162 EEHRVTVLMVTHD 174
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-180 |
8.43e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSL---------TRPSGWTVAHMAQEVKALdmPALDFvlsgdeey 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhttTPPSRRPVSMLFQENNLF--SHLTV-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 92 WQ-IQKQLAQPEQLSDSELAQLHgrfdeihgysapsKAAQLMAGLGFMEhqlRLDvSSFSGGWRMRLNLARTLMSRSDLL 170
Cdd:PRK10771 89 AQnIGLGLNPGLKLNAAQREKLH-------------AIARQMGIEDLLA---RLP-GQLSGGQRQRVALARCLVREQPIL 151
|
170
....*....|
gi 1348983253 171 LLDEPTNHLD 180
Cdd:PRK10771 152 LLDEPFSALD 161
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
303-485 |
9.47e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 303 EPTKMSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ--------RKASELL 374
Cdd:PRK13543 3 EPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQiqidgktaTRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 NIGYFAQhqMDALDGQASPMLQLSRLADKQISEA--TLRSFLGSFGFSGERmDTPCESFSGGERARLALALIvWQRPNVL 452
Cdd:PRK13543 83 FMAYLGH--LPGLKADLSTLENLHFLCGLHGRRAkqMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARL-WLSPAPL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1348983253 453 -ILDEPTNHLDLD----MRHALSMALQDfEGAVVLVSH 485
Cdd:PRK13543 159 wLLDEPYANLDLEgitlVNRMISAHLRG-GGAALVTTH 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-176 |
9.55e-05 |
|
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: 44.20 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGG-RVLFQkASMQIHPGWKVGLTGVNGAGKSTLFAALLGelgadegsLTRPSGWTVAHMAQEVkaLDMP 79
Cdd:COG0410 3 MLEVENLHAGYGGiHVLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISG--------LLPPRSGSIRFDGEDI--TGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 80 ALDFVLSGdeeywqiqkqLAQ-PE------QLS-----------DSELAQLHGRFDEIHGYsapskaaqlmaglgF---- 137
Cdd:COG0410 72 PHRIARLG----------IGYvPEgrrifpSLTveenlllgayaRRDRAEVRADLERVYEL--------------Fprlk 127
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1348983253 138 -MEHQLrldVSSFSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:COG0410 128 eRRRQR---AGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-204 |
9.73e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 32 LTGVNGAGKSTLFAALLGELGadeGSLTRPSGWTVAHMAqevKALDMPALDFVLSGDEEYWQI---QKQLAQPEQLSDSE 108
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYALY---GKARSRSKLRSDLIN---VGSEEASVELEFEHGGKRYRIerrQGEFAEFLEAKPSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 109 LAQLHGRFDEIHGY------------SAPSKAAQLMAGLGFMEHQLRL-----DVSSFSGGWRMRLNLARTLMsrsdlLL 171
Cdd:COG0419 102 RKEALKRLLGLEIYeelkerlkeleeALESALEELAELQKLKQEILAQlsgldPIETLSGGERLRLALADLLS-----LI 176
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 172 LDepTNHLDLDAILWLEDWLNAyegtLILISHD 204
Cdd:COG0419 177 LD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
141-255 |
1.04e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 141 QLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILISHDRDFLDAVTDHILHI 218
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHNMQQAARVSDMTAFF 223
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1348983253 219 eNQELTLYTGNYSTF-EVTRSERLAQ--QQQAFEKQVEAR 255
Cdd:PRK14243 224 -NVELTEGGGRYGYLvEFDRTEKIFNspQQQATRDYVSGR 262
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
511-643 |
1.18e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 511 DLQDYAKWLREARQQQINAQTALAQASAstnktaapakvDKEAQRKLAAQRREETRPLRKKIEQCESQIEKIQPRLASIE 590
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELED-----------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 591 EQLAdsslyEASRKEDLLKLMNEQTSLKATLEQAEETMLELMMELETLEQSFQ 643
Cdd:COG1579 80 EQLG-----NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
1.23e-04 |
|
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: 43.87 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHM-AQEVK------ 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILF-GGEDATDVpVQERNvgfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 75 --AL--DMPALDFVLSGDEeywqIQKQLAQPEQlsdselAQLHGRFDEIhgysapskaAQLMAGLGFME---HQLrldvs 147
Cdd:cd03296 82 hyALfrHMTVFDNVAFGLR----VKPRSERPPE------AEIRAKVHEL---------LKLVQLDWLADrypAQL----- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 148 sfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEG----TLILISHDRDFLDAVTDHIL 216
Cdd:cd03296 138 --SGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVV 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
138-243 |
1.33e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.85 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 138 MEHQLRLDVSSF--------SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEGTLI---LISHDRD 206
Cdd:PRK11124 123 EKLLERLRLKPYadrfplhlSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVE 202
|
90 100 110
....*....|....*....|....*....|....*..
gi 1348983253 207 FLDAVTDHILHIENQELtLYTGNYSTFEVTRSERLAQ 243
Cdd:PRK11124 203 VARKTASRVVYMENGHI-VEQGDASCFTQPQTEAFKN 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-180 |
1.59e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 102 EQLSDSELAQLHGRFDEIHGYSAPSKAAQLMAGLGFMEHQLRLdVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:NF000106 99 ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
320-474 |
1.64e-04 |
|
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: 43.76 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 320 GYPGK--SIASKISLQITPSSRIGLLGMNGAGKSTLIKSL-----------------VGDLALLNGQRKasellnIGYFA 380
Cdd:cd03251 9 RYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdsgrilidghdVRDYTLASLRRQ------IGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 381 QhqmDAL--DGQASPMLQLSRL--ADKQISEAT----LRSFLGSF--GFS---GERMDTpcesFSGGERARLALALIVWQ 447
Cdd:cd03251 83 Q---DVFlfNDTVAENIAYGRPgaTREEVEEAAraanAHEFIMELpeGYDtviGERGVK----LSGGQRQRIAIARALLK 155
|
170 180
....*....|....*....|....*..
gi 1348983253 448 RPNVLILDEPTNHLDLDMRHALSMALQ 474
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALE 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-253 |
1.90e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLE----DWLNAYEGTLILISHdRDFLDAVTDHILHIENQEl 223
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH-RIASIKRSDKIVVFNNPD- 1435
|
90 100 110
....*....|....*....|....*....|
gi 1348983253 224 tlYTGNYSTFEVTRSERLAQQQQAFEKQVE 253
Cdd:PTZ00265 1436 --RTGSFVQAHGTHEELLSVQDGVYKKYVK 1463
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
427-527 |
1.93e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 427 PCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAG 503
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
90 100
....*....|....*....|....
gi 1348983253 504 RCTefsGDLQDyakwlREARQQQI 527
Cdd:PRK13549 482 KLK---GDLIN-----HNLTQEQV 497
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
330-462 |
2.15e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 42.62 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLV---------GDLaLLNGQRKASELLNIGYFAQhQMDALDGQAS--PMLQLS 398
Cdd:cd03232 26 ISGYVKPGTLTALMGESGAGKTTLLDVLAgrktagvitGEI-LINGRPLDKNFQRSTGYVE-QQDVHSPNLTvrEALRFS 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 399 rladkqiseATLRsflgsfGFSGErmdtpcesfsggERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03232 104 ---------ALLR------GLSVE------------QRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
422-507 |
2.68e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.29 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 422 ERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD---LDMRHALSMALQDfEGAVVLVSHERQLIASVCDDLL 498
Cdd:PRK14267 141 DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVA 219
|
....*....
gi 1348983253 499 LVHAGRCTE 507
Cdd:PRK14267 220 FLYLGKLIE 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
321-507 |
2.73e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.85 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 321 YPGKSIAS--KISLQITPSSRIGLLGMNGAGKSTlIKSLV--------GDLaLLNGQ----------RKASELL------ 374
Cdd:PRK11176 351 YPGKEVPAlrNINFKIPAGKTVALVGRSGSGKST-IANLLtrfydideGEI-LLDGHdlrdytlaslRNQVALVsqnvhl 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 375 -------NIGYFAQHQmdaldgqaspmlqLSRladKQISEATLRSFLGSFGfsgERMDTPCE--------SFSGGERARL 439
Cdd:PRK11176 429 fndtianNIAYARTEQ-------------YSR---EQIEEAARMAYAMDFI---NKMDNGLDtvigengvLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASVcDDLLLVHAGRCTE 507
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKA-DEILVVEDGEIVE 558
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-216 |
2.78e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.11 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTrPSGWTVAhmAQEVKALDMPALDFVLSGDEEYW----QIQK 96
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII-IDGVDIT--DKKVKLSDIRKKVGLVFQYPEYQlfeeTIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 97 QLA-QPEQLSDSElaqlhgrfDEIHGYSapsKAAQLMAGLGFMEHQlrlDVSSF--SGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:PRK13637 104 DIAfGPINLGLSE--------EEIENRV---KRAMNIVGLDYEDYK---DKSPFelSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1348983253 174 EPTNHLD---LDAILWL-EDWLNAYEGTLILISHDRDFLDAVTDHIL 216
Cdd:PRK13637 170 EPTAGLDpkgRDEILNKiKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-645 |
2.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 517 KWLREARQQQINAQTALAQASASTNKTAAPAKVDKEAQRKLAAQRREETRPLRKKIEQCESQIEKIQPRLASIEEQLADS 596
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1348983253 597 SLYEASRKEDLLKLMNEQTSLKATLEQAEETMLELMMELETLEQSFQNS 645
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
147-215 |
3.06e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.91 E-value: 3.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 147 SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILISHDRDFLDAVTDHI 215
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYV 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
330-622 |
3.18e-04 |
|
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: 44.17 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQ--RKASellnIGYFAQH--------QMDALDGQA-------S 392
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHvhMKGS----VAYVPQQawiqndslRENILFGKAlnekyyqQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 393 PMLQLSRLADKQISEATLRSFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMA 472
Cdd:TIGR00957 733 VLEACALLPDLEILPSGDRTEIGEKGVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 473 LQDFEGAV-----VLVSHERQLIASVcdDLLLVHAGRCTEFSGDLQD-------YAKWLRE--ARQQQINAQTALAQASA 538
Cdd:TIGR00957 803 VIGPEGVLknktrILVTHGISYLPQV--DVIIVMSGGKISEMGSYQEllqrdgaFAEFLRTyaPDEQQGHLEDSWTALVS 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 539 STNKTAAPAK--------VDKEAQRKLAAQrreetrplrkkieqcESQIEKIQPRLASIEEqladssLYEASRKEDLLKL 610
Cdd:TIGR00957 881 GEGKEAKLIEngmlvtdvVGKQLQRQLSAS---------------SSDSGDQSRHHGSSAE------LQKAEAKEETWKL 939
|
330
....*....|..
gi 1348983253 611 MNEQTSLKATLE 622
Cdd:TIGR00957 940 MEADKAQTGQVE 951
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
144-206 |
3.20e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.15 E-value: 3.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 144 LDVSSF--SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLNAYEGTLILISHDRD 206
Cdd:PRK13651 159 LQRSPFelSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
132-206 |
3.44e-04 |
|
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: 43.02 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 132 MAGLGFMEHQLrldVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLnayEGTLILISHD 204
Cdd:cd03294 147 LVGLEGWEHKY---PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAEL---QKTIVFITHD 220
|
..
gi 1348983253 205 RD 206
Cdd:cd03294 221 LD 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
138-213 |
3.80e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 42.72 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 138 MEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY----EGTLILISHDRDFLDAVTD 213
Cdd:PRK14258 140 IKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLSD 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-226 |
3.87e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.87 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 29 KVGLTGVNGAGKSTLFAALLGELGADEGS-LTRPSGWTVAHMaQEVKALdmPALDFVLSGDeeywqiqkQLAQPEQLSDS 107
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSvLIRGEPITKENI-REVRKF--VGLVFQNPDD--------QIFSPTVEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 108 ELAQLHGRFDEihgYSAPSKAAQLMAGLGFMEHQLRLDvSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDA 183
Cdd:PRK13652 101 AFGPINLGLDE---ETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1348983253 184 ILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQELTLY 226
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
511-645 |
4.48e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 511 DLQDYAKWLREARQQQINAQTALAQASASTNKTAAPAKVDKEAQRKLAAQRREETRPLRKKIEQCESQIEKIQPRLASIE 590
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 591 EQLAdsslyeasrkedllKLMNEQTSLKATLEQAEETMLELMMELETLEQSFQNS 645
Cdd:TIGR02168 393 LQIA--------------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
521-641 |
4.75e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 521 EARQQQINAQTALAQASASTNKTAApAKVDKEAQRKLAAQRREETR---------PLRKKIEQCESQIEKIQPRLASIEE 591
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLEL-EELELELEEAQAEEYELLAElarleqdiaRLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 592 QLADSSLYEASRKEDLLKLMNEQTSLKATLEQAEETMLELMMELETLEQS 641
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
330-505 |
5.46e-04 |
|
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: 43.36 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGQRKASellnigyfaqhqmdaldGQASPMLQLSRLADKQISEAT 409
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS-----------------GRISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 410 LrsflgsFGFS----------------------GERMDTPCE----SFSGGERARLALALIVWQRPNVLILDEPTNHLDL 463
Cdd:TIGR01271 508 I------FGLSydeyrytsvikacqleedialfPEKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1348983253 464 DMRHALsmalqdFEGAV--VLVSHERQLIASV------CDDLLLVHAGRC 505
Cdd:TIGR01271 582 VTEKEI------FESCLckLMSNKTRILVTSKlehlkkADKILLLHEGVC 625
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
127-220 |
6.38e-04 |
|
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: 41.71 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 127 KAAQLMAGLGFMEHQLRLDvSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLNAYEG-TLILIS 202
Cdd:cd03298 108 AIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEMLDLVLDLHAETKmTVLMVT 186
|
90
....*....|....*...
gi 1348983253 203 HDRDFLDAVTDHILHIEN 220
Cdd:cd03298 187 HQPEDAKRLAQRVVFLDN 204
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
432-504 |
6.94e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.14 E-value: 6.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
432-504 |
7.88e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 42.01 E-value: 7.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIrelqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-550 |
8.60e-04 |
|
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: 42.69 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 323 GKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVGDL------ALLNGQRKASEL----LNIGYFAQHQM--DALDgQ 390
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLpptsgtVLVGGKDIETNLdavrQSLGMCPQHNIlfHHLT-V 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 391 ASPMLQLSRLADKQISEATLR--SFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEmeAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 469 LSMALQDFEGA--VVLVSHERQLIASVCDDLLLVHAGR--CTEFSGDLQD------YAKWLREAR--QQQINAQTALAQA 536
Cdd:TIGR01257 1100 IWDLLLKYRSGrtIIMSTHHMDEADLLGDRIAIISQGRlyCSGTPLFLKNcfgtgfYLTLVRKMKniQSQRGGCEGTCSC 1179
|
250
....*....|....
gi 1348983253 537 SASTNKTAAPAKVD 550
Cdd:TIGR01257 1180 TSKGFSTRCPARVD 1193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
150-220 |
9.03e-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: 42.01 E-value: 9.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIL-WLEDWLNAYEGTLILISHDRDFLDAVTDHILHIEN 220
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkAEILpYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
307-359 |
9.54e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 9.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 307 MSSPLLTLDQAEIGYPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG 359
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
329-492 |
9.57e-04 |
|
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: 40.38 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 329 KISLQITPSSRIGLLGMNGAGKSTLIKSLvgdLALLNGQRKASELLNigyFAQHQMDALDgqaspmlQLSRLADKQISEA 408
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPK---FSRNKLIFID-------QLQFLIDVGLGYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 409 TLrsflgsfgfsGERMDTpcesFSGGERARLALA--LIVWQRPNVLILDEPTNHLDL-DMRHALSM--ALQDFEGAVVLV 483
Cdd:cd03238 80 TL----------GQKLST----LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQqDINQLLEVikGLIDLGNTVILI 145
|
....*....
gi 1348983253 484 SHERQLIAS 492
Cdd:cd03238 146 EHNLDVLSS 154
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
520-630 |
1.04e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 520 REARQQQINAQTALAQASASTNKTAAPAKVDKEAQRKLA------AQRREETRPLRKKIEQCESQIEKIQPRLASIEEQL 593
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAeleselEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
90 100 110
....*....|....*....|....*....|....*..
gi 1348983253 594 ADSSLYEASRKEDLLKLMNEQTSLKATLEQAEETMLE 630
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
150-220 |
1.05e-03 |
|
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: 40.91 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL----NAYEGTLILISHDRDFLDAVTDHILHIEN 220
Cdd:TIGR01184 116 SGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDVDEALLLSDRVVMLTN 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-181 |
1.10e-03 |
|
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: 41.07 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT-------------RPSGWTVAH 68
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILldgkditnlpphkRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 69 MAQevkaldMPALDfvlsgdeeywqIQKQLAQPEQLSDSELAQLHGRFDEihgysapskaaqlMAGLGFMEHQLRLDVSS 148
Cdd:cd03300 81 YAL------FPHLT-----------VFENIAFGLRLKKLPKAEIKERVAE-------------ALDLVQLEGYANRKPSQ 130
|
170 180 190
....*....|....*....|....*....|...
gi 1348983253 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-223 |
1.13e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 41.35 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTL---FAALL----GELGADEGSLTRPSGwtvahmAQEVKALDMP-ALDFVLSgdeeyw 92
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLmqhFNALLkpssGTITIAGYHITPETG------NKNLKKLRKKvSLVFQFP------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 93 qiQKQLAQPEQLSDSELAQLHGRFDEihgYSAPSKAAQLMAGLGFMEHQLRLDVSSFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:PRK13641 95 --EAQLFENTVLKDVEFGPKNFGFSE---DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 173 DEPTNHLDLDAILWLEDWLNAYEG---TLILISHDRDFLDAVTDHILHIENQEL 223
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
1.14e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 41.62 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT-------------RPSGwTVA 67
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgrdvtglppekRNVG-MVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 68 -------HM--AQEV----KALDMPAldfvlsgdeeywqiqkqlaqpeqlsdselaqlhgrfDEIHgysapSKAAQLMA- 133
Cdd:COG3842 84 qdyalfpHLtvAENVafglRMRGVPK------------------------------------AEIR-----ARVAELLEl 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 134 -GLGFME----HQLrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA----ILWLEDWLNAYEGTLILISHD 204
Cdd:COG3842 123 vGLEGLAdrypHQL-------SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELGITFIYVTHD 195
|
250
....*....|...
gi 1348983253 205 RDflDAVT--DHI 215
Cdd:COG3842 196 QE--EALAlaDRI 206
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 |
1.15e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLT---RPSGWT---------VAHMAQEvkaldmpaLDFVlsgd 88
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILidgQEMRFAsttaalaagVAIIYQE--------LHLV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 89 eeywqiqkqlaqPEqLSDSE---LAQLHGRFDEIHGYSAPSKAAQLMAGLGfmehqLRLD----VSSFSGGWRMRLNLAR 161
Cdd:PRK11288 92 ------------PE-MTVAEnlyLGQLPHKGGIVNRRLLNYEAREQLEHLG-----VDIDpdtpLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 162 TLMSRSDLLLLDEPTNHL---DLDAILWLEDWLNAyEGTLIL-ISHDRDFLDAVTDHI 215
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLsarEIEQLFRVIRELRA-EGRVILyVSHRMEEIFALCDAI 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
521-640 |
1.29e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 521 EARQQQINAQTALAQASASTNKTAAPAKVDKEAQRKLAaQRREETRPLRKKIEQCESQIEKIQPRLASIEEQLADSSLYE 600
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1348983253 601 ASRKEDLLKLMNEQTSLKATLEQAEETMLELMMELETLEQ 640
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
330-507 |
1.40e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.93 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 330 ISLQITPSSRIGLLGMNGAGKSTLIKSLVGDLALLNGqrkasELL---------NIGYFAQH-QMDALDGQAS--PMLQL 397
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-----ELLiddhplhfgDYSYRSQRiRMIFQDPSTSlnPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 398 SRLAD---------------KQISEaTLRSFlgsfGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK15112 107 SQILDfplrlntdlepeqreKQIIE-TLRQV----GLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1348983253 463 LDMRHA---LSMALQDFEG-AVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK15112 182 MSMRSQlinLMLELQEKQGiSYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-180 |
1.55e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.49 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGG-RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAAL-------LGEL---GADEGSLTRPS-GWTVAHM 69
Cdd:PRK13657 335 VEFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRIlidGTDIRTVTRASlRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 70 AQEvkaldmpALDFVLSgDEEYWQIQKQLAQPEQLSDselaqlhgrfdeihgysapskAAQLMAGLGFMEHQ-LRLDV-- 146
Cdd:PRK13657 415 FQD-------AGLFNRS-IEDNIRVGRPDATDEEMRA---------------------AAERAQAHDFIERKpDGYDTvv 465
|
170 180 190
....*....|....*....|....*....|....*...
gi 1348983253 147 ----SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK13657 466 gergRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
432-491 |
1.69e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 40.87 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1348983253 432 SGGERARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIA 491
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEVA 205
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-204 |
1.83e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.85 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1348983253 143 RLDVSSF--SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAYEG--TLILISHD 204
Cdd:PRK14271 156 RLSDSPFrlSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
519-640 |
1.92e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 519 LREARQQQINAQTALAQ-----ASASTNKTAAPAKVDKEAQRKLAAQRREET-----RPLRKKIEQCESQIEKIQPRLAS 588
Cdd:TIGR02168 325 LEELESKLDELAEELAEleeklEELKEELESLEAELEELEAELEELESRLEEleeqlETLRSKVAQLELQIASLNNEIER 404
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 589 IEEQLADSslyeASRKEdllKLMNEQTSLKATLEQAEetMLELMMELETLEQ 640
Cdd:TIGR02168 405 LEARLERL----EDRRE---RLQQEIEELLKKLEEAE--LKELQAELEELEE 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
521-644 |
2.04e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 521 EARQQQINAQTALAQASASTNKTAAPAKVDKEAQRKLAAQRrEETRPLRKKIEQCESQIEKIQPRLASIEEQ-------L 593
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR-KDLARLEAEVEQLEERIAQLSKELTELEAEieeleerL 770
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 594 ADSSLYEASRKEDLLKLMNEQTSLKATLEQAEETMLELMMELETLEQSFQN 644
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
431-536 |
2.16e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 431 FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVS----HERQLIA---SVCDDLLLVH 501
Cdd:NF000106 145 YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTtqymEEAEQLAhelTVIDRGRVIA 224
|
90 100 110
....*....|....*....|....*....|....*.
gi 1348983253 502 AGRCTEFSGDLQDYAKWLREARQQQINAQT-ALAQA 536
Cdd:NF000106 225 DGKVDELKTKVGGRTLQIRPAHAAELDRMVgAIAQA 260
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
149-223 |
2.25e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.79 E-value: 2.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1348983253 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL----NAYEGTLILISHDRDFLDAVTDHILHIENQEL 223
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
432-462 |
2.25e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.45 E-value: 2.25e-03
10 20 30
....*....|....*....|....*....|.
gi 1348983253 432 SGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-180 |
2.46e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 40.07 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 1 MIQFDQVSLRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpsgwtvahmaqEVKALDMPA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL-----------DGKPVEGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 LDF-VLSGDEEY--WQ-IQKQLAQPEQLSDSELAQLHGRfdeihgysapskAAQLMAGLGFMEHQLRLdVSSFSGGWRMR 156
Cdd:PRK11248 70 AERgVVFQNEGLlpWRnVQDNVAFGLQLAGVEKMQRLEI------------AHQMLKKVGLEGAEKRY-IWQLSGGQRQR 136
|
170 180
....*....|....*....|....
gi 1348983253 157 LNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALD 160
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
119-233 |
2.57e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.60 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 119 IHGYSAPSKAAQLMAGLGFMEHqlRLDVSSF--SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEd 189
Cdd:PRK13631 147 VKKSEAKKLAKFYLNKMGLDDS--YLERSPFglSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgehemMQLILDAK- 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1348983253 190 wlnAYEGTLILISHDRDFLDAVTDHILHIENQELTLYTGNYSTF 233
Cdd:PRK13631 224 ---ANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
550-641 |
2.94e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 550 DKEAQRKLAAQRREETRPLRKKIEQCESQIEKIQPRLASIEEQLADSSLYEASRKEDLLKLMNEQTSLKATLEQAEETML 629
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
90
....*....|..
gi 1348983253 630 ELMMELETLEQS 641
Cdd:TIGR02169 776 KLEEALNDLEAR 787
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-223 |
3.07e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 40.06 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 13 GRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLTRpSGWTVAHMAQE-VKALDMPALDFVLSGDeey 91
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKYDKKSlLEVRKTVGIVFQNPDD--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 92 wqiqkQLAQPEQLSDSELAQLHGRF--DEIHGYSAPSKAAQLMAGlgFME---HQLrldvssfSGGWRMRLNLARTLMSR 166
Cdd:PRK13639 90 -----QLFAPTVEEDVAFGPLNLGLskEEVEKRVKEALKAVGMEG--FENkppHHL-------SGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1348983253 167 SDLLLLDEPTNHLD---LDAILWLEDWLNAyEGTLILIS-HDRDFLDAVTDHILHIENQEL 223
Cdd:PRK13639 156 PEIIVLDEPTSGLDpmgASQIMKLLYDLNK-EGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
133-216 |
3.13e-03 |
|
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: 39.91 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 133 AGLGFMehQLRLDVSSFSGGWRMRLNLARTLMSRSD---LLLLDEPTNHLDLDAILWLEDWLN--AYEG-TLILISHDRD 206
Cdd:cd03271 156 VGLGYI--KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQrlVDKGnTVVVIEHNLD 233
|
90
....*....|
gi 1348983253 207 FLdAVTDHIL 216
Cdd:cd03271 234 VI-KCADWII 242
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-216 |
3.20e-03 |
|
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: 40.77 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 134 GLGFMehQLRLDVSSFSGGWRMRLNLARTLMSRSD---LLLLDEPTNHLDLDAILWLEDWLN--AYEG-TLILISHDRDF 207
Cdd:TIGR00630 817 GLGYI--RLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQrlVDKGnTVVVIEHNLDV 894
|
....*....
gi 1348983253 208 LdAVTDHIL 216
Cdd:TIGR00630 895 I-KTADYII 902
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-223 |
3.36e-03 |
|
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: 39.59 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVS-LRRGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALlgelgadeGSLTRPSGWTVAHMAQEVKALDMPA 80
Cdd:cd03295 1 IEFENVTkRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI--------NRLIEPTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 81 L----DFVLS--GDEEYWQIQKQLAQPEQLSDSELAQLHGRFDEIHGysapskaaqlMAGL---GFME---HQLrldvss 148
Cdd:cd03295 73 LrrkiGYVIQqiGLFPHMTVEENIALVPKLLKWPKEKIRERADELLA----------LVGLdpaEFADrypHEL------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 149 fSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLNAyegTLILISHDRDFLDAVTDHILHIENQ 221
Cdd:cd03295 137 -SGGQQQRVGVARALAADPPLLLMDEPFGALDpitrdqlQEEFKRLQQELGK---TIVFVTHDIDEAFRLADRIAIMKNG 212
|
..
gi 1348983253 222 EL 223
Cdd:cd03295 213 EI 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-180 |
3.36e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.39 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGR--VLFQKASMQIHPGWKVGLTGVNGAGKSTLfAALLGEL-GADEGSLTrpsgwtvahmaqevkaLDM 78
Cdd:PRK11176 342 IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTI-ANLLTRFyDIDEGEIL----------------LDG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 PAL-DFVLSgdeeywQIQKQLAQPEQlsdselaQLHGRFDEIHG---------YSAPS--KAAQLMAGLGF---MEHQLR 143
Cdd:PRK11176 405 HDLrDYTLA------SLRNQVALVSQ-------NVHLFNDTIANniayarteqYSREQieEAARMAYAMDFinkMDNGLD 471
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1348983253 144 LDV----SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11176 472 TVIgengVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
148-221 |
3.43e-03 |
|
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: 39.09 E-value: 3.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIENQ 221
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-204 |
3.57e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.68 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 14 RVLFQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELgadegsltrPSGwtVAHMAQEVKALDMPALDFVLSGdeeywq 93
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL---------PAG--VRQTAGRVLLDGKPVAPCALRG------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 94 iqKQLAQPEQLSDSELAQL-----HGRfDEIHGYSAPSKAAQLMA-----GLGFMEHQLRLDVSSFSGGWRMRLNLARTL 163
Cdd:PRK10418 79 --RKIATIMQNPRSAFNPLhtmhtHAR-ETCLALGKPADDATLTAaleavGLENAARVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1348983253 164 MSRSDLLLLDEPTNHLDLDA---ILWLEDWLNAYEGT-LILISHD 204
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAqarILDLLESIVQKRALgMLLVTHD 200
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
331-507 |
3.62e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.02 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 331 SLQITPSSRIGLLGMNGAGKSTLIKSL--------------------VGDLALLNGQRKASELLNIGYFAQHQMDALDGQ 390
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptrgqvlidgvdiakISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 391 ASPMlQLSRLADKQISEATLRSfLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:PRK10070 128 AFGM-ELAGINAEERREKALDA-LRQVGLENYAHSYPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1348983253 471 MALQDFEG----AVVLVSHERQLIASVCDDLLLVHAGRCTE 507
Cdd:PRK10070 205 DELVKLQAkhqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
430-505 |
3.87e-03 |
|
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: 39.84 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsmalqdFEGAV--VLVSHERQLIAS------VCDDLLLVH 501
Cdd:cd03291 159 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI------FESCVckLMANKTRILVTSkmehlkKADKILILH 232
|
....
gi 1348983253 502 AGRC 505
Cdd:cd03291 233 EGSS 236
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-218 |
3.90e-03 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 39.28 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 21 SMQIHPGWKVGLTGVNGAGKSTLFAALLG-------------------ELGADE----G---SLTRP---SGWTVAH--- 68
Cdd:COG0396 20 NLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyevtsgsilldgedilELSPDEraraGiflAFQYPveiPGVSVSNflr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 69 -MAQEVKALDMPALDFVlsgdeeywqiqkqlaqpeqlsdselaqlhgrfdeihgysapSKAAQLMAGLGFMEHQLRLDV- 146
Cdd:COG0396 100 tALNARRGEELSAREFL-----------------------------------------KLLKEKMKELGLDEDFLDRYVn 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 147 SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY---EGTLILISHDRDFLDAVTDHILHI 218
Cdd:COG0396 139 EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILDYIKPDFVHV 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
390-504 |
4.18e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.01 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 390 QASPMLQLSRLADKQiseatlrsflgsfgfsgermdtPcESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LDM 465
Cdd:PRK11000 116 QVAEVLQLAHLLDRK----------------------P-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQM 172
|
90 100 110
....*....|....*....|....*....|....*....
gi 1348983253 466 RHALSMALQDFEGAVVLVSHERQLIASVCDDLLLVHAGR 504
Cdd:PRK11000 173 RIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
427-498 |
4.43e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 4.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 427 PCESFSGGERARLALA---LIVWQRPNVLILDEPTNHLDLDMRHALSMALQD--FEGAVVLVSHERQLIASVCDDLL 498
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSltHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-209 |
4.51e-03 |
|
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: 38.46 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 134 GLGFMehQLRLDVSSFSGGWRMRLNLARTLMSRSD--LLLLDEPTNHLDLDAILWLEDWLNAY--EG-TLILISHDRDFL 208
Cdd:cd03238 75 GLGYL--TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidLGnTVILIEHNLDVL 152
|
.
gi 1348983253 209 D 209
Cdd:cd03238 153 S 153
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
321-359 |
5.16e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 5.16e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1348983253 321 YPGKSIASKISLQITPSSRIGLLGMNGAGKSTLIKSLVG 359
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFG 46
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
150-180 |
5.38e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 39.63 E-value: 5.38e-03
10 20 30
....*....|....*....|....*....|.
gi 1348983253 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
127-216 |
5.59e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.34 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 127 KAAQLMAGLGFMEHQLRLDV--SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLNAyegT 197
Cdd:PRK11022 130 RAIDLLNQVGIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQQKENM---A 206
|
90
....*....|....*....
gi 1348983253 198 LILISHDRDFLDAVTDHIL 216
Cdd:PRK11022 207 LVLITHDLALVAEAAHKII 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
147-215 |
5.63e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 39.30 E-value: 5.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1348983253 147 SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL----NAYEGTLILISHDRDFLDAVTDHI 215
Cdd:PRK10851 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRV 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-180 |
5.67e-03 |
|
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: 38.75 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLRRGGR---VLfQKASMQIHPGWKVGLTGVNGAGKSTLFAALLGELGADEGSLtrpsgwtvahmaqEVKALDM 78
Cdd:cd03251 1 VEFKNVTFRYPGDgppVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI-------------LIDGHDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 79 PalDFVLSgdeeywQIQKQLAQPEQ---LSDSELAQ--LHGRFDEIHgySAPSKAAQLMAGLGF---MEHQLRLDV---- 146
Cdd:cd03251 67 R--DYTLA------SLRRQIGLVSQdvfLFNDTVAEniAYGRPGATR--EEVEEAARAANAHEFimeLPEGYDTVIgerg 136
|
170 180 190
....*....|....*....|....*....|....
gi 1348983253 147 SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03251 137 VKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-203 |
5.70e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 39.13 E-value: 5.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 143 RLDV--SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLNAY--EGTLILISH 203
Cdd:PRK14247 139 RLDApaGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTH 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-203 |
5.85e-03 |
|
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: 38.67 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 2 IQFDQVSLR---RGGRVLFQKASMQIHPGWKVGLTGVNGAGKSTlFAALL--------GEL---GADEGSLTRPsgWTVA 67
Cdd:cd03249 1 IEFKNVSFRypsRPDVPILKGLSLTIPPGKTVALVGSSGCGKST-VVSLLerfydptsGEIlldGVDIRDLNLR--WLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 68 HMA---QEVKALDMPALDFVLSGDEEywqiqkqLAQPEQLSDSELAQLHgrfDEI----HGYSAP--SKAAQLmaglgfm 138
Cdd:cd03249 78 QIGlvsQEPVLFDGTIAENIRYGKPD-------ATDEEVEEAAKKANIH---DFImslpDGYDTLvgERGSQL------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1348983253 139 ehqlrldvssfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLN-AYEG-TLILISH 203
Cdd:cd03249 141 -----------SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDrAMKGrTTIVIAH 196
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
432-485 |
6.09e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 38.92 E-value: 6.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG----AVVLVSH 485
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH 203
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
519-635 |
6.15e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 39.23 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 519 LREARQQQInaQTALAQASASTNKTAAPAKVDKEAQRKLAAQRREETrpLRKKIEQCESQIEKIQprlASIEEQLADS-- 596
Cdd:PRK06669 38 LREEEEEQV--EQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEE--LLKKTDEASSIIEKLQ---MQIEREQEEWee 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1348983253 597 ---SLYEASRKE-----------DLLKLMNEQTS------------LKATLEQAEETMLELMMEL 635
Cdd:PRK06669 111 eleRLIEEAKAEgyeegyekgreEGLEEVRELIEqlnkiieklikkREEILESSEEEIVELALDI 175
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-220 |
6.68e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 6.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 146 VSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLNAYEGTLILISHDRDFLDAVTDHILHIEN 220
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSN 466
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
513-582 |
7.85e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 37.29 E-value: 7.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1348983253 513 QDYAKWLREARQQqinAQTALAQASASTNKTAAP--AKVDKEAQRKLAAQRREETRPLRKKIEQCESQIEKI 582
Cdd:PRK07353 60 AQYEQQLASARKQ---AQAVIAEAEAEADKLAAEalAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDAL 128
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
562-645 |
8.03e-03 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 38.82 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1348983253 562 REETRPLRKKIEQCESQIEKIQPRLASIEeqladsslyEASRKEDLLKLMNEQTSLKATLEQAEETMLELMMELETLEQS 641
Cdd:pfam03961 155 KEKLEELEKELEELEEELEKLKKRLKKLP---------KKARGQLPPEKREQLEKLLETKNKLSEELEELEEELKELKEE 225
|
....
gi 1348983253 642 FQNS 645
Cdd:pfam03961 226 LESL 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
146-180 |
8.48e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including 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: 213200 [Multi-domain] Cd Length: 202 Bit Score: 38.01 E-value: 8.48e-03
10 20 30
....*....|....*....|....*....|....*
gi 1348983253 146 VSSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03233 116 VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
147-220 |
8.94e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 38.56 E-value: 8.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1348983253 147 SSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLNAYEGTLILISHDRDFLdAVTDHILHIEN 220
Cdd:PRK13650 139 ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKN 215
|
|
| |
