|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-622 |
0e+00 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 727.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKALDMPA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 IDFVLSGDEEYWDIQNKLAQPEQLTDSD-LAKLHGRFDEIHGYSAPSKAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNL 159
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANERNDGHaIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFETTRSE 239
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 240 RLAQQQQAFEKQQEARAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDTPFTFSFREPTKMSSPLLTLENASI 319
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 320 GYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDALDGQASPMLQLAR 399
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 400 IADKQiSEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA 479
Cdd:PRK10636 401 LAPQE-LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 480 VVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDYAKWLREARQQQINAQTAIEQNNSSSaapapAKVDKEAQRKEaAR 559
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANS-----AQARKDQKRRE-AE 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 560 RREQTRPIRKNIEKVESQIEKLQPRLAEIEEALADTSLYEANRKDDLLKLMNEQTELKAKLEQ 622
Cdd:PRK10636 554 LRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRKAELTACLQQQASAKSGLEE 616
|
|
| 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: 684.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 4 FDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKALD-MPAID 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDdLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 83 FVLSGDEEYWDIQNKLAQPEQLTDSD------LAKLHGRFDEIHGYSAPSKAAQLMAGLGFLEHQLRLNVASFSGGWRMR 156
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPdedlerLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFETT 236
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 237 RSERLAQQQQAFEKQQEARAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDTPFTFSFREPTKMSSPLLTLEN 316
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 317 ASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQmDALDGQASPMLQ 396
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 397 LARIADKQiSEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF 476
Cdd:COG0488 400 LRDGAPGG-TEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446536636 477 EGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDYAKW 518
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-520 |
8.92e-121 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 375.35 E-value: 8.92e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALlgSLGADEGSltrPSVWTVAHMAQEVKALDMPAI 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM--AMHAIDGI---PKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFVLSGD--------EEYWDIQNKLAQPEQLTDSD-----------------LAKLHGRFDEIHGYSAPSKAAQLMAGLG 136
Cdd:PLN03073 253 QCVLNTDiertqlleEEAQLVAQQRELEFETETGKgkgankdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 137 FLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 217 HIENQELTLYTGNYSTFETTRSERLAQQQQAFEKQQEARAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDTP 296
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 297 FTFSFREPT-KMSSPLLTLENASIGY-GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELL 374
Cdd:PLN03073 493 YKFEFPTPDdRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 NIGYFAQHQMDALDGQASPMLQLARIAdKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCF-PGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 455 DEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDYAKWLR 520
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQ 717
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-515 |
1.92e-104 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 326.85 E-value: 1.92e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEG--SLTrPSVwTVAHMAQEVKAL-D 77
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGnvSLD-PNE-RLGKLRQDQFAFeE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 MPAIDFVLSGDEEYWDIQNK----LAQPEqLTDSD---LAKLHGRFDEIHGYSAPSKAAQLMAGLGFLEHQ---LRLNVA 147
Cdd:PRK15064 79 FTVLDTVIMGHTELWEVKQErdriYALPE-MSEEDgmkVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQhygLMSEVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 148 SfsgGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYT 227
Cdd:PRK15064 158 P---GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 228 GNYSTFETTRS---ERLAQQQQAFEKQQearAHLQKFIDRFKAKATKARQAQSRIKQLERMQ--QLAPAHVDTPFtFSFR 302
Cdd:PRK15064 235 GNYDEYMTAATqarERLLADNAKKKAQI---AELQSFVSRFSANASKAKQATSRAKQIDKIKleEVKPSSRQNPF-IRFE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 303 EPTKMSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQH 382
Cdd:PRK15064 311 QDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 QMDALDGQASPMLQLARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK15064 391 HAYDFENDLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 463 LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDY 515
Cdd:PRK15064 471 MESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-520 |
1.44e-77 |
|
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: 257.17 E-value: 1.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGsLGADEGSLTRPSV-WTVAHMAQE--------VKALDMPAID 82
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFNGEARPQPgIKVGYLPQEpqldptktVRENVEEGVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 83 FVLSGDEEYWDIQNKLAQPEQLTDSDL---AKLHGRFDEIHGYSAPSKAAQLMaglgfleHQLRL-----NVASFSGGWR 154
Cdd:TIGR03719 95 EIKDALDRFNEISAKYAEPDADFDKLAaeqAELQEIIDAADAWDLDSQLEIAM-------DALRCppwdaDVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFE 234
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 235 TTRSERLAQQQQafekqqeARAHLQKFIDR---FKAKATKARQAQS--RIKQLERMQQLApahvdtpftFSFREPT---- 305
Cdd:TIGR03719 248 EQKQKRLEQEEK-------EESARQKTLKReleWVRQSPKGRQAKSkaRLARYEELLSQE---------FQKRNETaeiy 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 306 -----KMSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFA 380
Cdd:TIGR03719 312 ippgpRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 381 QHQmDALDG------QASPMLQLARIADKQISEatlRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:TIGR03719 392 QSR-DALDPnktvweEISGGLDIIKLGKREIPS---RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 455 DEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHG-GKCTEFEGDLQDYAKWLR 520
Cdd:TIGR03719 468 DEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGdSHVEWFEGNFSEYEEDKK 534
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-623 |
1.56e-76 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 256.42 E-value: 1.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 16 LFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEV-KALDMPAIDFVLSGDEE---- 90
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPpRNVEGTVYDFVAEGIEEqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 91 ---YWDIQNKLAQ-PEQLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGfLEHQLRLnvASFSGGWRMRLNLARTLMSR 166
Cdd:PRK11147 98 lkrYHDISHLVETdPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLG-LDPDAAL--SSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 167 SDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFETTRSERLAQQQQ 246
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 247 AFEKQQEARAHLQKFIdRFKAKATKARQaQSRIKQL-----ERMQQL-----APAHVDTpftfsfrepTKMSSPLL-TLE 315
Cdd:PRK11147 255 QNAEFDRKLAQEEVWI-RQGIKARRTRN-EGRVRALkalrrERSERRevmgtAKMQVEE---------ASRSGKIVfEME 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 316 NASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQmDALDGQASPML 395
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-AELDPEKTVMD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 396 QLARiaDKQISEATLR-----SFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:PRK11147 403 NLAE--GKQEVMVNGRprhvlGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 471 MALQDFEGAVVLVSHERQLIASVCDELLLVHG-GKCTEFEGDLQDyakwlreARQQQINAQTAIEQNNSSSAAPAPAKVD 549
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGnGKIGRYVGGYHD-------ARQQQAQYLALKQPAVKKKEEAAAPKAE 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 550 KEAQRKEAARRREQtrpirKNIEKVESQIEKLQPRLAEIEEALADTSLYeANRKDDLLKLMNEQTELKAKLEQY 623
Cdd:PRK11147 554 TVKRSSKKLSYKLQ-----RELEQLPQLLEDLEAEIEALQAQVADADFF-SQPHEQTQKVLADLADAEQELEVA 621
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-521 |
1.24e-69 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 236.17 E-value: 1.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGsLGADEGSLTRPSV-WTVAHMAQEVKaLD---------MPAI 81
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKEFEGEARPAPgIKVGYLPQEPQ-LDpektvrenvEEGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFVLSGDEEYWDIQNKLAQPEQLTD---SDLAKLHGRFDEIHGYSAPSKAAQLMAGLgflehqlRL-----NVASFSGGW 153
Cdd:PRK11819 96 AEVKAALDRFNEIYAAYAEPDADFDalaAEQGELQEIIDAADAWDLDSQLEIAMDAL-------RCppwdaKVTKLSGGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 154 RMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTF 233
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 234 ETTRSERLaqqqqafEKQQEARAHLQKFIDR---FKAKATKARQAQS--RIKQLERMQQLApahvdtpftFSFREPT--- 305
Cdd:PRK11819 249 LEQKAKRL-------AQEEKQEAARQKALKReleWVRQSPKARQAKSkaRLARYEELLSEE---------YQKRNETnei 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 306 ------KMSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYF 379
Cdd:PRK11819 313 fippgpRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQHQmDALDGQA------SPMLQLARIADKQISEatlRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK11819 393 DQSR-DALDPNKtvweeiSGGLDIIKVGNREIPS---RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 454 LDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHG-GKCTEFEGDLQDYAKWLRE 521
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGdSQVEWFEGNFQEYEEDKKR 537
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-222 |
1.54e-55 |
|
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: 185.34 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQevkaldmpai 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 dfvlsgdeeywdiqnklaqpeqltdsdlaklhgrfdeihgysapskaaqlmaglgflehqlrlnvasFSGGWRMRLNLAR 161
Cdd:cd03221 71 -------------------------------------------------------------------LSGGEKMRLALAK 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQE 222
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-234 |
3.64e-52 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 187.96 E-value: 3.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTR-PSVwTVAHMAQEVKALD-- 77
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETV-KIGYFDQHQEELDpd 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 MPAIDFVLSGDEEywdiqnklaqpeqltdsdlaklhgrFDEIHgysapskAAQLMAGLGFLEHQLRLNVASFSGGWRMRL 157
Cdd:COG0488 394 KTVLDELRDGAPG-------------------------GTEQE-------VRGYLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFE 234
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
312-504 |
8.34e-50 |
|
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: 169.94 E-value: 8.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQhqmdaldgqa 391
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 spmlqlariadkqiseatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 446536636 472 ALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
314-598 |
5.28e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 173.33 E-value: 5.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 314 LENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQH----------- 382
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEppldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 --------------QMDALDGQ-ASPMLQLARIADKQI---------SEATLRSFLGSFGFSGERMDTPCESFSGGERAR 438
Cdd:COG0488 81 tvldgdaelraleaELEELEAKlAEPDEDLERLAELQEefealggweAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 439 LALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGdlqDYAKW 518
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPG---NYSAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 519 LrEARQQQINAQTAIEqnnsssaapapAKVDKEAQRKEAARRREQTRPiRKnIEKVESQIEKLQpRLAEIEEALADTSLY 598
Cdd:COG0488 238 L-EQRAERLEQEAAAY-----------AKQQKKIAKEEEFIRRFRAKA-RK-AKQAQSRIKALE-KLEREEPPRRDKTVE 302
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-507 |
2.18e-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: 143.12 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSL---GADEGS-------LTRPSVW----TVAHMAQE 72
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEvlldgrdLLELSEAlrgrRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 73 VkaldMPAIDFVLSGDEEYWDIQNKLAQPEQltdsdlaklhgrfdeihgysAPSKAAQLMAGLGfLEHQLRLNVASFSGG 152
Cdd:COG1123 92 P----MTQLNPVTVGDQIAEALENLGLSRAE--------------------ARARVLELLEAVG-LERRLDRYPHQLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 153 WRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIENQELTlytg 228
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIV---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 229 nystfETTRSERLaqqqqafekqqearahlqkfidrfkakatkarqaqsrikqLERMQQLAPAHVDTPFTFSFREPTKMS 308
Cdd:COG1123 223 -----EDGPPEEI----------------------------------------LAAPQALAAVPRLGAARGRAAPAAAAA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 SPLLTLENASIGY-----GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERK 369
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 370 ASELLNIGYFAQHQMDALD-----GQ--ASPmLQLARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALA 442
Cdd:COG1123 338 RELRRRVQMVFQDPYSSLNprmtvGDiiAEP-LRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIA 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 443 --LIVwqRPNVLILDEPTNHLDLDMRHA---LSMALQDFEG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:COG1123 417 raLAL--EPKLLILDEPTSALDVSVQAQilnLLRDLQRELGlTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
307-527 |
2.16e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.20 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------RKASELLNIGYFA 380
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTvrlfgkPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 381 QH-QMDA-------------LDGQaSPMLQLARIADKQISEATLRSfLGSFGFSGERMDTpcesFSGGE--RARLALALI 444
Cdd:COG1121 82 QRaEVDWdfpitvrdvvlmgRYGR-RGLFRRPSRADREAVDEALER-VGLEDLADRPIGE----LSGGQqqRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 445 vwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCteFEGDLQDY--AKWL 519
Cdd:COG1121 156 --QDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVltPENL 231
|
....*...
gi 446536636 520 REARQQQI 527
Cdd:COG1121 232 SRAYGGPV 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-220 |
2.96e-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: 121.05 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPSVWTVAHMAQEVKAL- 76
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngEPIRDAREDYRRRLAYLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 DMPAIDFVLSGDE--EYWdiqnklaqpeqltdsdlAKLHGRFDeihgysAPSKAAQLMAGLGfLEHQLRLNVASFSGGWR 154
Cdd:COG4133 82 HADGLKPELTVREnlRFW-----------------AALYGLRA------DREAIDEALEAVG-LAGLADLPVRQLSAGQK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISHDRDFLDAitDHILHIEN 220
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAA--ARVLDLGD 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
311-504 |
4.91e-31 |
|
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: 121.69 E-value: 4.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASEL-LNIGYF 379
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlasLSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQHQMDALDGQASPMLQLARI-----------ADKQISEATLRSfLGSFGFSgermDTPCESFSGGERAR--LALALIvw 446
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYphlglfgrpsaEDREAVEEALER-TGLEHLA----DRPVDELSGGERQRvlIARALA-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 447 QRPNVLILDEPTNHLDLdmRHALSM-----ALQDFEG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1120 154 QEPPLLLLDEPTSHLDL--AHQLEVlellrRLARERGrTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-241 |
5.13e-31 |
|
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: 127.74 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKALDmpai 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALD---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 dfvlsGDEEYWdiqnklaqpEQLTD-SDLAKlhgrfdeIHGYSAPSKAaqLMAGLGFLEHQLRLNVASFSGGWRMRLNLA 160
Cdd:TIGR03719 399 -----PNKTVW---------EEISGgLDIIK-------LGKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIE-NQELTLYTGNYSTFETTRSE 239
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEEDKKR 535
|
..
gi 446536636 240 RL 241
Cdd:TIGR03719 536 RL 537
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
313-506 |
1.75e-30 |
|
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: 117.92 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 313 TLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASEL-LNIGYFAQ 381
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEilldgkdlasLSPKELaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 hqmdALDgqaspMLQLARIADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03214 81 ----ALE-----LLGLAHLADRPFNE-----------------------LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446536636 462 DLDMRHALsMAL-----QDFEGAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:cd03214 129 DIAHQIEL-LELlrrlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-241 |
2.19e-28 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 119.84 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKALDmpai 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 dfvlsGDEEYWdiqnklaqpEQLTD-SDLAKLHGRfdEIhgysaPSKAaqLMAGLGFL--EHQLRlnVASFSGGWRMRLN 158
Cdd:PRK11819 401 -----PNKTVW---------EEISGgLDIIKVGNR--EI-----PSRA--YVGRFNFKggDQQKK--VGVLSGGERNRLH 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIE-NQELTLYTGNYSTFETTR 237
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEYEEDK 535
|
....
gi 446536636 238 SERL 241
Cdd:PRK11819 536 KRRL 539
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
312-504 |
7.84e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.06 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkaseLLN---------------I 376
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI----YLDgkplsampppewrrqV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQhQMDALDGQASPMLQLA-RIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILD 455
Cdd:COG4619 77 AYVPQ-EPALWGGTVRDNLPFPfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 456 EPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
216-301 |
2.30e-27 |
|
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: 105.73 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 216 LHIENQELTLYTGNYSTFETTRSERLAQQQQAFEKQQEARAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDT 295
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*.
gi 446536636 296 PfTFSF 301
Cdd:pfam12848 81 P-KLRF 85
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-504 |
5.58e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.77 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 321 YGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELL-NIGYFAQHqmDALDGQ 390
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedvaRDPAEVRrRIGYVPQE--PALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 391 ASPMLQLARIA-----DKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:COG1131 88 LTVRENLRFFArlyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446536636 466 RHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1131 167 RRELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-241 |
2.26e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 108.02 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVwTVAHMAQEVKAldmpA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE-DVRKEPREARR----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 IdFVLSGDEEYWDIqnklaqpeqLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGFLEHqLRLNVASFSGGWRMRLNLA 160
Cdd:COG4555 76 I-GVLPDERGLYDR---------LTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEF-LDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHILHIENQELtLYTGNYSTF-ETT 236
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHKGKV-VAQGSLDELrEEI 223
|
....*
gi 446536636 237 RSERL 241
Cdd:COG4555 224 GEENL 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
314-505 |
4.55e-26 |
|
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: 106.46 E-value: 4.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 314 LENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPL------LAGERKASELLNIGYFAQH-QMD- 385
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtsgsirVFGKPLEKERKRIGYVPQRrSIDr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 386 ------------ALDGQASPMLQLARiADKQISEATLRsFLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLI 453
Cdd:cd03235 82 dfpisvrdvvlmGLYGHKGLFRRLSK-ADKAKVDEALE-RVGLSELADRQIGE----LSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 454 LDEPTNHLDLDMRHA---LSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:cd03235 156 LDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-223 |
5.18e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP----SVWT----VAHMA 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgKPlsamPPPEwrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 71 QEVKALDMPAIDFvlsgdeeywdiqnkLAQPEQLTdsdlaklHGRFDeihgysaPSKAAQLMAGLGFLEHQLRLNVASFS 150
Cdd:COG4619 81 QEPALWGGTVRDN--------------LPFPFQLR-------ERKFD-------RERALELLERLGLPPDILDKPVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA----ILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
312-504 |
8.51e-26 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 104.40 E-value: 8.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELL-NIGYFAQ 381
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEikvlgkdikKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HqmdaldgqasPMLqlariadkqISEATLRSFLgsfgfsgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03230 81 E----------PSL---------YENLTVRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446536636 462 DLDMRHALSMALQDF---EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03230 127 DPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
307-530 |
3.45e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 110.43 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSspLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------------- 367
Cdd:PRK11147 1 MS--LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivarlqqdpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 368 -------------RKASELLNIGYFAQHQMdALDGQASPMLQLARIADK-------QIsEATLRSFLGSFGFSGermDTP 427
Cdd:PRK11147 79 vegtvydfvaegiEEQAEYLKRYHDISHLV-ETDPSEKNLNELAKLQEQldhhnlwQL-ENRINEVLAQLGLDP---DAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 428 CESFSGG--ERARLALALIVwqRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PRK11147 154 LSSLSGGwlRKAALGRALVS--NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
250 260 270
....*....|....*....|....*....|
gi 446536636 506 TEFEGDLQDY----AKWLR-EARQqqiNAQ 530
Cdd:PRK11147 232 VSYPGNYDQYllekEEALRvEELQ---NAE 258
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
313-504 |
3.46e-25 |
|
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: 101.94 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 313 TLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkasellnigyfaqhqmdaldgqas 392
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 393 pmlqlARIADKQISEATLRSFLGSFGFsgermdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMA 472
Cdd:cd00267 56 -----ILIDGKDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 446536636 473 LQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd00267 123 LRELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
311-504 |
9.75e-25 |
|
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: 103.40 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELL---------- 374
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVRKEPRearrqigvlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 -------------NIGYFAQhqmdaldgqaspmlqLARIADKQIsEATLRSFLGSFGFSGERmDTPCESFSGGERARLAL 441
Cdd:COG4555 81 derglydrltvreNIRYFAE---------------LYGLFDEEL-KKRIEELIELLGLEEFL-DRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 442 ALIVWQRPNVLILDEPTNHLDLDMRHALS---MALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLReilRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
1.09e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 102.83 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsVW--TVAHMAQEVKALdmp 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR---VLgeDVARDPAEVRRR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 aIDFVlsgdeeywdIQNkLAQPEQLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGfLEHQLRLNVASFSGGWRMRLNL 159
Cdd:COG1131 75 -IGYV---------PQE-PALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHIL 216
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-220 |
3.25e-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: 99.24 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 3 QFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaldmpaid 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 83 fvlsgdeeywdiqnklaqpeqLTDSDLAKLHGRfdeihgysapskaaQLMAGLGFLeHQLrlnvasfSGGWRMRLNLART 162
Cdd:cd00267 58 ---------------------IDGKDIAKLPLE--------------ELRRRIGYV-PQL-------SGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
5.89e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 101.32 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT------RPSVWTVAHMAQEVK 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 75 A-LDMPA--IDFVLSGdeeywdiqnklaqpeqltdsdLAKLHGRFdeiHGYSAPSKAA--QLMAGLGfLEHQLRLNVASF 149
Cdd:COG1121 86 VdWDFPItvRDVVLMG---------------------RYGRRGLF---RRPSRADREAvdEALERVG-LEDLADRPIGEL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIeNQEL 223
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAateEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-223 |
9.65e-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: 99.53 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 3 QFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPSVWT---VAHMAQEVKAL 76
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPLEKErkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 -DMP--AIDFVLSGdeeywdiqnklaqpeqltdsdlakLHGRFDEIHGYSAPSKAAQLMA----GLGFLEHQlrlNVASF 149
Cdd:cd03235 81 rDFPisVRDVVLMG------------------------LYGHKGLFRRLSKADKAKVDEAlervGLSELADR---QIGEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIeNQEL 223
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPktqEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
310-493 |
1.20e-23 |
|
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: 99.09 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 310 PLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASELL--NIGYF 379
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepiRDAREDYrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQHqmDALDGQASP--MLQL-ARIADKQISEATLRSFLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILD 455
Cdd:COG4133 81 GHA--DGLKPELTVreNLRFwAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALArLLLSPAP-LWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446536636 456 EPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASV 493
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-220 |
2.10e-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: 98.69 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 3 QFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT----RPSVWTVAHMAQEVkal 76
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkDLTKLSLKELRRKV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 dmpaiDFVLsgdeeywdiQNklaqPE-QL----TDSDLA----KLHGRFDEIHgysapSKAAQLMAGLGfLEHQLRLNVA 147
Cdd:cd03225 78 -----GLVF---------QN----PDdQFfgptVEEEVAfgleNLGLPEEEIE-----ERVEEALELVG-LEGLRDRSPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-223 |
6.45e-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: 95.93 E-value: 6.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaldmpai 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 dfvlsgdeeywdiqnklaqpeqltdsdlaklhgrfdeIHGYSAPSKAAQLMAGLGFL--EHQL--RLNVA---SFSGGWR 154
Cdd:cd03230 59 -------------------------------------VLGKDIKKEPEEVKRRIGYLpeEPSLyeNLTVRenlKLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILI-SHDRDFLDAITDHILHIENQEL 223
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkEGKTILLsSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
322-526 |
1.28e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 102.12 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 322 GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPLLaGERKASELLNIGYFAQ------------------- 381
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKEFE-GEARPAPGIKVGYLPQepqldpektvrenveegva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HQMDALD-------GQASPMLQLARIADKQ-----ISEAT----LRSFLgsfgfsgER-M--------DTPCESFSGGER 436
Cdd:PRK11819 97 EVKAALDrfneiyaAYAEPDADFDALAAEQgelqeIIDAAdawdLDSQL-------EIaMdalrcppwDAKVTKLSGGER 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 437 ARLALALIVWQRPNVLILDEPTNHLDldmrhALSMA-----LQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGd 511
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD-----AESVAwleqfLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG- 243
|
250
....*....|....*..
gi 446536636 512 lqDYAKWL--REARQQQ 526
Cdd:PRK11819 244 --NYSSWLeqKAKRLAQ 258
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
312-504 |
1.36e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 96.63 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELL-NIGY- 378
Cdd:COG1122 1 IELENLSFSYPGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkditkKNLRELRrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 379 --FAQHQM-------D-ALdgqaSPM-LQLAR-IADKQISEAtlrsfLGSFGFSgERMDTPCESFSGGERARLALALIVW 446
Cdd:COG1122 81 fqNPDDQLfaptveeDvAF----GPEnLGLPReEIRERVEEA-----LELVGLE-HLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 447 QRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
314-504 |
1.97e-22 |
|
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: 95.61 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 314 LENASIGYGDKKIA--EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqMDALDGQA 391
Cdd:cd03225 2 LKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL--------------VDGKDLTK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 SPMLQLARI-------ADKQISEATLRS---F-LGSFGFSGERM-----------------DTPCESFSGGERARLALAL 443
Cdd:cd03225 68 LSLKELRRKvglvfqnPDDQFFGPTVEEevaFgLENLGLPEEEIeerveealelvgleglrDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-223 |
4.24e-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: 95.48 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHMAQev 73
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkdITKKNLRELRRKVG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 74 kaldmpaidFVLsgdeeywdiQNklaqPE-QLTDSDLaklhgrFDEI------HGYS---APSKAAQLMAGLGfLEHQLR 143
Cdd:COG1122 79 ---------LVF---------QN----PDdQLFAPTV------EEDVafgpenLGLPreeIRERVEEALELVG-LEHLAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 144 LNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:COG1122 130 RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDD 209
|
...
gi 446536636 221 QEL 223
Cdd:COG1122 210 GRI 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-504 |
1.06e-21 |
|
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: 99.11 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLG--SLGADEGSLtrpsVWTVAhMAQEVKALDMP 79
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI----IYHVA-LCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 A-----------------IDFVLSGDEEYWDIQNKLAQPEQLT------DSDLAKLHGRFDEIhGYSAPS---KAAQLMA 133
Cdd:TIGR03269 76 SkvgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfalygdDTVLDNVLEALEEI-GYEGKEavgRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 134 GLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-LDAIL---WLEDWLKAYEGTLILISHDRDFLD 209
Cdd:TIGR03269 155 MVQ-LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLvhnALEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 210 AITDHILHIENQELTLytgnystfETTRSERLaqqqqafekqqearahlQKFIDRFKAkatkarqaqsrikqLERmqqla 289
Cdd:TIGR03269 234 DLSDKAIWLENGEIKE--------EGTPDEVV-----------------AVFMEGVSE--------------VEK----- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 290 pahvdtpftfsFREpTKMSSPLLTLENASIGY-----GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLL 364
Cdd:TIGR03269 270 -----------ECE-VEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 365 AGE---RKASELLN---------------IGYFaqHQMDALDGQASPMLQLARIADKQISE--ATLRSF--LGSFGFSGE 422
Cdd:TIGR03269 338 SGEvnvRVGDEWVDmtkpgpdgrgrakryIGIL--HQEYDLYPHRTVLDNLTEAIGLELPDelARMKAVitLKMVGFDEE 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 423 R----MDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVC 494
Cdd:TIGR03269 416 KaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVC 495
|
570
....*....|
gi 446536636 495 DELLLVHGGK 504
Cdd:TIGR03269 496 DRAALMRDGK 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-209 |
1.25e-21 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 99.25 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFD--QVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKALDmp 79
Cdd:PRK11147 318 IVFEmeNVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 aidfvlsgdeeywdiqnklaqPEQLTDSDLAK------LHGRFDEIHGYsapskaAQlmaglGFLEHQLRLN--VASFSG 151
Cdd:PRK11147 396 ---------------------PEKTVMDNLAEgkqevmVNGRPRHVLGY------LQ-----DFLFHPKRAMtpVKALSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLD 209
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
312-510 |
2.23e-21 |
|
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: 92.64 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQItPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLN-IGYFAQ 381
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTiridgqdvlKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HQM--------DALDGQASpmlqLARIADKQISEATLRSfLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:cd03264 80 EFGvypnftvrEFLDYIAW----LKGIPSKEVKARVDEV-LELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 454 LDEPTNHLDLDMRHALSMALQDF-EGAVVLVS-HERQLIASVCDELLLVHGGKCTeFEG 510
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
312-504 |
2.82e-21 |
|
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: 93.73 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGE-----RKASELLNIGYFA 380
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvDLAGVdlhglSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 381 QHQMDALDGQASPMLQLARI-------ADKQISEATLRSFLGSFG---FSGERMDTpcesFSGGERARLALALIVWQRPN 450
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIphrslwaGDSPHDAAVVDRALARTElshLADRDMST----LSGGERQRVHVARALAQEPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 451 VLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVS-HERQLIASVCDELLLVHGGK 504
Cdd:TIGR03873 158 LLLLDEPTNHLDVRAQLETLALVRELaaTGVTVVAAlHDLNLAASYCDHVVVLDGGR 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
312-504 |
6.79e-21 |
|
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: 90.35 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKK--IAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqmdaLDG 389
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----------------LDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QASpmlqlariadKQISEATLRSFLGSFG-----FSGERMDTpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLD 464
Cdd:cd03246 64 ADI----------SQWDPNELGDHVGYLPqddelFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 465 MRHALSMALQDFEGA---VVLVSHERQLIASvCDELLLVHGGK 504
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
309-507 |
8.24e-21 |
|
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: 96.13 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 SPLLTLENASIGY--GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP---------LLAGE--RKASELL- 374
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdlLELSEALr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 --NIGYFAQHQMDALDG-----QASPMLQLARIADKQISEATLRSfLGSFGFsGERMDTPCESFSGGERARLALALIVWQ 447
Cdd:COG1123 82 grRIGMVFQDPMTQLNPvtvgdQIAEALENLGLSRAEARARVLEL-LEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 448 RPNVLILDEPTNHLDLDMRH---ALSMALQDFEG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAeilDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-177 |
9.32e-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: 89.24 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTR----PSVWTVAHMAQEVKALDmpaidfvlsgdeeywdiQN 96
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdLTDDERKSLRKEIGYVF-----------------QD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 97 KLAQPEqLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLG---FLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:pfam00005 68 PQLFPR-LTVRENLRLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 446536636 174 EPTN 177
Cdd:pfam00005 147 EPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
330-459 |
1.14e-20 |
|
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: 88.86 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----------RKASELLNIGYFAQH-----QMDALD--GQA 391
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDpqlfpRLTVREnlRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 392 SPMLQLARIADKQISEAtLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:pfam00005 84 LLLKGLSKREKDARAEE-ALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-204 |
3.18e-20 |
|
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: 90.49 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP-SVWTVAHMAQEVkAL 76
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlASLSRRELARRI-AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 dmpaidfvlsgdeeywdiqnkLAQ----PEQLTDSDLAkLHGRFDEIHGYSAPSK-----AAQLMAGLGFLEHQLRlNVA 147
Cdd:COG1120 80 ---------------------VPQeppaPFGLTVRELV-ALGRYPHLGLFGRPSAedreaVEEALERTGLEHLADR-PVD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EG-TLILISHD 204
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLareRGrTVVMVLHD 197
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
282-507 |
5.62e-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: 94.06 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 282 LERMQQLAPAHVDTPFTFSFREPTkmSSPLLTLENASIGY--GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG 359
Cdd:COG4987 306 ARRLNELLDAPPAVTEPAEPAPAP--GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 360 DLPLLAGE-----RKASELL------NIGYFAQ--HQMDA-----LdgqaspmlqlaRIADKQISEATLRSFLGSFGFSG 421
Cdd:COG4987 384 FLDPQSGSitlggVDLRDLDeddlrrRIAVVPQrpHLFDTtlrenL-----------RLARPDATDEELWAALERVGLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 422 ------ERMDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsmaLQDFEGA-----VVLVSHE 486
Cdd:COG4987 453 wlaalpDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEAlagrtVLLITHR 529
|
250 260
....*....|....*....|.
gi 446536636 487 RQLIASVcDELLLVHGGKCTE 507
Cdd:COG4987 530 LAGLERM-DRILVLEDGRIVE 549
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
7.39e-20 |
|
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: 88.43 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT--RPSVWTVAHMAQEVKAL-DM 78
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdGKSYQKNIEALRRIGALiEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 79 PAIDFVLSGDEeywdiqNKLAqpeqltdsdLAKLHGRFDEIHgysapsKAAQLMAGLGFLEHQLrlnVASFSGGWRMRLN 158
Cdd:cd03268 81 PGFYPNLTARE------NLRL---------LARLLGIRKKRI------DEVLDVVGLKDSAKKK---VKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
1.13e-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: 92.91 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRR--GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT----------RPSVW-TVAH 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdldEDDLRrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 69 MAQEVkaldmpaidFVLSGDeeywdIQN--KLAQPEqLTDSDLAKlhgrfdeihgysapskAAQLmAGLGFLEHQLR--L 144
Cdd:COG4987 414 VPQRP---------HLFDTT-----LREnlRLARPD-ATDEELWA----------------ALER-VGLGDWLAALPdgL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 145 NV------ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIlwLEDWLKAYEG-TLILISHDRDFLDAItDH 214
Cdd:COG4987 462 DTwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQAL--LADLLEALAGrTVLLITHRLAGLERM-DR 538
|
250
....*....|
gi 446536636 215 ILHIENQELT 224
Cdd:COG4987 539 ILVLEDGRIV 548
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-504 |
1.19e-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: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 321 YGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLNIGYFAQHQ--MDALDG 389
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEitfdgksyqKNIEALRRIGALIEAPgfYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QaSPMLQLARIadKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LDM 465
Cdd:cd03268 90 R-ENLRLLARL--LGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgiKEL 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 446536636 466 RhALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03268 166 R-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-219 |
1.39e-19 |
|
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: 87.87 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 11 RGGRVL--FQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-----------LTRPSVWTVAHM-------- 69
Cdd:COG4778 19 QGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwvdLAQASPREILALrrrtigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 70 AQEVKALD-MPAIDFVlsgdeeywdiqnklAQP--EQLTDSDLAKlhgrfdeihgysapSKAAQLMAGLGFLEHQLRLNV 146
Cdd:COG4778 99 SQFLRVIPrVSALDVV--------------AEPllERGVDREEAR--------------ARARELLARLNLPERLWDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 147 ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAyEGTLIL-ISHDRDFLDAITDHILHIE 219
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKA-RGTAIIgIFHDEEVREAVADRVVDVT 226
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
7-216 |
2.15e-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: 88.33 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPSVWTVAHMAQEVKALDMPAIDfvls 86
Cdd:TIGR03873 7 VSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-LAGVDLHGLSRRARARRVALVE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 87 gdeeywdiQNKLAQPEqLTDSDLAKLhGR--FDEIHGYSAPSKAAQLMAGLGF--LEHQLRLNVASFSGGWRMRLNLART 162
Cdd:TIGR03873 82 --------QDSDTAVP-LTVRDVVAL-GRipHRSLWAGDSPHDAAVVDRALARteLSHLADRDMSTLSGGERQRVHVARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLK--AYEGTLILIS-HDRDFLDAITDHIL 216
Cdd:TIGR03873 152 LAQEPKLLLLDEPTNHLDVRAQLETLALVRelAATGVTVVAAlHDLNLAASYCDHVV 208
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
314-541 |
2.86e-19 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 92.23 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 314 LENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSL---------------------VGD------------ 360
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkncqilhveqevVGDdttalqcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 361 ---LPLLAGE----RKASELLNIGYFAQHQMDALDGQASPML--QLARI------ADKQISEATLRSFLGSFGFSGERMD 425
Cdd:PLN03073 260 ierTQLLEEEaqlvAQQRELEFETETGKGKGANKDGVDKDAVsqRLEEIykrlelIDAYTAEARAASILAGLSFTPEMQV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 426 TPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270
....*....|....*....|....*....|....*.
gi 446536636 506 TEFEGdlqDYAKWLREARQQQINAQTAIEQNNSSSA 541
Cdd:PLN03073 420 VTYKG---DYDTFERTREEQLKNQQKAFESNERSRS 452
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
312-504 |
3.70e-19 |
|
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: 85.13 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGD--KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkasellnIgyfaqhqmdALDG 389
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE--------I---------LIDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QASPMLQLARIAdKQISEATLRSFLgsfgFSGermdTPCES-FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:cd03228 64 VDLRDLDLESLR-KNIAYVPQDPFL----FSG----TIRENiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 446536636 469 LSMALQDFEG--AVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:cd03228 135 ILEALRALAKgkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
309-505 |
8.20e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.32 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 SPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQ--HQMDA 386
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 387 LDGQASPMLQL-ARIADKQISEATLRSflgsfgFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:PRK09544 82 LPLTVNRFLRLrPGTKKEDILPALKRV------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446536636 466 RHAL----SMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PRK09544 156 QVALydliDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHIC 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
309-504 |
1.04e-18 |
|
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: 85.91 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 SPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP--------LLaGERKASELL-----N 375
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrLF-GERRGGEDVwelrkR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 376 IGYFAQHQMDALDGQASP----------MLQLAR-IADKQISEAtlRSFLGSFGFSgERMDTPCESFSGGERAR--LALA 442
Cdd:COG1119 80 IGLVSPALQLRFPRDETVldvvlsgffdSIGLYRePTDEQRERA--RELLELLGLA-HLADRPFGTLSQGEQRRvlIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 443 LIvwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG--AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1119 157 LV--KDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
1.82e-18 |
|
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: 89.05 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRR-GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrpsvwTVAHmaQEVKALDMPA 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI------LING--VDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 I--DFVLSGDEEYW---------DIQNKLAQPEQLTDS-DLAKLHgrfDEIhgysapskaAQLMAGlgfLEHQLRLNVAS 148
Cdd:COG4988 409 WrrQIAWVPQNPYLfagtirenlRLGRPDASDEELEAAlEAAGLD---EFV---------AALPDG---LDTPLGEGGRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD--AILW--LEDWLKAYegTLILISHDRDFLDAItDHILHIENQELT 224
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKGR--TVILITHRLALLAQA-DRILVLDDGRIV 550
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
2.30e-18 |
|
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: 83.25 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaldmpaidfv 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 85 lsgdeeywdiqnklaqpeqltdsdlakLHGRfdEIHGYSAPSKA------AQLMAGLGfLEHQLRLNVASFSGGWRMRLN 158
Cdd:cd03214 58 ---------------------------LDGK--DLASLSPKELArkiayvPQALELLG-LAHLADRPFNELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
270-485 |
3.89e-18 |
|
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: 87.80 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 270 TKARQAQSRIKQLERMQQLAPAHVD-TPFTFSFREPTkmssplLTLENASIGYGDKKIAEK-IKLQITPNSRIGLLGMNG 347
Cdd:TIGR02868 298 TRVRAAAERIVEVLDAAGPVAEGSApAAGAVGLGKPT------LELRDLSAGYPGAPPVLDgVSLDLPPGERVAILGPSG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 348 AGKSTLIKSLVGDLPLLAGE----------RKASELLN-IGYFAQ--HQMDALDGQAspmLQLAR--IADKQISEATLRS 412
Cdd:TIGR02868 372 SGKSTLLATLAGLLDPLQGEvtldgvpvssLDQDEVRRrVSVCAQdaHLFDTTVREN---LRLARpdATDEELWAALERV 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 413 FLGSFGFS-GERMDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA-LSMALQDFEG-AVVLVSH 485
Cdd:TIGR02868 449 GLADWLRAlPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADElLEDLLAALSGrTVVLITH 528
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
314-514 |
4.03e-18 |
|
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: 84.09 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 314 LENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASE------LLNIGYF 379
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgediSGLSEaelyrlRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQH-----QMDALDGQASPMLQLARIADKQISEATlRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLIL 454
Cdd:cd03261 83 FQSgalfdSLTVFENVAFPLREHTRLSEEEIREIV-LEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 455 DEPTNHLD---LDMRHALSMALQDFEGA-VVLVSHERQLIASVCDELLLVHGGKcTEFEGDLQD 514
Cdd:cd03261 161 DEPTAGLDpiaSGVIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGK-IVAEGTPEE 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
4.44e-18 |
|
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: 84.32 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAH--MA- 70
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRilfdgrdITGLPPHRIARlgIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 71 --QEVKAL-DMPAIDFVLSGdeeywdIQNKLaqPEQLTDSDLAKLHGRFDEIhgySAPSKAAQLMAGLGfLEHQLRLNVA 147
Cdd:COG0411 84 tfQNPRLFpELTVLENVLVA------AHARL--GRGLLAALLRLPRARREER---EARERAEELLERVG-LADRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPT---NHLDLDAILWLEDWLKAYEG-TLILISHDRDFLDAITDHIL 216
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-462 |
4.60e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 87.38 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSL----GADEGSLTRPSVWTVAHMAQEVKA- 75
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELpllsGERQSQFSHITRLSFEQLQKLVSDe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 76 -----LDMpaidfvLSGDEEywDIQNKLAQPEQltdsdlaklhgrfDEIHgysAPSKAAQLMAGLGfLEHQLRLNVASFS 150
Cdd:PRK10938 83 wqrnnTDM------LSPGED--DTGRTTAEIIQ-------------DEVK---DPARCEQLAQQFG-ITALLDRRFKYLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG---TLILISHDRDFLDAITDHILHIENQELTLyT 227
Cdd:PRK10938 138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLAE-T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 228 GnystfetTRSERLaqqqqafekqqearahlqkfidrfkakatkarqAQSRIKQLERMQQLAPAHVDTPFTFSFREPTKM 307
Cdd:PRK10938 217 G-------EREEIL---------------------------------QQALVAQLAHSEQLEGVQLPEPDEPSARHALPA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 308 SSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP-------LLAGERKAS-ELL----- 374
Cdd:PRK10938 257 NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgysndlTLFGRRRGSgETIwdikk 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 NIGYFA-QHQMD----------ALDG--------QAspmlqlarIADKQISEAtlRSFLGSFGFSGERMDTPCESFSGGE 435
Cdd:PRK10938 337 HIGYVSsSLHLDyrvstsvrnvILSGffdsigiyQA--------VSDRQQKLA--QQWLDILGIDKRTADAPFHSLSWGQ 406
|
490 500 510
....*....|....*....|....*....|
gi 446536636 436 RaRLAL---ALIvwQRPNVLILDEPTNHLD 462
Cdd:PRK10938 407 Q-RLALivrALV--KHPTLLILDEPLQGLD 433
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
311-504 |
4.93e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.40 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkasellnigYFAQHQMDALDG- 389
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV---------RLNGRPLAAWSPw 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 ----------QASPM----------------LQLARIADKQISEATLrsflgsfgfsgERMDtpCESF--------SGGE 435
Cdd:COG4559 72 elarrravlpQHSSLafpftveevvalgrapHGSSAAQDRQIVREAL-----------ALVG--LAHLagrsyqtlSGGE 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 436 RAR--LALALI-VWQ----RPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG4559 139 QQRvqLARVLAqLWEpvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
310-505 |
4.98e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 310 PLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGER----------KASELlnigyf 379
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwSPAEL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQHQmdALDGQASPM----------------LQLARIADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLALAL 443
Cdd:PRK13548 75 ARRR--AVLPQHSSLsfpftveevvamgrapHGLSRAEDDALVAAALAQ-VDLAHLAGRDYPQ----LSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 444 I---VWQ---RPNVLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PRK13548 148 VlaqLWEpdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
311-508 |
5.26e-18 |
|
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: 83.32 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEK----IKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERKASE 372
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalddVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiifdgkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 373 LLNIGYFAQHQMDALD-----GQ--ASPML-QLARIADKQISEATLRSFLGsFGFSGERMDT-PCEsFSGGERAR--LAL 441
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprmtiGEqiAEPLRiHGKLSKKEARKEAVLLLLVG-VGLPEEVLNRyPHE-LSGGQRQRvaIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 442 ALIVwqRPNVLILDEPTNHLDLDMRH---ALSMALQD-FEGAVVLVSHERQLIASVCDELLLVHGGKCTEF 508
Cdd:cd03257 159 ALAL--NPKLLIADEPTSALDVSVQAqilDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
5.36e-18 |
|
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: 83.98 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTlfaaLLGSLGADEgsltRPSVwtvahmAQEVKALDMPA 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDL----PPTY------GNDVRLFGERR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 idfvlsGDEEYWDIQNKL-----AQPEQLTDSDLAK---LHGRFDEIHGYSAPS-----KAAQLMAGLGfLEHQLRLNVA 147
Cdd:COG1119 69 ------GGEDVWELRKRIglvspALQLRFPRDETVLdvvLSGFFDSIGLYREPTdeqreRARELLELLG-LAHLADRPFG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK--AYEG--TLILISHDRDFLDAITDHILHIEN 220
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDklAAEGapTLVLVTHHVEEIPPGITHVLLLKD 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
320-504 |
1.18e-17 |
|
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: 82.17 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 320 GYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLNIGYFAQHqmDALDG 389
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingysirtDRKAARQSLGYCPQF--DALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QASPM--LQL-ARIadKQISEATLRS----FLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03263 89 ELTVRehLRFyARL--KGLPKSEIKEevelLLRVLGLTDKA-NKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446536636 463 LDMRHALSMALQDFEG--AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03263 166 PASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
312-510 |
1.33e-17 |
|
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: 80.82 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYG--DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkasellnigYFAQHQMDALDG 389
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QASpmlqlariadKQISEATLRSFLgsfgFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD-LDMRHA 468
Cdd:cd03247 72 ALS----------SLISVLNQRPYL----FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 469 LSMALQDFEG-AVVLVSHERQLIASVcDELLLVHGGKcTEFEG 510
Cdd:cd03247 138 LSLIFEVLKDkTLIWITHHLTGIEHM-DKILFLENGK-IIMQG 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
312-504 |
1.48e-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: 81.56 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkasellnigYFAQHQMDALDGQ- 390
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV---------LFDGKPLDIAARNr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 391 ----------------ASPMLQLARIADKQISEA--TLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVL 452
Cdd:cd03269 72 igylpeerglypkmkvIDQLVYLAQLKGLKKEEArrRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 453 ILDEPTNHLD-LDMRHALS--MALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03269 151 ILDEPFSGLDpVNVELLKDviRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
313-504 |
1.51e-17 |
|
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: 81.53 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 313 TLENASIGYGDK-KIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-------RKASELL-NIGYFAQHQ 383
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpIKAKERRkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 384 MDALdGQASPMLQLaRIADKQISE--ATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03226 81 DYQL-FTDSVREEL-LLGLKELDAgnEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 462 DLdmRHALSMA-----LQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03226 158 DY--KNMERVGelireLAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-220 |
1.58e-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: 80.50 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGR--VLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrpsvwtvahmaqevkaldmp 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 aidfvlsgdeeYWDIQNklaqpeqLTDSDLAKLHGRFdeihGYsAPSKAaQLMAGLgflehqLRLNVasFSGGWRMRLNL 159
Cdd:cd03228 60 -----------LIDGVD-------LRDLDLESLRKNI----AY-VPQDP-FLFSGT------IRENI--LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 160 ARTLMSRSDLLLLDEPTNHLDLD--AILW--LEDWLKayEGTLILISHdRDFLDAITDHILHIEN 220
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPEteALILeaLRALAK--GKTVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
2.22e-17 |
|
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: 81.15 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 7 VSLRRGGRVLfQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKALDMPAIDFVLs 86
Cdd:cd03226 7 FSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 87 gdeeywdiqnklaqpeqLTDSDLAKLHGRFDEIHGYsaPSKAAQLMAGLGFLEHQLRlNVASFSGGWRMRLNLARTLMSR 166
Cdd:cd03226 85 -----------------FTDSVREELLLGLKELDAG--NEQAETVLKDLDLYALKER-HPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 167 SDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
311-522 |
1.04e-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: 80.23 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYG----DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----------RKASELLN 375
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgrpvtrrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 376 IGYFAQHQMDALDgqasPMLQLA-------RIADKQISEATLRSFLGSFGFSGERMD-TPcESFSGGERARLAL--ALIV 445
Cdd:COG1124 81 VQMVFQDPYASLH----PRHTVDrilaeplRIHGLPDREERIAELLEQVGLPPSFLDrYP-HQLSGGQRQRVAIarALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 446 wqRPNVLILDEPTNHLDLDMR----HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE-------FEGDLQD 514
Cdd:COG1124 156 --EPELLLLDEPTSALDVSVQaeilNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEeltvadlLAGPKHP 233
|
....*...
gi 446536636 515 YAKWLREA 522
Cdd:COG1124 234 YTRELLAA 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
302-507 |
1.89e-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: 82.88 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 302 REPTKMSSPLLTLENASIGYGD-KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKAS--ELLNIGY 378
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 379 FAQHQMDALDGQASPMLQ--LA---RIADKQISEATLRSFLGSFGFSG------ERMDTPCES----FSGGERARLALAL 443
Cdd:COG4988 407 ASWRRQIAWVPQNPYLFAgtIRenlRLGRPDASDEELEAALEAAGLDEfvaalpDGLDTPLGEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEG-AVVLVSHERQLIASvCDELLLVHGGKCTE 507
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGrTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
312-508 |
1.96e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 78.76 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELL----------------- 374
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLldgkdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 -NIGYFAQH----QMDALDGQASPmLQLARIADKQISEATLRSFLGSFGFSGERMD-TPCESFSGGERARLALA--LIVw 446
Cdd:cd03260 81 rRVGMVFQKpnpfPGSIYDNVAYG-LRLHGIKLKEELDERVEEALRKAALWDEVKDrLHALGLSGGQQQRLCLAraLAN- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 447 qRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVCDELLLVHGGKCTEF 508
Cdd:cd03260 159 -EPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
310-506 |
2.06e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 310 PLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkaselLNIGYFAQHQMDA--L 387
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT------VLVAGDDVEALSAraA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 388 DGQASPMLQLARIA----DKQISEATLRSFLGSFGFSGER-----------------MDTPCESFSGGERARLALALIVW 446
Cdd:PRK09536 76 SRRVASVPQDTSLSfefdVRQVVEMGRTPHRSRFDTWTETdraaveramertgvaqfADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 447 QRPNVLILDEPTNHLDLDmrHA-----LSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK09536 156 QATPVLLLDEPTASLDIN--HQvrtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
312-504 |
3.16e-16 |
|
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: 77.94 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLNIGYFAQH 382
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 -----QMDALDGQASPmLQLARIADKQISEATLRSfLGSFGFSGERMDTPcESFSGGERARLALA--LIVwqRPNVLILD 455
Cdd:cd03259 81 yalfpHLTVAENIAFG-LKLRGVPKAEIRARVREL-LELVGLEGLLNRYP-HELSGGQQQRVALAraLAR--EPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 456 EPTNHLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03259 156 EPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
312-504 |
3.30e-16 |
|
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: 78.02 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIA--EKIKLQITPNSRIGLLGMNGAGKSTLIKslvgdlpLLAGERKASE---LL------------ 374
Cdd:cd03245 3 IEFRNVSFSYPNQEIPalDNVSLTIRAGEKVAIIGRVGSGKSTLLK-------LLAGLYKPTSgsvLLdgtdirqldpad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 ---NIGYFAQHQMdALDGQASPMLQLAR--IADKQISEATLRSFLGSF------GFS---GERMDtpceSFSGGERARLA 440
Cdd:cd03245 76 lrrNIGYVPQDVT-LFYGTLRDNITLGAplADDERILRAAELAGVTDFvnkhpnGLDlqiGERGR----GLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 441 LALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHeRQLIASVCDELLLVHGGK 504
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGR 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
312-504 |
3.94e-16 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 82.19 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGD--KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------------RKasel 373
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidlrqidpaslRR---- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 374 lNIGYFAQHqmDAL------------DGQASP--MLQLARIAdkQISEATLR------SFLGSFGfsgermdtpcESFSG 433
Cdd:COG2274 550 -QIGVVLQD--VFLfsgtirenitlgDPDATDeeIIEAARLA--GLHDFIEAlpmgydTVVGEGG----------SNLSG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 434 GERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGR 686
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
312-504 |
7.62e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERK----------ASELL-NIGYFA 380
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlsSRQLArRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 381 QHQMdALDGQA---------SPMLQL-ARIA--DKQISE-ATLRSFLGSFGfsgermDTPCESFSGGERARLALALIVWQ 447
Cdd:PRK11231 83 QHHL-TPEGITvrelvaygrSPWLSLwGRLSaeDNARVNqAMEQTRINHLA------DRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 448 RPNVLILDEPTNHLDLD-----MRhaLSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINhqvelMR--LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-204 |
1.05e-15 |
|
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: 80.48 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVwtvahMAQEVKALDMPAIDFVLSGDEEY 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV-----PVSSLDQDEVRRRVSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 92 WD---IQN-KLAQPEqLTDSDLAKLHGRFD-EIHGYSAPSKAAQLMAGLGflehqlrlnvASFSGGWRMRLNLARTLMSR 166
Cdd:TIGR02868 421 FDttvRENlRLARPD-ATDEELWAALERVGlADWLRALPDGLDTVLGEGG----------ARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446536636 167 SDLLLLDEPTNHLDLDAIL-WLEDWLKAYEG-TLILISHD 204
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-504 |
1.71e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 75.87 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 321 YGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELL-NIGYFAQHQM--DALD 388
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvREPREVRrRIGIVFQDLSvdDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 389 GQASpMLQLARIADKQISEATLR--SFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:cd03265 90 GWEN-LYIHARLYGVPGAERRERidELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446536636 467 HAL----SMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03265 168 AHVweyiEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
320-499 |
1.90e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 320 GYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQM--DALDGQASPMLQL 397
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 398 AR-----------IADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:NF040873 81 GRwarrglwrrltRDDRAAVDDALER-VGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 446536636 467 HALSMALQDFEG---AVVLVSHERQLIASVCDELLL 499
Cdd:NF040873 156 ERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-220 |
2.08e-15 |
|
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: 79.88 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLR--RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---------RPSVWT--VAH 68
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASLRrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 69 MAQEVK----------ALDMPAIDfvlsgDEEYWDIqnklaqpeqltdSDLAKLHgrfDEIhgysapskaAQLMAGLgfl 138
Cdd:COG2274 554 VLQDVFlfsgtireniTLGDPDAT-----DEEIIEA------------ARLAGLH---DFI---------EALPMGY--- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 139 EHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAIL-WLEDWlkayegTLILISHDRDFLdA 210
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDaeteaiiLENLRrLLKGR------TVIIIAHRLSTI-R 674
|
250
....*....|
gi 446536636 211 ITDHILHIEN 220
Cdd:COG2274 675 LADRIIVLDK 684
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
272-525 |
2.49e-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: 79.41 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 272 ARQAQSRIKQLERMQQLAPAHVDTPftfsfrEPTkmssPLLTLENASIGY--GDKKIAEKIKLQITPNSRIGLLGMNGAG 349
Cdd:COG4618 301 ARQAYRRLNELLAAVPAEPERMPLP------RPK----GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 350 KSTLIKSLVGDLPLLAGE---------RKASELL--NIGYFAQH-------------QMDALDGQAspMLQLARIADkqI 405
Cdd:COG4618 371 KSTLARLLVGVWPPTAGSvrldgadlsQWDREELgrHIGYLPQDvelfdgtiaeniaRFGDADPEK--VVAAAKLAG--V 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 406 SEATLR------SFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--E 477
Cdd:COG4618 447 HEMILRlpdgydTRIGEGGAR----------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaR 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446536636 478 GA-VVLVSHERQLIAsVCDELLLVHGGKCTEFeGDLQDYAKWLREARQQ 525
Cdd:COG4618 517 GAtVVVITHRPSLLA-AVDKLLVLRDGRVQAF-GPRDEVLARLARPAAA 563
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
300-509 |
3.00e-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: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 300 SFREPTKMSSPLLTLENAS--IGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----RKASEL 373
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvtvrGRVSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 374 LNIGYFaqhqmdaLDGQAS---------PMLQLARIADKQISEATLrsflgsfGFS--GERMDTPCESFSGGERARLALA 442
Cdd:cd03220 89 LGLGGG-------FNPELTgreniylngRLLGLSRKEIDEKIDEII-------EFSelGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 443 LIVWQRPNVLILDEPTNHLDLD--------MRHALSMAlqdfeGAVVLVSHERQLIASVCDELLLVHGGKCTEFE 509
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAfqekcqrrLRELLKQG-----KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-502 |
3.13e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.08 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 26 PGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVW------------------------TVAHMAQEV----KALD 77
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWdevlkrfrgtelqnyfkklyngeiKVVHKPQYVdlipKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 MPAIDFVLSGDEeywdiqnklaqpeqltdsdlaklHGRFDEIhgysapskAAQLmaglgFLEHQLRLNVASFSGGWRMRL 157
Cdd:PRK13409 178 GKVRELLKKVDE-----------------------RGKLDEV--------VERL-----GLENILDRDISELSGGELQRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 158 NLARTLMSRSDLLLLDEPTNHLDL-------DAILWLedwlkAYEGTLILISHDRDFLDAITDHIlHIenqeltLY--TG 228
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHDLAVLDYLADNV-HI------AYgePG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 229 NYSTFETTRSerlaqqqqafekqqeARAHLQKFIDRFkakatkARQAQSRIKqlermqqlapahvDTPFTFSFREPT--K 306
Cdd:PRK13409 290 AYGVVSKPKG---------------VRVGINEYLKGY------LPEENMRIR-------------PEPIEFEERPPRdeS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDkkiaekIKL-----QITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASelLNIGYFAQ 381
Cdd:PRK13409 336 ERETLVEYPDLTKKLGD------FSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISYKPQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HQMDALDGQASPMLqlariadKQISEATLRSFLGS---FGFSGER-MDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:PRK13409 408 YIKPDYDGTVEDLL-------RSITDDLGSSYYKSeiiKPLQLERlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446536636 458 TNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHG 502
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
320-523 |
3.30e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 320 GYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----RKASeLLNIG-------------YF-- 379
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRvevngRVSA-LLELGagfhpeltgreniYLng 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 -----AQHQMDALdgqaspmlqLARIADkqiseatlrsflgsfgFS--GERMDTPCESFSGGERARLALALIVWQRPNVL 452
Cdd:COG1134 114 rllglSRKEIDEK---------FDEIVE----------------FAelGDFIDQPVKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 453 ILDEptnhldldmrhALS-----------MALQDF---EGAVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD---- 514
Cdd:COG1134 169 LVDE-----------VLAvgdaafqkkclARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD-GDPEEviaa 236
|
....*....
gi 446536636 515 YAKWLREAR 523
Cdd:COG1134 237 YEALLAGRE 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
316-507 |
3.62e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.51 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 316 NASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKS------------LVGDLPLLAGERKASEL-LNIGYFAQH 382
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCinkleeitsgdlIVDGLKVNDPKVDERLIrQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 -----QMDALDGQASPMLQLaRIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:PRK09493 86 fylfpHLTALENVMFGPLRV-RGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 458 TNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
4.25e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 74.71 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPSVWTVAHMAQEVKAldmpAI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHDVVREPREVRR----RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFV---LSGDEEywdiqnklaqpeqLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGFLEHQLRLnVASFSGGWRMRLN 158
Cdd:cd03265 76 GIVfqdLSVDDE-------------LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRL-VKTYSGGMRRRLE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLDLDAI--LW--LEDWLKAYEGTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-220 |
4.40e-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: 75.22 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRG----GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPsvwtVAHMAQEV 73
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgRP----VTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 74 KALDMPAI--DFVLSGDEeYWDIQNKLAQPeqltdsdlAKLHGRFDeihgysAPSKAAQLMA--GLG--FLE---HQLrl 144
Cdd:COG1124 77 FRRRVQMVfqDPYASLHP-RHTVDRILAEP--------LRIHGLPD------REERIAELLEqvGLPpsFLDrypHQL-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 145 nvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:COG1124 140 -----SGGQRQRVAIARALILEPELLLLDEPTSALDVsvqAEILNLLKDLREERGlTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-181 |
4.95e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP-SVWTVAHMAQ----- 71
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngRPlADWSPAELARrravl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 72 -------------EVKAldMPAIDFVLSGDEEywdiqNKLAQpEQLTDSDLAKLHGRFdeihgYsapskaaqlmaglgfl 138
Cdd:PRK13548 82 pqhsslsfpftveEVVA--MGRAPHGLSRAED-----DALVA-AALAQVDLAHLAGRD-----Y---------------- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446536636 139 eHQLrlnvasfSGGWRMRLNLARTLMSRSD------LLLLDEPTNHLDL 181
Cdd:PRK13548 133 -PQL-------SGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDL 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
321-504 |
5.06e-15 |
|
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: 75.06 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 321 YGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDL-P---------LLAGERKASELLNIGY-FAQHQMDALDg 389
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPtsgevrvagLVPWKRRKKFLRRIGVvFGQKTQLWWD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 qASPMLQLARIAD-KQISEATLRSFLGsfGFS-----GERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDL 463
Cdd:cd03267 110 -LPVIDSFYLLAAiYDLPPARFKKRLD--ELSelldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 464 DMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03267 187 VAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
311-510 |
5.71e-15 |
|
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: 74.33 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKK----IAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDL------PLLAGERKASE----LLNI 376
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLepdagfATVDGFDVVKEpaeaRRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQHqmDALDGQASPMLQLARIAD-----KQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNV 451
Cdd:cd03266 81 GFVSDS--TGLYDRLTARENLEYFAGlyglkGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 452 LILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKcTEFEG 510
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTHIMQEVERLCDRVVVLHRGR-VVYEG 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-504 |
6.68e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 302 REPTKMSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKAS 371
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgvpvpaRARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 372 ELLNIGYFAqhQMDALDGQASPMLQLA------RIADKQIsEATLRSFLgSFGFSGERMDTPCESFSGGERARLALALIV 445
Cdd:PRK13536 112 ARARIGVVP--QFDNLDLEFTVRENLLvfgryfGMSTREI-EAVIPSLL-EFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 446 WQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLArgkTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-507 |
7.88e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.70 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 323 DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASEllNIGYFAQH--QMDALD---------GQA 391
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDifQIDAIKlrkevgmvfQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 SPMLQLArIAD-----------------KQISEATLRSfLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:PRK14246 100 NPFPHLS-IYDniayplkshgikekreiKKIVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 455 DEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
307-514 |
1.55e-14 |
|
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: 73.48 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER----KASEL--- 373
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgeiLVDGQDitglSEKELyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 374 -LNIGY-FaqhQMDAL-------DGQASPMLQLARIADKQISEATLRSfLGSFGFSG--ERMdtPCEsFSGGERARLALA 442
Cdd:COG1127 81 rRRIGMlF---QGGALfdsltvfENVAFPLREHTDLSEAEIRELVLEK-LELVGLPGaaDKM--PSE-LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 443 --LIVwqRPNVLILDEPT-----------NHLDLDMRHALSMalqdfegAVVLVSHERQLIASVCDELLLVHGGKCtEFE 509
Cdd:COG1127 154 raLAL--DPEILLYDEPTagldpitsaviDELIRELRDELGL-------TSVVVTHDLDSAFAIADRVAVLADGKI-IAE 223
|
....*
gi 446536636 510 GDLQD 514
Cdd:COG1127 224 GTPEE 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
1.84e-14 |
|
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: 72.79 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLR----RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVwTVAHMAQEVKAl 76
Cdd:cd03266 1 MITADALTKRfrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF-DVVKEPAEARR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 dmpAIDFVLSGDEEYwdiqNKLAQPEQLtdSDLAKLHG-RFDEIHGysAPSKAAQLMAglgfLEHQLRLNVASFSGGWRM 155
Cdd:cd03266 79 ---RLGFVSDSTGLY----DRLTARENL--EYFAGLYGlKGDELTA--RLEELADRLG----MEELLDRRVGGFSTGMRQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 156 RLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHI 215
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGKCILFStHIMQEVERLCDRV 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-218 |
2.10e-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: 76.17 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqeVKALDMPA 80
Cdd:TIGR02857 322 LEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA-------------VNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 IDFVLSGDEEYWDIQNKLAQPEQLTDS-DLAKLHGRFDEIHGYSAPSKAAQLMAGLGF-LEHQLRLNVASFSGGWRMRLN 158
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAENiRLARPDASDAEIREALERAGLDEFVAALPQgLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLDLD-AILWLEDWLKAYEG-TLILISHDRDFLdAITDHILHI 218
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAEtEAEVLEALRALAQGrTVLLVTHRLALA-ALADRIVVL 529
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
10-216 |
3.36e-14 |
|
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: 72.42 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 10 RRGGRVL--FQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-----------LTRPSVW--------TVAH 68
Cdd:TIGR02324 15 QQGGVRLpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRilvrhegawvdLAQASPRevlevrrkTIGY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 69 MAQEVKALD-MPAIDFVlsgdeeywdiqnklAQPEQLTDSDLAKlhgrfdeihgysAPSKAAQLMAGLGFLEHQLRLNVA 147
Cdd:TIGR02324 95 VSQFLRVIPrVSALEVV--------------AEPLLERGVPREA------------ARARARELLARLNIPERLWHLPPA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVM 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
307-504 |
3.67e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG----------ERKASELLNI 376
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgepvpSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQhqMDALDgqaspmlqlariADKQISEaTLRSFLGSFGFSG-----------------ERMDTPCESFSGGERARL 439
Cdd:PRK13537 83 GVVPQ--FDNLD------------PDFTVRE-NLLVFGRYFGLSAaaaralvppllefakleNKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA---VVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgktILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
312-504 |
3.74e-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: 71.06 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkasellniGYFaqhqmdalDGQa 391
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS---------ILI--------DGE- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 spmlqlaRIADKQISEATLRSFLG----SFG-FSG-ERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:cd03229 63 -------DLTDLEDELPPLRRRIGmvfqDFAlFPHlTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 466 RHALSMALQD----FEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03229 136 RREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-220 |
4.34e-14 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 71.85 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---------TRPSVW--TVAH 68
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqLDPADLrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 69 MAQEVK----------ALDMPAIDfvlsgDEEYwdiqnkLAQPEQLTDSDLAKLHGrfdeiHGYsapskaaqlmaglgfl 138
Cdd:cd03245 83 VPQDVTlfygtlrdniTLGAPLAD-----DERI------LRAAELAGVTDFVNKHP-----NGL---------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 139 EHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG--TLILISHDRDFLDaITDHIL 216
Cdd:cd03245 131 DLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD-LVDRII 209
|
....
gi 446536636 217 HIEN 220
Cdd:cd03245 210 VMDS 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-505 |
5.26e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 71.04 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 320 GYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERKASELLnigyfaqhqmdaLDGQASPMLQLAR 399
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG---RRTGLGVSGEVL------------INGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 400 IA------DKQISEATLRSFLGsfgFSGErmdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL 473
Cdd:cd03213 83 IIgyvpqdDILHPTLTVRETLM---FAAK-----LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 446536636 474 QDF--EGAVVLVS-HE-RQLIASVCDELLLVHGGKC 505
Cdd:cd03213 155 RRLadTGRTIICSiHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
311-514 |
5.29e-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: 71.84 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIA----EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGE--RKA 370
Cdd:cd03258 1 MIELKNVSKVFGDTGGKvtalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGKelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 371 SEllNIGYFAQH-----QMDALDGQASPmLQLARIADKQISEATLRsFLGSFGFSGERMDTPcESFSGGERARLALALIV 445
Cdd:cd03258 81 RR--RIGMIFQHfnllsSRTVFENVALP-LEIAGVPKAEIEERVLE-LLELVGLEDKADAYP-AQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 446 WQRPNVLILDEPTNHLD-------LDMRHALSmalQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEfEGDLQD 514
Cdd:cd03258 156 ANNPKVLLCDEATSALDpettqsiLALLRDIN---RELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE-EGTVEE 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-223 |
6.18e-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: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVKALDMp 79
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG--------LLRPTSGRVRLDGADISQWDP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 aidfvlsgdEEYWDIQNKLAQPEQLTDSDLAklhgrfDEIhgysapskaaqlmaglgflehqlrlnvasFSGGWRMRLNL 159
Cdd:cd03246 72 ---------NELGDHVGYLPQDDELFSGSIA------ENI-----------------------------LSGGQRQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLdAITDHILHIENQEL 223
Cdd:cd03246 108 ARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
312-458 |
6.24e-14 |
|
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: 71.31 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLN---IGYF 379
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrditGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQHQMdaLDGQASPM--LQL-ARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDE 456
Cdd:cd03224 81 PEGRR--IFPELTVEenLLLgAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
..
gi 446536636 457 PT 458
Cdd:cd03224 159 PS 160
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-206 |
6.28e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKALD-MPaidfvlsgdee 90
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDsLP----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 91 ywdiqnklaqpeqLTDSDLAKLhGRFDEIHGYSAPSKAAQ------LMA-GLGFLEHQlrlNVASFSGGWRMRLNLARTL 163
Cdd:NF040873 72 -------------LTVRDLVAM-GRWARRGLWRRLTRDDRaavddaLERvGLADLAGR---QLGELSGGQRQRALLAQGL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446536636 164 MSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG---TLILISHDRD 206
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
307-504 |
6.87e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.26 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSsplLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLP--LLAGERka 370
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGletpdsgrivlngrDLFtnLPPRER-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 371 sellNIGYFAQH-----QMD-------ALDGQASPMLQLARIADKQISEATLRSFlgsfgfsGERMdtPCEsFSGGERAR 438
Cdd:COG1118 76 ----RVGFVFQHyalfpHMTvaeniafGLRVRPPSKAEIRARVEELLELVQLEGL-------ADRY--PSQ-LSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 439 LALA--LIVwqRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1118 142 VALAraLAV--EPEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-184 |
7.40e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTL---FAALL----GSLGADEGSLTRPSVWTVAHMAQEV 73
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLppaaGTIKLDGGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 74 KALDmPAidfvLSGDE--EYWdiqnklaqpeqltdsdlAKLHGRFDeihgySAPSKAAQLMaGLGFLEHqlrLNVASFSG 151
Cdd:PRK13539 82 NAMK-PA----LTVAEnlEFW-----------------AAFLGGEE-----LDIAAALEAV-GLAPLAH---LPFGYLSA 130
|
170 180 190
....*....|....*....|....*....|...
gi 446536636 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAI 184
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
312-504 |
1.16e-13 |
|
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: 70.93 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGE----RKASEL--LNIGYF 379
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditgLPPHEIarLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQH-----QMDALD--------GQASPMLQLARIADKQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVW 446
Cdd:cd03219 81 FQIprlfpELTVLEnvmvaaqaRTGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 447 QRPNVLILDEPTNHLDLDMRHALS---MALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAeliRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-222 |
1.36e-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: 69.94 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 32 LTGVNGAGKSTLFAALLGSL-GadEGSLTRPSVWTVAHMAQEVKALDMPAIDFVLSGDEEYwDIQNKLAQPEQ---LTDS 107
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALtG--ELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKY-TITRSLAILENvifCHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 108 DLAKLhgrfdeihgysapskaaqLMAGLGFLehqlrlnvasfSGGWRM------RLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:cd03240 104 ESNWP------------------LLDMRGRC-----------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446536636 182 DAI-LWLEDWLKAYEGT----LILISHDRDFLDAItDHILHIENQE 222
Cdd:cd03240 155 ENIeESLAEIIEERKSQknfqLIVITHDEELVDAA-DHIYRVEKDG 199
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
312-492 |
1.51e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.08 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------RKASELL--NI 376
Cdd:COG2884 2 IRFENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkRREIPYLrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GY-FAQHQ----MDALDGQASPmLQLARIADKQIsEATLRSFLGSFGFSGeRMDTPCESFSGGERARLAL--ALIVwqRP 449
Cdd:COG2884 82 GVvFQDFRllpdRTVYENVALP-LRVTGKSRKEI-RRRVREVLDLVGLSD-KAKALPHELSGGEQQRVAIarALVN--RP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446536636 450 NVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIAS 492
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
312-504 |
1.69e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.17 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIaeKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG---------------ERKASELlni 376
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGrilwngqdltalppaERPVSML--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 gyFAQH----QMDALDGQA---SPMLQLARIADKQISEATLRSFLGSFGfsgERMdtpCESFSGGERARLALA-LIVWQR 448
Cdd:COG3840 77 --FQENnlfpHLTVAQNIGlglRPGLKLTAEQRAQVEQALERVGLAGLL---DRL---PGQLSGGQRQRVALArCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 449 PnVLILDEPTNHLDLDMRH---ALSMALQDFEGAVVL-VSHERQLIASVCDELLLVHGGK 504
Cdd:COG3840 149 P-ILLLDEPFSALDPALRQemlDLVDELCRERGLTVLmVTHDPEDAARIADRVLLVADGR 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
1.89e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.08 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHM--- 69
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdLSRLKRREIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 70 ----AQEVKAL-DMPAID---FVLsgdeeywdiqnklaqpeqltdsdlaklhgrfdEIHGYSAPSKAAQLMAGL---GfL 138
Cdd:COG2884 81 igvvFQDFRLLpDRTVYEnvaLPL--------------------------------RVTGKSRKEIRRRVREVLdlvG-L 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 139 EHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILI-SHDRDFLDAITDHI 215
Cdd:COG2884 128 SDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRV 207
|
....*....
gi 446536636 216 LHIENQELT 224
Cdd:COG2884 208 LELEDGRLV 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
2.56e-13 |
|
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: 72.63 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVS----LRRGGRVlfqKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWT 65
Cdd:COG1123 260 LLEVRNLSkrypVRGKGGV---RAvddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSilfdgkdLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 66 VAHMAQEV--------KALD--MPAidfvlsGDEeywdiqnkLAQPeqltdsdlAKLHGRFDEIhgySAPSKAAQLMAGL 135
Cdd:COG1123 337 LRELRRRVqmvfqdpySSLNprMTV------GDI--------IAEP--------LRLHGLLSRA---ERRERVAELLERV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 136 GFLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIL-WLEDWLKAYEGTLILISHDRDFLDAI 211
Cdd:COG1123 392 GLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqAQILnLLRDLQRELGLTYLFISHDLAVVRYI 471
|
....*
gi 446536636 212 TDHIL 216
Cdd:COG1123 472 ADRVA 476
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-502 |
3.43e-13 |
|
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: 72.51 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 30 IGLTGVNGAGKSTLFAALLGSLGADEGSLTRPsvwtvahmaqevkaldmPAIDFVL---SGDE--EYW-DIQN---KLAQ 100
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEE-----------------PSWDEVLkrfRGTElqDYFkKLANgeiKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 101 PEQLTD----------SDLAKlhgRFDEiHGysapsKAAQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLL 170
Cdd:COG1245 165 KPQYVDlipkvfkgtvRELLE---KVDE-RG-----KLDELAEKLG-LENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 171 LLDEPTNHLDL-------DAILWLEDWLKAyegtLILISHDRDFLDAITDHIlHIenqeltLY--TGNYSTFETTRSerl 241
Cdd:COG1245 235 FFDEPSSYLDIyqrlnvaRLIRELAEEGKY----VLVVEHDLAILDYLADYV-HI------LYgePGVYGVVSKPKS--- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 242 aqqqqafekqqeARAHLQKFID--------RFKakatkarqaqsrikqlermqqlapahvDTPFTFSFREPT--KMSSPL 311
Cdd:COG1245 301 ------------VRVGINQYLDgylpeenvRIR---------------------------DEPIEFEVHAPRreKEEETL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDkkiaekIKL-----QITPNSRIGLLGMNGAGKSTLIKslvgdlpLLAGERKASE-----LLNIGYFAQ 381
Cdd:COG1245 342 VEYPDLTKSYGG------FSLeveggEIREGEVLGIVGPNGIGKTTFAK-------ILAGVLKPDEgevdeDLKISYKPQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HQMDALDGQASPMLqlariadkqiSEATLRSFLGSF-------GFSGER-MDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:COG1245 409 YISPDYDGTVEEFL----------RSANTDDFGSSYykteiikPLGLEKlLDKNVKDLSGGELQRVAIAACLSRDADLYL 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 454 LDEPTNHLDLDMRHALSMALQDF---EGAVVLV-SHERQLIASVCDELLLVHG 502
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRFaenRGKTAMVvDHDIYLIDYISDRLMVFEG 531
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
308-502 |
3.45e-13 |
|
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: 70.07 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 308 SSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER----KASELL--- 374
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRDitglPPHRIArlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 ------NIGYF------------AQHQMDALDGQASPMLQLARIADKQISEATLRsFLGSFGFsGERMDTPCESFSGGER 436
Cdd:COG0411 81 iartfqNPRLFpeltvlenvlvaAHARLGRGLLAALLRLPRARREEREARERAEE-LLERVGL-ADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 437 ARLALALIVWQRPNVLILDEPTNHLDLDMRHALS---MALQDFEG-AVVLVSHERQLIASVCDELL-LVHG 502
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAeliRRLRDERGiTILLIEHDMDLVMGLADRIVvLDFG 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-220 |
4.73e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTR--PSVWTVAHMAQEVKALdMP 79
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgEPVPSRARHARQRVGV-VP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 AIDFVlsgDEEYWDIQNKLaqpeqltdsdlakLHGRFdeiHGYSAPSKAAQLMAGLGF--LEHQLRLNVASFSGGWRMRL 157
Cdd:PRK13537 87 QFDNL---DPDFTVRENLL-------------VFGRY---FGLSAAAARALVPPLLEFakLENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 158 NLARTLMSRSDLLLLDEPTNHLDLDA--ILW--LEDWLkAYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
308-500 |
4.93e-13 |
|
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: 71.93 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 308 SSPLLTLENASIGYGDKKIAEK-IKLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPLLAGERkASELL 374
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRpVSFTVPPGERVALVGPSGAGKSTLLNLLlgfvdptegsiaVNGVPLADADA-DSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 NIGYFAQH-QMdaLDGQASPMLQLAR--IADKQISEATLRSFLGSFGFS-GERMDTPCES----FSGGERARLALALIVW 446
Cdd:TIGR02857 397 QIAWVPQHpFL--FAGTIAENIRLARpdASDAEIREALERAGLDEFVAAlPQGLDTPIGEggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 447 QRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIAsVCDELLLV 500
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAA-LADRIVVL 529
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
330-504 |
6.13e-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: 68.29 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASE-------LLNIGY-FAQHQ----MDALDG 389
Cdd:cd03255 23 VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgtdiSKLSEkelaafrRRHIGFvFQSFNllpdLTALEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QASPMLqLARIADKQIsEATLRSFLGSFGFsGERMDTPCESFSGGERARLALA--LIvwQRPNVLILDEPTNHLDLDMRH 467
Cdd:cd03255 103 VELPLL-LAGVPKKER-RERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIAraLA--NDPKIILADEPTGNLDSETGK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446536636 468 A---LSMALQDFEG-AVVLVSHERQLiASVCDELLLVHGGK 504
Cdd:cd03255 178 EvmeLLRELNKEAGtTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-215 |
7.95e-13 |
|
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: 67.92 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEvkaldMPAIDFVLSGDeeywdiqnklAQ 100
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-----RQSLGYCPQFD----------AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 101 PEQLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGFLEHQLRLnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTnhLD 180
Cdd:cd03263 87 FDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKR-ARTLSGGMKRKLSLAIALIGGPSVLLLDEPT--SG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446536636 181 LDA----ILWleDWLKAYEG--TLILISHDRDFLDAITDHI 215
Cdd:cd03263 164 LDPasrrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
8.71e-13 |
|
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: 68.30 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVkaldmpai 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG--------LLRPDSGEVLIDGEDI-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 dFVLSGDEEYwDIQNK---LAQPEQLTDS-----DLA---KLHGRFDEihgysaPSKAAQLMAGLGF--LEHQLRLNVAS 148
Cdd:cd03261 65 -SGLSEAELY-RLRRRmgmLFQSGALFDSltvfeNVAfplREHTRLSE------EEIREIVLEKLEAvgLRGAEDLYPAE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDwlkAYEGTLILISHDRDFLDAITDHIL 216
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKK---ELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
312-514 |
9.07e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.37 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLN-IGY------ 378
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILApdsgevLWDGEPLDPEDRRrIGYlpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 379 -------------FAQ-HQMDALDgqaspmlqlariADKQISEatlrsFLGSFGFsGERMDTPCESFSGGE--RARLALA 442
Cdd:COG4152 82 lypkmkvgeqlvyLARlKGLSKAE------------AKRRADE-----WLERLGL-GDRANKKVEELSKGNqqKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 443 LIvwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGA-VVLVSHERQLIASVCDELLLVHGGKcTEFEGDLQD 514
Cdd:COG4152 144 LL--HDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTtVIFSSHQMELVEELCDRIVIINKGR-KVLSGSVDE 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-504 |
9.81e-13 |
|
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: 71.01 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLG--SLGADEGSLtrpsVWTVAHM-AQEVKALDMPAIDFV---------LSGD 88
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEI----YWSGSPLkASNIRDTERAGIVIIhqeltlvpeLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 89 EEYWdIQNKLAQPEQLTDSDLAKLhgrfdeihgysapsKAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSD 168
Cdd:TIGR02633 97 ENIF-LGNEITLPGGRMAYNAMYL--------------RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 169 LLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHILHIENQEltlytgnystfettrserlaqqq 245
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ----------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 246 qafekqqearaHLqkfidrfkakATKARQAQSR---IKQL--ERMQQLAPahvdtpftfsfREPTKMSSPLLTLENASIG 320
Cdd:TIGR02633 219 -----------HV----------ATKDMSTMSEddiITMMvgREITSLYP-----------HEPHEIGDVILEARNLTCW 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 321 YGD---KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPllaGERKASELLNigyfaQHQMDALDGQASPMLQL 397
Cdd:TIGR02633 267 DVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP---GKFEGNVFIN-----GKPVDIRNPAQAIRAGI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 398 ARIAD--------------KQISEATLRSF-----------LGSFGFSGERM-------DTPCESFSGGERARLALALIV 445
Cdd:TIGR02633 339 AMVPEdrkrhgivpilgvgKNITLSVLKSFcfkmridaaaeLQIIGSAIQRLkvktaspFLPIGRLSGGNQQKAVLAKML 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 446 WQRPNVLILDEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKyeiYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-219 |
1.32e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRR-GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVK----- 74
Cdd:COG4178 362 ALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYlplgt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 75 ---ALDMPAIDFVLSgDEEYWDIqnklaqpeqLTDSDLAKLHGRFDEIHGYSapskaaqlmaglgfleHQLrlnvasfSG 151
Cdd:COG4178 442 lreALLYPATAEAFS-DAELREA---------LEAVGLGHLAERLDEEADWD----------------QVL-------SL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKA--YEGTLILISHdRDFLDAITDHILHIE 219
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
330-505 |
1.60e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.94 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP-----LLAGER----KASELLNI-GYFAQHQMdaldgQASPM----- 394
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPlsdwSAAELARHrAYLSQQQS-----PPFAMpvfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 395 --LQLARIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGE--RARLALALI-VWQRPN----VLILDEPTNHLDLDM 465
Cdd:COG4138 90 laLHQPAGASSEAVEQLLAQLAEALGLE-DKLSRPLTQLSGGEwqRVRLAAVLLqVWPTINpegqLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 466 RHALSMALQDF---EGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:COG4138 169 QAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
312-495 |
2.17e-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: 67.21 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEK-IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLN----I 376
Cdd:cd03256 1 IEVENLSKTYPNGKKALKdVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlidgtdinkLKGKALRQlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQH-----QMDALD-------GQAS---PMLQLARIADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLAL 441
Cdd:cd03256 81 GMIFQQfnlieRLSVLEnvlsgrlGRRStwrSLFGLFPKEEKQRALAALER-VGLLDKAYQRADQ----LSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 442 ALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVS-HERQLIASVCD 495
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYAD 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
307-504 |
2.53e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.59 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----RKASELL----NIG 377
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRilldgRDVTGLPpekrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 378 YFAQH-----QMDALD----GqaspmLQLARIADKQIsEATLRSFLGSFGFSG--ERMdtPCEsFSGGERARLALA--LI 444
Cdd:COG3842 81 MVFQDyalfpHLTVAEnvafG-----LRMRGVPKAEI-RARVAELLELVGLEGlaDRY--PHQ-LSGGQQQRVALAraLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 445 VwqRPNVLILDEPTNHLDL----DMRHALSMALQDFEGAVVLVSHErQLIA-SVCDELLLVHGGK 504
Cdd:COG3842 152 P--EPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHD-QEEAlALADRIAVMNDGR 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-216 |
2.55e-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: 67.08 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHMA-----QE 72
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgedITGLPPHEIARLGigrtfQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 73 VKAL-DMPAIDFVLSGdeeywdiqnklAQPEQLTDSDLAKLHGRFDEihgysAPSKAAQLMAGLGfLEHQLRLNVASFSG 151
Cdd:cd03219 84 PRLFpELTVLENVMVA-----------AQARTGSGLLLARARREERE-----ARERAEELLERVG-LADLADRPAGELSY 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 152 GWRMRLNLARTLMSRSDLLLLDEPT---NHLDLDAIL-WLEDwLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAeLIRE-LRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
330-507 |
2.58e-12 |
|
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: 67.52 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERKASELLNIGYFAQHQMDALDGQAS--- 392
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLGlekpaqgtvsfrgqDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMTvrq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 393 ----PMLQLARIaDKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:TIGR02769 110 iigePLRHLTSL-DESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 469 LSMAL----QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:TIGR02769 189 ILELLrklqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
3.49e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKaldmpa 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 idfvlsgdeeywdiqnklaqpeqlTDSDLAKLHGRFDEIHGysaPSKAAQLMAGLGFLE--HQLRLNVASFSGGWRMRLN 158
Cdd:PRK09544 78 ------------------------LDTTLPLTVNRFLRLRP---GTKKEDILPALKRVQagHLIDAPMQKLSGGETQRVL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTL----ILISHDRDFLDAITDHIL 216
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVL 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
3.81e-12 |
|
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: 66.38 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPsvwtVAHMAQEV 73
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgKD----LLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 74 KALDMPAIDFVlsgdeeYWDIQNKLaQP-----EQLTDSdlAKLHGRfdeIHGYSAPSKAA-QLMAGLGFLEHQLRLNVA 147
Cdd:cd03257 77 RKIRRKEIQMV------FQDPMSSL-NPrmtigEQIAEP--LRIHGK---LSKKEARKEAVlLLLVGVGLPEEVLNRYPH 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKA-YEGTLILISHDRDFLDAITDHIL 216
Cdd:cd03257 145 ELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
316-507 |
4.11e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 316 NASIGYGDKKIA--EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------------RKASELLNIGY 378
Cdd:PRK10584 13 KKSVGQGEHELSilTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEvslvgqplhqmdeeaRAKLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 379 FAQHQM-----DALDGQASPMLqLARIADKQiSEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK10584 93 VFQSFMliptlNALENVELPAL-LRGESSRQ-SRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 454 LDEPTNHLD-------LDMRHALSmalQDFEGAVVLVSHERQLiASVCDELLLVHGGKCTE 507
Cdd:PRK10584 170 ADEPTGNLDrqtgdkiADLLFSLN---REHGTTLILVTHDLQL-AARCDRRLRLVNGQLQE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-223 |
4.34e-12 |
|
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: 65.97 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALlgslgadeGSLTRPSVWTVAHMAQEVKALD 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQAlkgvSLSIEKGEFVAIVGPSGSGKSTLLNIL--------GGLDRPTSGEVRVDGTDISKLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 MPAID--------FVLsgdeeywdiQNKLAQPEqLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGfLEHQLRLNVASF 149
Cdd:cd03255 73 EKELAafrrrhigFVF---------QSFNLLPD-LTALENVELPLLLAGVPKKERRERAEELLERVG-LGDRLNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AIL-WLEDWLKAYEGTLILISHDRDfLDAITDHILHIENQEL 223
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkEVMeLLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
285-504 |
5.24e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 285 MQQLaPAHVDTPFTfsfreptkmssplltLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIK--------- 355
Cdd:PRK10575 1 MQEY-TNHSDTTFA---------------LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKmlgrhqpps 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 356 ---SLVGDLPLLAGERKASELlNIGYFAQhQMDALDGQASPML----------QLAR--IADKQISEATLrSFLGSFGFS 420
Cdd:PRK10575 65 egeILLDAQPLESWSSKAFAR-KVAYLPQ-QLPAAEGMTVRELvaigrypwhgALGRfgAADREKVEEAI-SLVGLKPLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 421 GERMDtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLD-------LDMRHALSmalQDFEGAVVLVSHERQLIASV 493
Cdd:PRK10575 142 HRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqvdvLALVHRLS---QERGLTVIAVLHDINMAARY 214
|
250
....*....|.
gi 446536636 494 CDELLLVHGGK 504
Cdd:PRK10575 215 CDYLVALRGGE 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-228 |
6.99e-12 |
|
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: 65.82 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 18 QKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT----RPSVWTVAHMAQevkaldmpaIDFVLSGDEE-YW 92
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglVPWKRRKKFLRR---------IGVVFGQKTQlWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 93 DIQ-----NKLAQPEQLTDSDLAKlhgRFDEIhgysapskaAQLMAglgfLEHQLRLNVASFSGGWRMRLNLARTLMSRS 167
Cdd:cd03267 109 DLPvidsfYLLAAIYDLPPARFKK---RLDEL---------SELLD----LEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 168 DLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQELtLYTG 228
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-181 |
7.48e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.91 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAH----M 69
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvrlngrpLAAWSPWELARrravL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 70 AQEVK-ALDMPAIDFVLSGdeeywdiqnklAQPeqltdsdLAKLHGRFDEIhgysapskAAQLMA--GLGFLEHQlrlNV 146
Cdd:COG4559 81 PQHSSlAFPFTVEEVVALG-----------RAP-------HGSSAAQDRQI--------VREALAlvGLAHLAGR---SY 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446536636 147 ASFSGGWRMRLNLARTL-------MSRSDLLLLDEPTNHLDL 181
Cdd:COG4559 132 QTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-180 |
1.05e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 64.52 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWkIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMaQEVKAL----- 76
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRigylp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 -------DMPAIDFVlsgdeEYwdiqnklaqpeqltdsdLAKLHGrfdeIHGYSAPSKAAQLMAGLGFLEHQLRLnVASF 149
Cdd:cd03264 79 qefgvypNFTVREFL-----DY-----------------IAWLKG----IPSKEVKARVDEVLELVNLGDRAKKK-IGSL 131
|
170 180 190
....*....|....*....|....*....|.
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03264 132 SGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
311-491 |
1.18e-11 |
|
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: 64.68 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKK----IAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAGER-------KASEL 373
Cdd:TIGR02211 1 LLKCENLGKRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGlDNPtsgevLFNGQSlsklssnERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 374 LNI--GYFAQ--HQM---DALDGQASPMLqlarIADKQISEATLRSF--LGSFGFsGERMDTPCESFSGGERARLALALI 444
Cdd:TIGR02211 81 RNKklGFIYQfhHLLpdfTALENVAMPLL----IGKKSVKEAKERAYemLEKVGL-EHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446536636 445 VWQRPNVLILDEPTNHLD-------LDMRHALSmalQDFEGAVVLVSHERQLIA 491
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDnnnakiiFDLMLELN---RELNTSFLVVTHDLELAK 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-204 |
1.19e-11 |
|
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: 64.89 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGsltRPSVWTVAHMAQEVKALDMPAI 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG---APDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 D--------------FVLSgdeeywdIQNKLAQPEQLTDSdlaKLHGRFDEIhgysapSKAAQLMAGLgFLEHQLRLNVA 147
Cdd:cd03260 78 ElrrrvgmvfqkpnpFPGS-------IYDNVAYGLRLHGI---KLKEELDER------VEEALRKAAL-WDEVKDRLHAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK--AYEGTLILISHD 204
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
312-490 |
1.22e-11 |
|
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: 64.09 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDlP---------LLAGErkasELLNI------ 376
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyevtegeiLFKGE----DITDLppeera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 --GYFAQHQmdaldgqaSPMlqlariadkQISEATLRSFLGSFGfsgermdtpcESFSGGERARLALALIVWQRPNVLIL 454
Cdd:cd03217 76 rlGIFLAFQ--------YPP---------EIPGVKNADFLRYVN----------EGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 446536636 455 DEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLI 490
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLreEGkSVLIITHYQRLL 167
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-220 |
1.44e-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: 63.36 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVwTVAHMAQEVKALDmPAI 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-DLTDLEDELPPLR-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFVlsgdeeywdIQNklaqpeqltdsdlaklhgrfdeihgysapskaAQLMAGLGFLEhqlrlNVA-SFSGGWRMRLNLA 160
Cdd:cd03229 79 GMV---------FQD--------------------------------FALFPHLTVLE-----NIAlGLSGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK---AYEG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKslqAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-507 |
1.49e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.93 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLnigyfaqhqmdaLDGQA 391
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVY------------LDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 --------------------SPM------------LQLARIA-DKQISEATLRSFLGSFGFSGE---RMDTPCESFSGGE 435
Cdd:PRK14247 72 ifkmdvielrrrvqmvfqipNPIpnlsifenvalgLKLNRLVkSKKELQERVRWALEKAQLWDEvkdRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 436 RARLALALIVWQRPNVLILDEPTNHLDLDMR---HALSMALQDfEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTakiESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
309-458 |
1.81e-11 |
|
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: 64.23 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 SPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASEL--LNI 376
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSirfdgeditgLPPHRIarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GY-------FAQhqmdaldgqaspM-----LQLARIA--DKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLAL- 441
Cdd:COG0410 81 GYvpegrriFPS------------LtveenLLLGAYArrDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIg 148
|
170
....*....|....*...
gi 446536636 442 -ALIvwQRPNVLILDEPT 458
Cdd:COG0410 149 rALM--SRPKLLLLDEPS 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-180 |
1.93e-11 |
|
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: 67.63 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLgSLGADEGSLTRPSV-WTVAHMAQEVKALD-MPAIDFVLSGde 89
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVsWNSVTLQTWRKAFGvIPQKVFIFSG-- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 90 eywDIQNKLAQPEQLTDSDLAKLHgrfDEIhgySAPSKAAQLMAGLGFlehQLRLNVASFSGGWRMRLNLARTLMSRSDL 169
Cdd:TIGR01271 1307 ---TFRKNLDPYEQWSDEEIWKVA---EEV---GLKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|.
gi 446536636 170 LLLDEPTNHLD 180
Cdd:TIGR01271 1375 LLLDEPSAHLD 1385
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
328-502 |
2.02e-11 |
|
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: 67.73 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 328 EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKA---SELLNIGYFAQH-----QMDALD----GQASPML 395
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagkSILTNISDVHQNmgycpQFDAIDdlltGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 396 --QLARIADKQISEATLRSfLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHAL---S 470
Cdd:TIGR01257 2036 yaRLRGVPAEEIEKVANWS-IQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwntI 2113
|
170 180 190
....*....|....*....|....*....|...
gi 446536636 471 MALQDFEGAVVLVSHERQLIASVCDEL-LLVHG 502
Cdd:TIGR01257 2114 VSIIREGRAVVLTSHSMEECEALCTRLaIMVKG 2146
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
312-508 |
2.07e-11 |
|
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: 63.59 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDK--KIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqMDALDG 389
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE--------------IDGIDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QASPMLQLAR----IA-DKQISEATLRSFLGSFG-------FSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:cd03369 73 STIPLEDLRSsltiIPqDPTLFSGTIRSNLDPFDeysdeeiYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 458 TNHLDLDMRHALSMAL-QDFEGAVVL-VSHERQLIASvCDELLLVHGGKCTEF 508
Cdd:cd03369 153 TASIDYATDALIQKTIrEEFTNSTILtIAHRLRTIID-YDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
322-506 |
2.15e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 322 GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLN-----IGYFAQHQMDALdgq 390
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKptsgsvLIRGEPITKENIRevrkfVGLVFQNPDDQI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 391 ASPMLQlARIA--------DKQISEATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13652 92 FSPTVE-QDIAfgpinlglDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 463 LDMRHALSMALQDFEG----AVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK13652 170 PQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
321-504 |
2.36e-11 |
|
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: 63.70 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 321 YGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPLLAGERKASEL-LNIGYFAQH----- 382
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdsgtiiIDGLKLTDDKKNINELrQKVGMVFQQfnlfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 QMDALDGQASPmLQLARIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03262 90 HLTVLENITLA-PIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 463 LDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03262 168 PELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
312-506 |
2.54e-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: 62.45 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKA----SELLNIGYFAQ 381
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKpdsgeiLVDGKEVSfaspRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HQMdaldgqaspmlqlariadkqiseatlrsflgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03216 81 YQL-----------------------------------------------SVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 462 DLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:cd03216 114 TPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
312-504 |
2.59e-11 |
|
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: 63.26 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEK-----IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASEllNIGYFAQhqmda 386
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 387 ldgqaSPMLQlariadkqisEATLRS---FlgsfgfsGERMDTP--------CE---------------------SFSGG 434
Cdd:cd03250 74 -----EPWIQ----------NGTIREnilF-------GKPFDEEryekvikaCAlepdleilpdgdlteigekgiNLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 435 ERARLALALIVWQRPNVLILDEPTNHLDLD-----MRHALSMALQDfEGAVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHvgrhiFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
307-462 |
2.79e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSL--VGDL-P--LLAGE-------------- 367
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLnPevTITGSivynghniysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 368 ----RKasellNIGYFAQhqmdaldgQASPM-----------LQLARIADKQI-SEATLRSFLGS--FGFSGERMDTPCE 429
Cdd:PRK14239 81 tvdlRK-----EIGMVFQ--------QPNPFpmsiyenvvygLRLKGIKDKQVlDEAVEKSLKGAsiWDEVKDRLHDSAL 147
|
170 180 190
....*....|....*....|....*....|...
gi 446536636 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-203 |
2.83e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.24 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT-----RPSVWTVAHMAQEVkal 76
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpVPARARLARARIGV--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 dMPAIDFVlsgDEEYWDIQNKLaqpeqltdsdlakLHGRFdeiHGYSAPSKAAQLMAGLGF--LEHQLRLNVASFSGGWR 154
Cdd:PRK13536 119 -VPQFDNL---DLEFTVRENLL-------------VFGRY---FGMSTREIEAVIPSLLEFarLESKADARVSDLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDA--ILW--LEDWLkAYEGTLILISH 203
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLL-ARGKTILLTTH 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
312-504 |
2.85e-11 |
|
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: 63.90 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAGERKASELL---NIGYFAQH 382
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPdsgtiLFGGEDATDVPVqerNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 -----QMDALDGQASPmLQLARIADKQiSEATLR----SFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLI 453
Cdd:cd03296 83 yalfrHMTVFDNVAFG-LRVKPRSERP-PEAEIRakvhELLKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 454 LDEPTNHLDLDMRHALSMALQDFEGAV----VLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-206 |
3.50e-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: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGAD---EGSL----TRpsvwtVAHMAQEV 73
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVllngRR-----LTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 74 KALDMPAIDFVLSgdeEYWDIQNKLAqpeqltdsdlaklhgrFDEIHGYSAPSKAAQLM-----AGLGFLEHQlrlNVAS 148
Cdd:COG4136 76 RRIGILFQDDLLF---PHLSVGENLA----------------FALPPTIGRAQRRARVEqaleeAGLAGFADR---DPAT 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDW----LKAYEGTLILISHDRD 206
Cdd:COG4136 134 LSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE 195
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
312-514 |
3.60e-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: 63.45 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------------RKASelLNIG 377
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKilidgqdithlpmhERAR--LGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 378 YFAQhqmdaldgQAS------------PMLQLARIADKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIV 445
Cdd:TIGR04406 80 YLPQ--------EASifrkltveenimAVLEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 446 WQRPNVLILDEPTNHLD----LDMRHaLSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTeFEGDLQD 514
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDpiavGDIKK-IIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVL-AEGTPAE 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
311-504 |
3.63e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------RKASELLNIGY 378
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 379 FAQH-----QMDALDGQASpMLQLARIADKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK10895 83 LPQEasifrRLSVYDNLMA-VLQIRDDLSAEQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 454 LDEPTNHLD----LDMRHALSMaLQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK10895 161 LDEPFAGVDpisvIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
323-510 |
3.74e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 323 DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLNI----GYFAQHqmdaldg 389
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditDKKVKLSDIrkkvGLVFQY------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 qasPMLQLAR------IA---------DKQISEATLRSfLGSFGFSGERM--DTPCEsFSGGERARLALALIVWQRPNVL 452
Cdd:PRK13637 92 ---PEYQLFEetiekdIAfgpinlglsEEEIENRVKRA-MNIVGLDYEDYkdKSPFE-LSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 453 ILDEPTNHLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDELLLVHGGKCtEFEG 510
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKC-ELQG 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-504 |
4.19e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLL---AGE---------RKASELL-NIGY-FAQHQ--------MDAL 387
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---ILvptSGEvrvlgyvpfKRRKEFArRIGVvFGQRSqlwwdlpaIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 388 DgqaspmLqLARIADkqISEATLRSFLGSF--GFS-GERMDTPCESFSGGERAR--LALALIvwQRPNVLILDEPTNHLD 462
Cdd:COG4586 118 R------L-LKAIYR--IPDAEYKKRLDELveLLDlGELLDTPVRQLSLGQRMRceLAAALL--HRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446536636 463 LDMRHalsmALQDF-------EGA-VVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG4586 187 VVSKE----AIREFlkeynreRGTtILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
333-506 |
4.98e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 333 QITPNSRIGLLGMNGAGKSTLIKSLVGDLP-----LLAG----ERKASELLNI-GYFAQHQMDALDGQASPMLQLARIAD 402
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiQFAGqpleAWSAAELARHrAYLSQQQTPPFAMPVFQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 403 KQI--SEATLRSFLGSFGFsGERMDTPCESFSGGE--RARLALA-LIVWQRPN----VLILDEPTNHLDLDMRHALSMAL 473
Cdd:PRK03695 98 TRTeaVASALNEVAEALGL-DDKLGRSVNQLSGGEwqRVRLAAVvLQVWPDINpagqLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 446536636 474 QDFE---GAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK03695 177 SELCqqgIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
309-507 |
5.24e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 SPLLTLENASIGY---------GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLA 365
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlespsqgnvswrgePLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 366 GERKASELLNIGYFAQHQMDALDGQ-------ASPMLQLARIaDKQISEATLRSFLGSFGFSGERMDTPCESFSGG--ER 436
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRktvreiiREPLRHLLSL-DKAERLARASEMLRAVDLDDSVLDKRPPQLSGGqlQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 437 ARLALALIVwqRPNVLILDEPTNHLDLdMRHALSMAL-----QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK10419 160 VCLARALAV--EPKLLILDEAVSNLDL-VLQAGVIRLlkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
329-504 |
5.34e-11 |
|
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: 62.70 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 329 KIKLQiTPNSRIGLLGMNGAGKSTLIKSLVG------------DLPLLAGERK---ASELLNIGY-FAQHQ----MDALD 388
Cdd:cd03297 16 KIDFD-LNEEVTGIFGASGAGKSTLLRCIAGlekpdggtivlnGTVLFDSRKKinlPPQQRKIGLvFQQYAlfphLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 389 GQASPMLQLARIADKQISEATLRSF-LGSFGFSgermdtPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH 467
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLgLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446536636 468 ALSMAL----QDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03297 169 QLLPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-203 |
5.90e-11 |
|
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: 61.99 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---TRPSVWTVAHMAQEVKAL-DMPA 80
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwnGTPLAEQRDEPHENILYLgHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 IDFVLSGDE--EYWdiqNKLAQPEQLTDSD-LAKlhgrfdeihgysapskaaqlmAGLGFLEHqlrLNVASFSGGWRMRL 157
Cdd:TIGR01189 84 LKPELSALEnlHFW---AAIHGGAQRTIEDaLAA---------------------VGLTGFED---LPAAQLSAGQQRRL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446536636 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISH 203
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
312-485 |
6.35e-11 |
|
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: 62.49 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIA----EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLNIGYFAQ 381
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HQ-----MDALDGQASPmLQLARIADKQISEATlRSFLGSFGFSGERMDTPCEsFSGGERARLALA--LIVwqRPNVLIL 454
Cdd:cd03293 81 QDallpwLTVLDNVALG-LELQGVPKAEARERA-EELLELVGLSGFENAYPHQ-LSGGMRQRVALAraLAV--DPDVLLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 446536636 455 DEPTNHLD----LDMRHALSMALQDFEGAVVLVSH 485
Cdd:cd03293 156 DEPFSALDaltrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
318-507 |
6.38e-11 |
|
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: 65.53 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 318 SIGYGDKkIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGdlplLAGERKASELLN---------------IGYFAQH 382
Cdd:TIGR01193 482 SYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG----FFQARSGEILLNgfslkdidrhtlrqfINYLPQE 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 Q-------MDALDGQASPMLQLARIaDKQISEATLRSFLGSF--GFsGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:TIGR01193 557 PyifsgsiLENLLLGAKENVSQDEI-WAACEIAEIKDDIENMplGY-QTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 454 LDEPTNHLDLDMRHALS---MALQDfeGAVVLVSHeRQLIASVCDELLLVHGGKCTE 507
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVnnlLNLQD--KTIIFVAH-RLSVAKQSDKIIVLDHGKIIE 688
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
305-514 |
7.32e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 305 TKMSSPLLTLENASIGY----GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERKAS--------E 372
Cdd:PRK09473 6 QQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG---LLAANGRIGgsatfngrE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 373 LLNIgyfAQHQMDALDGQ------ASPMLQL---ARIAD---------KQISEATlrSFLGSFGF--------SGERMDT 426
Cdd:PRK09473 83 ILNL---PEKELNKLRAEqismifQDPMTSLnpyMRVGEqlmevlmlhKGMSKAE--AFEESVRMldavkmpeARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 427 PCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRhALSMAL-----QDFEGAVVLVSHERQLIASVCDELLLVH 501
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ-AQIMTLlnelkREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250
....*....|...
gi 446536636 502 GGKCTEFeGDLQD 514
Cdd:PRK09473 237 AGRTMEY-GNARD 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
312-505 |
8.62e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.02 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGD-KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHqmdaldgq 390
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 391 asPMLqlariadkqiSEATLRSFLgsfgfsgermdtpC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:cd03223 73 --PYL----------PLGTLREQL-------------IypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*....
gi 446536636 467 HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:cd03223 128 DRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
340-536 |
1.04e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.53 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVGDLPLLAGE-RKASELLNIGYFA--QHQMDALDGQASPMLQLArIADKQISEATLRsfLGS 416
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKvDRNGEVSVIAISAglSGQLTGIENIEFKMLCMG-FKRKEIKAMTPK--IIE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 417 FGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA---VVLVSHERQLIASV 493
Cdd:PRK13546 130 FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQF 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446536636 494 CDELLLVHGGKCTEFeGDLQD----YAKWLREARQQQINAQTAIEQN 536
Cdd:PRK13546 210 CTKIAWIEGGKLKDY-GELDDvlpkYEAFLNDFKKKSKAEQKEFRNK 255
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-225 |
1.05e-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: 60.79 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaldmp 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 aidfvlsgdeeywdiqnklaqpeqLTDSDLAKLHGRFDeiHGYSAPSKAAQLMAGlgflehQLRLNV-ASFSGGWRMRLN 158
Cdd:cd03247 61 ------------------------LDGVPVSDLEKALS--SLISVLNQRPYLFDT------TLRNNLgRRFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLD-LDAILWLEDWLKAYEG-TLILISHDrdfLDAIT--DHILHIENQELTL 225
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKDkTLIWITHH---LTGIEhmDKILFLENGKIIM 176
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
140-513 |
1.10e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 140 HQLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAYEG-TLILISHDRDFLDAITDHI 215
Cdd:PRK15134 155 HQL-------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQQELNmGLLFITHNLSIVRKLADRV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 216 LHIENQELTlytgnystfETTRSERLAQQQqafekqqeARAHLQKFIDRfkakatkarqaqsrikqlERMQQLAPAHVDT 295
Cdd:PRK15134 228 AVMQNGRCV---------EQNRAATLFSAP--------THPYTQKLLNS------------------EPSGDPVPLPEPA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 296 PftfsfreptkmssPLLTLENASIGYGDKK------IAEKIKLQ-----ITPNSRIGLLGMNGAGKST-------LIKS- 356
Cdd:PRK15134 273 S-------------PLLDVEQLQVAFPIRKgilkrtVDHNVVVKnisftLRPGETLGLVGESGSGKSTtglallrLINSq 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 357 ---LVGDLPLLAGERKasELLNIgyfaQHQMDAL----DGQASPMLQLARIAD-------KQIS----EATLRSFLGSFG 418
Cdd:PRK15134 340 geiWFDGQPLHNLNRR--QLLPV----RHRIQVVfqdpNSSLNPRLNVLQIIEeglrvhqPTLSaaqrEQQVIAVMEEVG 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 419 FSGE-RMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQ-DFEGAVVLVSHERQLIASV 493
Cdd:PRK15134 414 LDPEtRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAqilALLKSLQqKHQLAYLFISHDLHVVRAL 492
|
410 420
....*....|....*....|
gi 446536636 494 CDELLLVHGGKCTEfEGDLQ 513
Cdd:PRK15134 493 CHQVIVLRQGEVVE-QGDCE 511
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.14e-10 |
|
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: 60.52 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaldmpai 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 dfvlsgdeeywdiqnklaqpeqltdsdlakLHGRfdEIHGYSaPSKAAQlmAGLGFLeHQLrlnvasfSGGWRMRLNLAR 161
Cdd:cd03216 59 ------------------------------VDGK--EVSFAS-PRDARR--AGIAMV-YQL-------SVGERQMVEIAR 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISHRLDEVFEIADRV 152
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-221 |
1.21e-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: 62.04 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 30 IGLTGVNGAGKSTLFAALLGSLGADEGSLTRPsVWTVAHMAQEVKA-LDMPAIDFVLS-----GDEEYWdiQNKLAQPEQ 103
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKAdYEGTVRDLLSSitkdfYTHPYF--KTEIAKPLQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 104 LTDsdlaklhgrfdeihgysapskaaqlmaglgFLEHQLRlnvaSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA 183
Cdd:cd03237 105 IEQ------------------------------ILDREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446536636 184 ILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQ 221
Cdd:cd03237 151 RLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
307-485 |
1.30e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----RKASELLNI------ 376
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhyrMRDGQLRDLyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 ----------GYFAQHQMDALDGQASpmlqlariADKQISE--------------ATLRSFLGSFGFSGERMDTPCESFS 432
Cdd:PRK11701 82 errrllrtewGFVHQHPRDGLRMQVS--------AGGNIGErlmavgarhygdirATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 433 GGERARLALALIVWQRPNVLILDEPTNHLD-------LDMRHALsmaLQDFEGAVVLVSH 485
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGL---VRELGLAVVIVTH 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
312-507 |
1.72e-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: 61.73 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYG--DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAgerKASELLN 375
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfyvpengrvlvdghDLALAD---PAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 376 IGYFAQHQM---------DALDGQASPM---LQLARIADKQisEATLRSFLGSFGFSGERmdtpCESFSGGERARLALAL 443
Cdd:cd03252 78 VGVVLQENVlfnrsirdnIALADPGMSMervIEAAKLAGAH--DFISELPEGYDTIVGEQ----GAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
312-457 |
2.03e-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: 61.40 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------------RKASelLNIG 377
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpmhKRAR--LGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 378 YFAQhqmdaldgQAS------------PMLQLARIADKQISEaTLRSFLGSFGFSGERmDTPCESFSGGERARLALALIV 445
Cdd:cd03218 79 YLPQ--------EASifrkltveenilAVLEIRGLSKKEREE-KLEELLEEFHITHLR-KSKASSLSGGERRRVEIARAL 148
|
170
....*....|..
gi 446536636 446 WQRPNVLILDEP 457
Cdd:cd03218 149 ATNPKFLLLDEP 160
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-502 |
2.08e-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: 61.66 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 334 ITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErKASELLNIGYFAQH------------QMDALDGQ----------A 391
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-IEIELDTVSYKPQYikadyegtvrdlLSSITKDFythpyfkteiA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 SPmLQLARIADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03237 101 KP-LQIEQILDREVPE-----------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*
gi 446536636 472 ALQDF----EGAVVLVSHERQLIASVCDELLLVHG 502
Cdd:cd03237 157 VIRRFaennEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-223 |
2.29e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 3 QFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---TRP-SVWTVAHMAQEVKALdm 78
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldAQPlESWSSKAFARKVAYL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 79 paidfvlsgdeeywdiQNKLAQPEQLTDSDLAKLhGRFdEIHG----YSAPSKA----AQLMAGLGFLEHQLrlnVASFS 150
Cdd:PRK10575 91 ----------------PQQLPAAEGMTVRELVAI-GRY-PWHGalgrFGAADREkveeAISLVGLKPLAHRL---VDSLS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIENQEL 223
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-224 |
2.46e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 60.83 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGG-----RVLfQKASMQLHPGWKIGLTGVNGAGKSTLfaalLGSLGAdegsLTRPSvwtvahmaqevka 75
Cdd:COG1136 4 LLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTL----LNILGG----LDRPT------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 76 ldmpaidfvlSGdeEYW----DIqnklaqpEQLTDSDLAKLHGR--------------------------FDEIHGYSAP 125
Cdd:COG1136 62 ----------SG--EVLidgqDI-------SSLSERELARLRRRhigfvfqffnllpeltalenvalpllLAGVSRKERR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 126 SKAAQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAilwLEDWLKAYEGTL 198
Cdd:COG1136 123 ERARELLERVG-LGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTI 198
|
250 260
....*....|....*....|....*.
gi 446536636 199 ILISHDRDfLDAITDHILHIENQELT 224
Cdd:COG1136 199 VMVTHDPE-LAARADRVIRLRDGRIV 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
2.64e-10 |
|
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: 61.15 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSltrpsvwtvahmaqevkaldmpa 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE----------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 idfVLSGDEEYWDiqnklaqpeqLTDSDLAKLHGRF-----------------------DEIHGYSaPSKAAQL------ 131
Cdd:COG1127 62 ---ILVDGQDITG----------LSEKELYELRRRIgmlfqggalfdsltvfenvafplREHTDLS-EAEIRELvlekle 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 132 MAGLGFLEHQLrlnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD------LDA-ILWLEDWLKAyegTLILISHD 204
Cdd:COG1127 128 LVGLPGAADKM---PSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDElIRELRDELGL---TSVVVTHD 201
|
250 260 270
....*....|....*....|....*....|....*..
gi 446536636 205 RDFLDAITDHILHIENQELtLYTGNYSTFETTRSERL 241
Cdd:COG1127 202 LDSAFAIADRVAVLADGKI-IAEGTPEELLASDDPWV 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-203 |
2.73e-10 |
|
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: 60.20 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPSVWTVAHMAQEVKAL-DMPA 80
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARGLLYLgHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 IDFVLSGDE--EYWDIQNKLAQPEQLTDSdlaklhgrfdeihgysapskaaqlmAGLGFLEHqlrLNVASFSGGWRMRLN 158
Cdd:cd03231 84 IKTTLSVLEnlRFWHADHSDEQVEEALAR-------------------------VGLNGFED---RPVAQLSAGQQRRVA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISH 203
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-216 |
2.93e-10 |
|
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: 61.04 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRG-GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS----------LTRPSVWTV-AHM 69
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlidgtdinkLKGKALRQLrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 70 A---QEVKALD-MPAIDFVLSGdeeywdiqnKLAQpeqltDSDLAKLHGRFDEIHGYsapsKAAQLMAGLGFLEHQLRlN 145
Cdd:cd03256 81 GmifQQFNLIErLSVLENVLSG---------RLGR-----RSTWRSLFGLFPKEEKQ----RALAALERVGLLDKAYQ-R 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 146 VASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILIS-HDRDFLDAITDHIL 216
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIV 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
312-504 |
3.25e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDK-----KIAEKIKLQITPNSRIGLLGMNGAGKSTLIK------------SLVGDLPLLAGERKASELL 374
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 N----IGY---FAQHQM--DALDGQ-ASPMLQLAriADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALI 444
Cdd:PRK13645 87 RlrkeIGLvfqFPEYQLfqETIEKDiAFGPVNLG--ENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 445 VWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
310-508 |
3.75e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 310 PLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLvGDLPLLAGERKASEllNIGYFAQH------Q 383
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG--RVEFFNQNiyerrvN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 384 MDALDGQAS---------------------------PMLQLARIADKQISEATLRSFLGSfgfsgeRMDTPCESFSGGER 436
Cdd:PRK14258 83 LNRLRRQVSmvhpkpnlfpmsvydnvaygvkivgwrPKLEIDDIVESALKDADLWDEIKH------KIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 437 ARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHG-----GKCTE 507
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVE 236
|
.
gi 446536636 508 F 508
Cdd:PRK14258 237 F 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
306-507 |
4.80e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 306 KMSSPLLTLENasIGY--GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIK---SLV----GDLpLLAGErKASELLNI 376
Cdd:PRK10247 2 QENSPLLQLQN--VGYlaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKivaSLIsptsGTL-LFEGE-DISTLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQ----HQMDALDGQA--SPMLQLARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPN 450
Cdd:PRK10247 78 IYRQQvsycAQTPTLFGDTvyDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 451 VLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASvCDEL--LLVHGGKCTE 507
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIhryvREQNIAVLWVTHDKDEINH-ADKVitLQPHAGEMQE 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
312-504 |
5.79e-10 |
|
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: 59.94 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG---------------DLPLLAGERkasellNI 376
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfetptsgeilldgkdITNLPPHKR------PV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQH-----QMDALDGQASPmLQLARIaDKQISEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNV 451
Cdd:cd03300 75 NTVFQNyalfpHLTVFENIAFG-LRLKKL-PKAEIKERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 452 LILDEPTNHLDLDMRHALS---MALQDFEG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
342-462 |
6.39e-10 |
|
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: 59.04 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 342 LLGMNGAGKSTLIKSLVGDLPLLAGE-------------RKASELLNIGyfaqHQmDALDGQASPMLQL----ARIADKQ 404
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRvllnggpldfqrdSIARGLLYLG----HA-PGIKTTLSVLENLrfwhADHSDEQ 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 405 ISEATLRSFLGSFGfsgermDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03231 106 VEEALARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
340-500 |
6.69e-10 |
|
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: 59.76 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVG------------------DLpLLAGERkasELLN-----IGYFAQH-----QMDALDGQA 391
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGnylpdsgsilvrhdggwvDL-AQASPR---EILAlrrrtIGYVSQFlrvipRVSALDVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 SPMLQLAriADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERAR--LALALIVwqRPNVLILDEPTNHLDLDMRHAL 469
Cdd:COG4778 116 EPLLERG--VDREEARARARELLARLNLPERLWDLPPATFSGGEQQRvnIARGFIA--DPPLLLLDEPTASLDAANRAVV 191
|
170 180 190
....*....|....*....|....*....|....
gi 446536636 470 SMALQDF--EG-AVVLVSHERQLIASVCDELLLV 500
Cdd:COG4778 192 VELIEEAkaRGtAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
315-463 |
6.86e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 315 ENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG---------ERKASELL--NIGYFAQHQ 383
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiQHYASKEVarRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 384 MDALDGQAS-----------PMLQLARIADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVL 452
Cdd:PRK10253 91 TTPGDITVQelvargryphqPLFTRWRKEDEEAVTKAMQA-TGITHLADQSVDT----LSGGQRQRAWIAMVLAQETAIM 165
|
170
....*....|.
gi 446536636 453 ILDEPTNHLDL 463
Cdd:PRK10253 166 LLDEPTTWLDI 176
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
328-500 |
8.16e-10 |
|
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: 59.33 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 328 EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGD-LP----------------LLAGERKASEL--LNIGYFAQH-----Q 383
Cdd:TIGR02324 25 KNVSLTVNAGECVALSGPSGAGKSTLLKSLYANyLPdsgrilvrhegawvdlAQASPREVLEVrrKTIGYVSQFlrvipR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 384 MDALDGQASPMLQLAriADKQISEATLRSFLGSFGFSgERM-DTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:TIGR02324 105 VSALEVVAEPLLERG--VPREAARARARELLARLNIP-ERLwHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446536636 463 LDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLV 500
Cdd:TIGR02324 182 AANRQVVVELIAEAKArgaALIGIFHDEEVRELVADRVMDV 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
313-485 |
8.62e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 59.71 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 313 TLENASIGYGDKKIAEKIKLQItPNSRI-GLLGMNGAGKSTLIkSLVGDL-PLLAGE-----------------RKAS-- 371
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTI-PKGGItALIGPNGAGKSTLL-SMISRLlPPDSGEvlvdgldvattpsrelaKRLAil 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 372 -------------ELLNIGYFAQHQmdaldGQASPmlqlariADKQISEATLRsFLGSFGFSGERMDTpcesFSGGERAR 438
Cdd:COG4604 81 rqenhinsrltvrELVAFGRFPYSK-----GRLTA-------EDREIIDEAIA-YLDLEDLADRYLDE----LSGGQRQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 439 LALALIVWQRPNVLILDEPTNhlDLDMRHALSM------ALQDFEGAVVLVSH 485
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLN--NLDMKHSVQMmkllrrLADELGKTVVIVLH 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
329-514 |
1.20e-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: 60.51 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 329 KIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERK-ASELLN--------------IGYFAQhqmdaldgQAS- 392
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlNGRTLFdsrkgiflppekrrIGYVFQ--------EARl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 393 -PMLQL----------ARIADKQISEATLRSFLGSfgfsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:TIGR02142 87 fPHLSVrgnlrygmkrARPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 462 DLDMRHALSMALQ----DFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD 514
Cdd:TIGR02142 163 DDPRKYEILPYLErlhaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAE 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
1.30e-09 |
|
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: 58.68 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVwTVAHMAQEVKALDMPAI 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-DVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFVLsgdeeyWD----IQNkLAQPeqltdsdLAKLHGRFDEIHgysapSKAAQLMAGLGfLEHQLRLNVASFSGGWRMRL 157
Cdd:cd03259 80 DYAL------FPhltvAEN-IAFG-------LKLRGVPKAEIR-----ARVRELLELVG-LEGLLNRYPHELSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELqrelGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
288-504 |
1.37e-09 |
|
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: 58.64 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 288 LAPAHVDTPFTF---SFREPTKMSSPLLtlenasigygdkkiaEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLL 364
Cdd:cd03248 3 LAPDHLKGIVKFqnvTFAYPTRPDTLVL---------------QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 365 AGE----RKASELLNIGYFaqHQMDALDGQaSPML-----------QLARIADKQISEATLRSFLGSF------GFSGEr 423
Cdd:cd03248 68 GGQvlldGKPISQYEHKYL--HSKVSLVGQ-EPVLfarslqdniayGLQSCSFECVKEAAQKAHAHSFiselasGYDTE- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 424 MDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVcDELLLVH 501
Cdd:cd03248 144 VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVERA-DQILVLD 222
|
...
gi 446536636 502 GGK 504
Cdd:cd03248 223 GGR 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
330-491 |
1.41e-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: 58.57 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------RKASELL--NIGYFAQ-----HQMDALDGQ 390
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngqdvsdlrGRAIPYLrrKIGVVFQdfrllPDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 391 ASPMlqlaRIADKQISEATLR--SFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:cd03292 100 AFAL----EVTGVPPREIRKRvpAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180
....*....|....*....|....*.
gi 446536636 469 LSMALQDFE--GAVVLVS-HERQLIA 491
Cdd:cd03292 175 IMNLLKKINkaGTTVVVAtHAKELVD 200
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
312-504 |
1.44e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.31 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERKAS--ELL-NIGYFAQHQMDA-L 387
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL-------LRLLAGLETPSagELLaGTAPLAEAREDTrL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 388 DGQASPMLQLARIADK-------QISEATLRSfLGSFGFSGERMDTPCeSFSGGERARLALALIVWQRPNVLILDEPTNH 460
Cdd:PRK11247 86 MFQDARLLPWKKVIDNvglglkgQWRDAALQA-LAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 461 LD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11247 164 LDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
1.52e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 58.95 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLR----RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL-------TRPSvWTVAHM 69
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkpvTGPG-PDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 70 AQEvKALdMP---AID---FVLsgdeeywdiqnklaqpeqltdsdlaklhgrfdEIHGYSAPSKAAQLMA-----GL-GF 137
Cdd:COG1116 86 FQE-PAL-LPwltVLDnvaLGL--------------------------------ELRGVPKAERRERAREllelvGLaGF 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 138 LE---HQLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAIL------WLEDWLKAYEGTLILISHDRD 206
Cdd:COG1116 132 EDaypHQL-------SGGMRQRVAIARALANDPEVLLMDEPFGA--LDALTrerlqdELLRLWQETGKTVLFVTHDVD 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-204 |
1.53e-09 |
|
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: 58.25 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVwTVAHMA 70
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEvlvdgepVTGPGP-DRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 71 QEvKALdMP---AIDFVLSGDEeywdiQNKLAQPEQLtdsdlaklhgrfdeihgysapSKAAQLMA--GL-GFLE---HQ 141
Cdd:cd03293 80 QQ-DAL-LPwltVLDNVALGLE-----LQGVPKAEAR---------------------ERAEELLElvGLsGFENaypHQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 142 LrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLKAYEGTLILISHD 204
Cdd:cd03293 132 L-------SGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
312-511 |
1.72e-09 |
|
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: 60.59 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG------------------------DLPLLAGE 367
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyvERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 368 R-------KASELLNIGYFAQHQMDALDGQASPMLQ--LARIADKQISEATLRSfLGSFGFSGE---------------- 422
Cdd:TIGR03269 81 PcpvcggtLEPEEVDFWNLSDKLRRRIRKRIAIMLQrtFALYGDDTVLDNVLEA-LEEIGYEGKeavgravdliemvqls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 423 -RMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD---LDMRH-ALSMALQDFEGAVVLVSHERQLIASVCDEL 497
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHnALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....
gi 446536636 498 LLVHGGKCTEfEGD 511
Cdd:TIGR03269 240 IWLENGEIKE-EGT 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-202 |
1.76e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.13 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSltrpsvwtVAHMAQEV-KALDMP 79
Cdd:PRK15056 7 IVVNDVTVTwRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK--------ISILGQPTrQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 AIDFVLSGDEEYWDIqnklaqPEQLTDsdlAKLHGRFDEIHGYSAPSK-----AAQLMAGLGFLEHQLRlNVASFSGGWR 154
Cdd:PRK15056 79 LVAYVPQSEEVDWSF------PVLVED---VVMMGRYGHMGWLRRAKKrdrqiVTAALARVDMVEFRHR-QIGELSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446536636 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAyEGTLILIS 202
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRD-EGKTMLVS 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-232 |
2.35e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 13 GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgADEGSLTRPSVwtvahmaqEVKALDMPAIDFVLSgdeeyW 92
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGI--------ELRELDPESWRKHLS-----W 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 93 DIQNKLAQPEQLTDS-DLAKLHGRFDEIHGYSAPSKAAQLMAGLGF-LEHQLRLNVASFSGGWRMRLNLARTLMSRSDLL 170
Cdd:PRK11174 428 VGQNPQLPHGTLRDNvLLGNPDASDEQLQQALENAWVSEFLPLLPQgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 171 LLDEPTNHLDLDA-ILWLEDWLKAYEG-TLILISHDRDFLDAItDHILHIENQELtLYTGNYST 232
Cdd:PRK11174 508 LLDEPTASLDAHSeQLVMQALNAASRRqTTLMVTHQLEDLAQW-DQIWVMQDGQI-VQQGDYAE 569
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
312-514 |
3.18e-09 |
|
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: 57.73 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIaEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERKasellNIG 377
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGfikpdsgkillngkDITNLPPEKR-----DIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 378 YFAQH-----QMDALDGQASPMLQlaRIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALA--LIVwqRPN 450
Cdd:cd03299 75 YVPQNyalfpHMTVYKNIAYGLKK--RKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIAraLVV--NPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 451 VLILDEPTNHLDL----DMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD 514
Cdd:cd03299 150 ILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEE 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
305-504 |
3.20e-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: 57.83 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 305 TKMSSPLLTLENASIGYGDKK----IAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAGE------- 367
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPtsgtvRLAGQdlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 368 ------RKAsellNIGYFAQH-----QMDALDGQASPmLQLARIADkqiSEATLRSFLGSFGFsGERMD-TPCEsFSGGE 435
Cdd:COG4181 82 dararlRAR----HVGFVFQSfqllpTLTALENVMLP-LELAGRRD---ARARARALLERVGL-GHRLDhYPAQ-LSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQDFEGA-VVLVSHERQLiASVCDELLLVHGGK 504
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRERGTtLVLVTHDPAL-AARCDRVLRLRAGR 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
330-503 |
3.31e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDALDGQASPMLQLAriaDKQISEAT 409
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFP---ESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 410 LRSFLG----SFGFSGERMD-------------------TPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:PRK13643 102 VLKDVAfgpqNFGIPKEKAEkiaaeklemvgladefwekSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446536636 467 ---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK13643 181 iemMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
128-219 |
3.93e-09 |
|
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: 57.30 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 128 AAQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLKAYEGTLILISH 203
Cdd:cd03297 112 VDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTH 190
|
90
....*....|....*.
gi 446536636 204 DRDFLDAITDHILHIE 219
Cdd:cd03297 191 DLSEAEYLADRIVVME 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
140-511 |
4.26e-09 |
|
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: 59.31 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 140 HQLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD--LDA-ILWLEDWLKAYEGT-LILISHD----RDFldai 211
Cdd:COG4172 155 HQL-------SGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqILDLLKDLQRELGMaLLLITHDlgvvRRF---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 212 TDHILHIENQELTlytgnystfETTRSERLaqqqqafekqqearahlqkfidrFKAkatkARQAQSRiKQLERMQQLAPA 291
Cdd:COG4172 224 ADRVAVMRQGEIV---------EQGPTAEL-----------------------FAA----PQHPYTR-KLLAAEPRGDPR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 292 HVDTPftfsfreptkmSSPLLTLENASIGY-----------GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGd 360
Cdd:COG4172 267 PVPPD-----------APPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 361 lpLLAGERKAsellnigYFAQHQMDALDGQA-------------------SPMLQLARI-----------ADKQISEATL 410
Cdd:COG4172 335 --LIPSEGEI-------RFDGQDLDGLSRRAlrplrrrmqvvfqdpfgslSPRMTVGQIiaeglrvhgpgLSAAERRARV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 411 RSFLGSFGFSGERMDT-PCEsFSGGERARLALA--LIVwqRPNVLILDEPTNHLDLDMRH---ALSMALQDFEG-AVVLV 483
Cdd:COG4172 406 AEALEEVGLDPAARHRyPHE-FSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDVSVQAqilDLLRDLQREHGlAYLFI 482
|
410 420
....*....|....*....|....*...
gi 446536636 484 SHERQLIASVCDELLLVHGGKCTEfEGD 511
Cdd:COG4172 483 SHDLAVVRALAHRVMVMKDGKVVE-QGP 509
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
307-507 |
4.77e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGY----GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP-----------LLAGER--K 369
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvypsgdiRFHGESllH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 370 ASELL-------NIGYFAQHQMDAL------DGQASPMLQLARIADKQISEATLRSFLGSFGF--SGERMDTPCESFSGG 434
Cdd:PRK15134 81 ASEQTlrgvrgnKIAMIFQEPMVSLnplhtlEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 435 ERARLALALIVWQRPNVLILDEPTNHLDL-----------DMRHALSMALqdfegavVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilqllrELQQELNMGL-------LFITHNLSIVRKLADRVAVMQNG 233
|
....
gi 446536636 504 KCTE 507
Cdd:PRK15134 234 RCVE 237
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-220 |
4.77e-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: 56.71 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSvwTVAHMAQEvkALDMPA-----IDFVLSGDEEYWDIQ 95
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQE--PWIQNGtirenILFGKPFDEERYEKV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 96 NKLAQPEQltdsDLAKL-HGRFDEIHGysapskaaqlmaglgflehqlrlNVASFSGGWRMRLNLARTLMSRSDLLLLDE 174
Cdd:cd03250 101 IKACALEP----DLEILpDGDLTEIGE-----------------------KGINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446536636 175 P--------TNHLDLDAIlwLEDWLKayEGTLILISHDRDFLdAITDHILHIEN 220
Cdd:cd03250 154 PlsavdahvGRHIFENCI--LGLLLN--NKTRILVTHQLQLL-PHADQIVVLDN 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
312-488 |
4.83e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.72 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP---------LLAGER---KASELLNIGYF 379
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsasgevLLNGRRltaLPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 380 AQhqmDAL------DGQ----ASPMlQLARIADKQISEATLRSfLGSFGFsGERmdTPcESFSGGERARLALALIVWQRP 449
Cdd:COG4136 82 FQ---DDLlfphlsVGEnlafALPP-TIGRAQRRARVEQALEE-AGLAGF-ADR--DP-ATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 450 NVLILDEPTNHLDLDMRHALSM----ALQDFEGAVVLVSHERQ 488
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREfvfeQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
307-462 |
5.25e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.72 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGY-GDKKIAEK-IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELL---------- 374
Cdd:PRK13635 1 MKEEIIRVEHISFRYpDAATYALKdVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 -NIGYFAQH----------QMD---ALDGQASPMLQLARIADKQISEATLRSFLgsfgfsgermDTPCESFSGGERARLA 440
Cdd:PRK13635 81 rQVGMVFQNpdnqfvgatvQDDvafGLENIGVPREEMVERVDQALRQVGMEDFL----------NREPHRLSGGQKQRVA 150
|
170 180
....*....|....*....|..
gi 446536636 441 LALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLD 172
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
312-462 |
5.26e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASI----GYGDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGErkasellNIGYFA 380
Cdd:COG1101 2 LELKNLSKtfnpGTVNEKRAlDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPpdsgsiLIDGK-------DVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 381 QHQ---------MDALDGQASPM-----LQLA---------RIADKQISEATLRSFLGSFGFSGE-RMDTPCESFSGGER 436
Cdd:COG1101 75 EYKrakyigrvfQDPMMGTAPSMtieenLALAyrrgkrrglRRGLTKKRRELFRELLATLGLGLEnRLDTKVGLLSGGQR 154
|
170 180
....*....|....*....|....*.
gi 446536636 437 ARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-224 |
6.14e-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: 56.67 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLR---RGGRV-LFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVKAL 76
Cdd:COG4181 8 IIELRGLTKTvgtGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG--------LDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 DMPA--------IDFVLsgdeeywdiqnklaQPEQLTDSDLA--------KLHGRFDeihgysAPSKAAQLMA--GLGFL 138
Cdd:COG4181 80 DEDArarlrarhVGFVF--------------QSFQLLPTLTAlenvmlplELAGRRD------ARARARALLErvGLGHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 139 EH----QLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEG-TLILISHDRDfLDA 210
Cdd:COG4181 140 LDhypaQL-------SGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHDPA-LAA 211
|
250
....*....|....
gi 446536636 211 ITDHILHIENQELT 224
Cdd:COG4181 212 RCDRVLRLRAGRLV 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
285-502 |
6.46e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 285 MQQLAPAHVDTPFTFSFREPTKMSSPLLT-LENASIGYGDKK--IAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDL 361
Cdd:COG2401 1 MARYNPFFVLMRVTKVYSSVLDLSERVAIvLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 362 PLLAGERKASELLNIGYFAQHQMDALDGQASPMLQLARIADKQISEATLrsFLGSFgfsgermdtpcESFSGGERARLAL 441
Cdd:COG2401 81 KGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLNAVGLSDAVL--WLRRF-----------KELSTGQKFRFRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 442 ALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHG 502
Cdd:COG2401 148 ALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarraGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-216 |
6.55e-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: 59.03 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 23 QLHPGWKIGLTGVNGAGKSTlFAALL-GSLGADEGSLtrPSVWTVAHMAQEVKA-LDMPAIDFVLSGDEEYWD---IQNK 97
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTT-FAKILaGVLKPDEGEV--DEDLKISYKPQYISPdYDGTVEEFLRSANTDDFGssyYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 98 LAQPeqltdsdlaklhgrfdeihgysapskaaqlmagLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTN 177
Cdd:COG1245 439 IIKP---------------------------------LG-LEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446536636 178 HLDldailwLEDWLKA----------YEGTLILISHDRDFLDAITDHIL 216
Cdd:COG1245 485 HLD------VEQRLAVakairrfaenRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-213 |
8.49e-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: 56.35 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLR--RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVwTVAHMAQEV--KALD 77
Cdd:cd03244 3 IEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV-DISKIGLHDlrSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 M-PAIDFVLSGdeeywDIQNKLAQPEQLTDSDLaklhgrfdeihgYSApSKAAQL----MAGLGFLEHQLRLNVASFSGG 152
Cdd:cd03244 82 IiPQDPVLFSG-----TIRSNLDPFGEYSDEEL------------WQA-LERVGLkefvESLPGGLDTVVEEGGENLSVG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 153 WRMRLNLARTLMSRSDLLLLDEPTNHLDL--DAILW--LEDWLKAYegTLILISHdRdfLDAITD 213
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPetDALIQktIREAFKDC--TVLTIAH-R--LDTIID 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
312-485 |
1.01e-08 |
|
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: 55.44 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-RKASELLNIGYFAQHQ------- 383
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEvRWNGTPLAEQRDEPHEnilylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 384 MDALDGQASPMLQL---ARI---ADKQISEAtlrsfLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILDE 456
Cdd:TIGR01189 81 LPGLKPELSALENLhfwAAIhggAQRTIEDA-----LAAVGLTG-FEDLPAAQLSAGQQRRLALArLWLSRRP-LWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 446536636 457 PTNHLD---LDMRHALSMALQDFEGAVVLVSH 485
Cdd:TIGR01189 154 PTTALDkagVALLAGLLRAHLARGGIVLLTTH 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
431-507 |
1.11e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.28 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 431 FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQ-DFEGAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnLMMDLQqELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
.
gi 446536636 507 E 507
Cdd:PRK11308 235 E 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
307-514 |
1.13e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.78 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEK-IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----------RKASELL 374
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKgININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilfdgkpidysRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 --NIGYFAQ---HQMDAL----DGQASPM-LQLAriaDKQISEaTLRSFLGSFGFSGERmDTPCESFSGGERARLALALI 444
Cdd:PRK13636 81 reSVGMVFQdpdNQLFSAsvyqDVSFGAVnLKLP---EDEVRK-RVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 445 VWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTeFEGDLQD 514
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKE 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-216 |
1.50e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 23 QLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPSVwTVAHMAQEVKA-LDMPAIDFvlsgdeeywdiqnklaqp 101
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-PEL-KISYKPQYIKPdYDGTVEDL------------------ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 102 eqltdsdLAKLHGRFDEIHGYSapskaaQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDl 181
Cdd:PRK13409 421 -------LRSITDDLGSSYYKS------EIIKPLQ-LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD- 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 182 dailwLEDWLKA----------YEGTLILISHDRDFLDAITDHIL 216
Cdd:PRK13409 486 -----VEQRLAVakairriaeeREATALVVDHDIYMIDYISDRLM 525
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-188 |
1.60e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.16 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT-----------RPSVWTVAHM 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 70 AQEVkaldmpAIDFVLSGdeeywdiqnklaqpEQLTDSDLAKLHGRFDEiHGYSAPSKAAQLMAGLGFLEHQLRlNVASF 149
Cdd:PRK09536 83 PQDT------SLSFEFDV--------------RQVVEMGRTPHRSRFDT-WTETDRAAVERAMERTGVAQFADR-PVTSL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD-AILWLE 188
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLE 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
312-507 |
1.62e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.48 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPL----LAGERKA---- 370
Cdd:COG1132 340 IEFENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLlrfydptsgrilIDGVDIrdltLESLRRQigvv 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 371 ---SELL------NIGYFAQhqmDALDGQaspMLQLARIAdkQISEatlrsFLGSF--GFsgermDTPCE----SFSGGE 435
Cdd:COG1132 420 pqdTFLFsgtireNIRYGRP---DATDEE---VEEAAKAA--QAHE-----FIEALpdGY-----DTVVGergvNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF-EGA-VVLVSHeRqlIASV--CDELLLVHGGKCTE 507
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmKGRtTIVIAH-R--LSTIrnADRILVLDDGRIVE 554
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-214 |
1.62e-08 |
|
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: 55.63 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHM-----AQE 72
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqdITKLPMHKRARLgigylPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 73 vkaldmPAIDFVLSGDEeywdiqNKLAQPEQLTDSDlaklhgrfDEIHgysapSKAAQLMAGLGfLEHqLRLNVASF-SG 151
Cdd:cd03218 84 ------ASIFRKLTVEE------NILAVLEIRGLSK--------KERE-----EKLEELLEEFH-ITH-LRKSKASSlSG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEdwlkayegTLILISHDRDFLDAITDH 214
Cdd:cd03218 137 GERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQ--------KIIKILKDRGIGVLITDH 191
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-204 |
1.65e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.00 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLrrGGRVlfQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGsLGADEGSLT---RP-SVWTVAHMA------- 70
Cdd:COG4138 1 LQLNDVAV--AGRL--GPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILlngRPlSDWSAAELArhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 71 -QEVKALDMPAIdfvlsgdeEYWDiqnkLAQPEQLTDSDLAKLhgrfdeihgysapskAAQLMAGLGfLEHQLRLNVASF 149
Cdd:COG4138 76 qQQSPPFAMPVF--------QYLA----LHQPAGASSEAVEQL---------------LAQLAEALG-LEDKLSRPLTQL 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 150 SGGWRMRLNLARTLM-------SRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISHD 204
Cdd:COG4138 128 SGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.72e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 56.27 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGwKI-GLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHMAQE 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKG-EIfGLLGPNGAGKTTTIRIILGILAPDSGEvlwdgepLDPEDRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 73 vKAL--DMPAIdfvlsgdeeywdiqnklaqpEQLTdsDLAKLhgrfdeiHGYS---APSKAAQLMAGLGfLEHQLRLNVA 147
Cdd:COG4152 80 -RGLypKMKVG--------------------EQLV--YLARL-------KGLSkaeAKRRADEWLERLG-LGDRANKKVE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHIL 216
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFSsHQMELVEELCDRIV 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-205 |
1.75e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVS-LRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPS---VWTVAHMAQEVKAL 76
Cdd:PRK10908 1 MIRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--------IERPSagkIWFSGHDITRLKNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 DMPAI---------DFVLSGDEEYWDiqnKLAQPEQLTDSDLAKLHGRfdeihgysapskAAQLMAGLGFLEHQLRLNVa 147
Cdd:PRK10908 73 EVPFLrrqigmifqDHHLLMDRTVYD---NVAIPLIIAGASGDDIRRR------------VSAALDKVGLLDKAKNFPI- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDlDAIlwLEDWLKAYEG------TLILISHDR 205
Cdd:PRK10908 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-DAL--SEGILRLFEEfnrvgvTVLMATHDI 197
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-220 |
1.79e-08 |
|
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: 54.08 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRG-GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQevkaldmpa 80
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 idfvlsgdeeywdiqnklaqpeqltdsdlaklhgrfdeiHGYSAPskaaqlmaglGFLEHQLRL---NVasFSGGWRMRL 157
Cdd:cd03223 72 ---------------------------------------RPYLPL----------GTLREQLIYpwdDV--LSGGEQQRL 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHdRDFLDAITDHILHIEN 220
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-176 |
2.10e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT----RPSVWTVAHMAQEvkal 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkDITDWQTAKIMRE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 dmpAIDFVLSGDEEYwdiqNKLAQPEQLTdsdlakLHGRFDEIHGYSAP-SKAAQLMAGLGFLEHQlrlNVASFSGGWRM 155
Cdd:PRK11614 81 ---AVAIVPEGRRVF----SRMTVEENLA------MGGFFAERDQFQERiKWVYELFPRLHERRIQ---RAGTMSGGEQQ 144
|
170 180
....*....|....*....|.
gi 446536636 156 RLNLARTLMSRSDLLLLDEPT 176
Cdd:PRK11614 145 MLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
307-507 |
2.13e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGY-GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----RKASEL----LNI 376
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEirldgRPLSSLshsvLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GyFAQHQMDAL---DG-----------------QASPMLQLARIAdKQISEAtLRSFLGSFGfsgermdtpcESFSGGER 436
Cdd:PRK10790 416 G-VAMVQQDPVvlaDTflanvtlgrdiseeqvwQALETVQLAELA-RSLPDG-LYTPLGEQG----------NNLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 437 ARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVcDELLLVHGGKCTE 507
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEA-DTILVLHRGQAVE 554
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
340-508 |
2.25e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLN--IGYFAQHQ----------------MDALDGQA 391
Cdd:PRK10762 281 LGVSGLMGAGRTELMKVLYGALPRTSGYvtldghevvtRSPQDGLAngIVYISEDRkrdglvlgmsvkenmsLTALRYFS 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 392 SPMLQLARIADKQiseaTLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:PRK10762 361 RAGGSLKHADEQQ----AVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ 436
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446536636 472 ALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK-CTEF 508
Cdd:PRK10762 437 LINQFkaEGlSIILVSSEMPEVLGMSDRILVMHEGRiSGEF 477
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
307-485 |
2.29e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 55.48 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGY----GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLNI 376
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptsgevLVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GY-FAQHQ----MDALD----GqaspmLQLARIADKQIsEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALA--LIV 445
Cdd:COG1116 83 GVvFQEPAllpwLTVLDnvalG-----LELRGVPKAER-RERARELLELVGLAGFEDAYPHQ-LSGGMRQRVAIAraLAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446536636 446 wqRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSH 485
Cdd:COG1116 156 --DPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTH 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
322-485 |
2.32e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 322 GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RK-----ASELLNIGyfaqHQmDALD 388
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEvlwqgepiRRqrdeyHQDLLYLG----HQ-PGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 389 GQASPM--LQ-LARIADKQiSEATLRSFLGSFGFSGeRMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDldm 465
Cdd:PRK13538 87 TELTALenLRfYQRLHGPG-DDEALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID--- 161
|
170 180
....*....|....*....|....*.
gi 446536636 466 RHALSMALQDFE------GAVVLVSH 485
Cdd:PRK13538 162 KQGVARLEALLAqhaeqgGMVILTTH 187
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
312-512 |
2.47e-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: 55.34 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGD-----------------LPLLAGER------ 368
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsyevtsgtilfkgqdlLELEPDERaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 369 ------------KASELLNIGYFAQHQMDALDgqASPMLQLARIADK-----QISEATLRSFLGsfgfsgermdtpcESF 431
Cdd:TIGR01978 81 lafqypeeipgvSNLEFLRSALNARRSARGEE--PLDLLDFEKLLKEklallDMDEEFLNRSVN-------------EGF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 432 SGGERAR---LALALIvwqRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASVC-DELLLVHGGK 504
Cdd:TIGR01978 146 SGGEKKRneiLQMALL---EPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKpDYVHVLLDGR 222
|
....*...
gi 446536636 505 CTEfEGDL 512
Cdd:TIGR01978 223 IVK-SGDV 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
321-526 |
2.51e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 321 YGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIK--------------------SLVGDL--PLLAGERKASELLN--I 376
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegsivvngqtiNLVRDKdgQLKVADKNQLRLLRtrL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQH-----QMDALDGQASPMLQLARIADKQISEATLRsFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNV 451
Cdd:PRK10619 95 TMVFQHfnlwsHMTVLENVMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 452 LILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCTEfEGDLQDYAKWLREARQQQ 526
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLHQGKIEE-EGAPEQLFGNPQSPRLQQ 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-205 |
2.77e-08 |
|
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: 55.63 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGAdEGSLTRPSV-WTVAHMAQEVKALD-MPAIDFVLSGDe 89
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVsWNSVPLQKWRKAFGvIPQKVFIFSGT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 90 eywdIQNKLAQPEQLTDSDLAKLHgrfDEIhgySAPSKAAQLMAGLGFlehQLRLNVASFSGGWRMRLNLARTLMSRSDL 169
Cdd:cd03289 93 ----FRKNLDPYGKWSDEEIWKVA---EEV---GLKSVIEQFPGQLDF---VLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 446536636 170 LLLDEPTNHLDLDAILWLEDWLK-AYEGTLILISHDR 205
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHR 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
311-504 |
2.90e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEK-IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER---KASELLN----I 376
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKptsgevLIKGEPikyDKKSLLEvrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQHQMDAL-------DGQASPM-LQLariaDKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQR 448
Cdd:PRK13639 81 GIVFQNPDDQLfaptveeDVAFGPLnLGL----SKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 449 PNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVS-HERQLIASVCDELLLVHGGK 504
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGK 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-219 |
3.25e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLG-------SLGADEGSLTRPSVWTVAHMA--- 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfykptggTILLRGQHIEGLPGHQIARMGvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 71 --QEVKAL-DMPAIDFVLsgdeeywdiqnkLAQPEQLTDSDLAKLHG----RFDEihgYSAPSKAAQLMAGLGFLEHQLR 143
Cdd:PRK11300 85 tfQHVRLFrEMTVIENLL------------VAQHQQLKTGLFSGLLKtpafRRAE---SEALDRAATWLERVGLLEHANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 144 lNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL------DLDAILwleDWLKAYEG-TLILISHDRDFLDAITDHIL 216
Cdd:PRK11300 150 -QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDELI---AELRNEHNvTVLLIEHDMKLVMGISDRIY 225
|
...
gi 446536636 217 HIE 219
Cdd:PRK11300 226 VVN 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-223 |
3.26e-08 |
|
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: 55.20 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVKALD---MPAI--DFVLSGDEEY---- 91
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLG--------LEKPAQGTVSFRGQDLYQLDrkqRRAFrrDVQLVFQDSPsavn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 92 --WDIQNKLAQP-EQLTDSDLAKLHGRfdeihgysapskAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSD 168
Cdd:TIGR02769 103 prMTVRQIIGEPlRHLTSLDESEQKAR------------IAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 169 LLLLDEPTNHLDL---DAILWLEDWLKAYEGT-LILISHDRDFLDAITDHILHIENQEL 223
Cdd:TIGR02769 171 LIVLDEAVSNLDMvlqAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
312-486 |
3.34e-08 |
|
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: 54.18 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-----DLPLLAGERKASEL----LNIGYFAQH 382
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleeptSGRIYIGGRDVTDLppkdRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 -----QMDALDGQASPmLQLaRIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:cd03301 81 yalypHMTVYDNIAFG-LKL-RKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|...
gi 446536636 458 TNHLD----LDMRHALSMALQDFEGAVVLVSHE 486
Cdd:cd03301 158 LSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
311-503 |
4.10e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIgyfaqhqmdALDGQ 390
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDV---------TLNGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 391 ---ASPMLQLAR------------------------------------IADKQISEATLrSFLGSFGFSGERMDTpcesF 431
Cdd:PRK13547 72 plaAIDAPRLARlravlpqaaqpafafsareivllgrypharragaltHRDGEIAWQAL-ALAGATALVGRDVTT----L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 432 SGGERARLALALIVWQ---------RPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELL 498
Cdd:PRK13547 147 SGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAARHADRIA 226
|
....*
gi 446536636 499 LVHGG 503
Cdd:PRK13547 227 MLADG 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
315-507 |
4.31e-08 |
|
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: 54.15 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 315 ENASIGYGDKKIAEK-IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqmdaLDGQASp 393
Cdd:cd03254 6 ENVNFSYDEKKPVLKdINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL-----------------IDGIDI- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 394 mlqlariadKQISEATLRSFLG-----SFGFSGE-----RMDTPC----------------------------------E 429
Cdd:cd03254 68 ---------RDISRKSLRSMIGvvlqdTFLFSGTimeniRLGRPNatdeevieaakeagahdfimklpngydtvlgengG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:cd03254 139 NLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-229 |
5.72e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.10 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrpsVWtvahMAQEVkaldmpaidfvLSGDEEYW-----DIQ 95
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV----AW----LGKDL-----------LGMKDDEWravrsDIQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 96 NKLAQPeqltdsdLAKLHGR--------------FDEIHGYSAPSKAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNLAR 161
Cdd:PRK15079 102 MIFQDP-------LASLNPRmtigeiiaeplrtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIAR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 162 TLMSRSDLLLLDEPTNHLDLD----AILWLEDWLKAYEGTLILISHDRDFLDAITDHIlhienqeLTLYTGN 229
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSiqaqVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV-------LVMYLGH 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
312-491 |
6.07e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.58 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKK-IAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG---------DLPllagerKASELLnigYFAQ 381
Cdd:COG4178 363 LALEDLTLRTPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygsgriARP------AGARVL---FLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HqmdaldgqasPMLQLARIAD--------KQISEATLRSFLGSFGFSG--ERMDTPC---ESFSGGERARLALALIVWQR 448
Cdd:COG4178 434 R----------PYLPLGTLREallypataEAFSDAELREALEAVGLGHlaERLDEEAdwdQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 449 PNVLILDEPTNHLDLDMRHALSMALQD--FEGAVVLVSHERQLIA 491
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRSTLAA 548
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
323-504 |
6.23e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.45 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 323 DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLNIGYFAQHQMDALDGQAsPMLQ 396
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpssgtiTIAGYHITPETGNKNLKKLRKKVSLVFQF-PEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 397 LAR---------------IADKQISEATLRsFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:PRK13641 98 LFEntvlkdvefgpknfgFSEDEAKEKALK-WLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446536636 462 DLDMRHALSMALQDFEGA---VVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-204 |
6.50e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 26 PGWKIGLTGVNGAGKSTLFAALLGslgADEGSLTRPSVW--TVAHMAQEVKA-LDMPAIDFVLsgdeeywdiQNKLAQP- 101
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAG---LDDGSSGEVSLVgqPLHQMDEEARAkLRAKHVGFVF---------QSFMLIPt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 102 -EQLTDSDL-AKLHGRFDEihgySAPSKAAQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:PRK10584 103 lNALENVELpALLRGESSR----QSRNGAKALLEQLG-LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180
....*....|....*....|....*....
gi 446536636 180 DLDAILWLEDWL----KAYEGTLILISHD 204
Cdd:PRK10584 178 DRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-224 |
7.36e-08 |
|
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: 54.73 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 26 PGWKI-GLTGVNGAGKSTLFAALLGSLGADEGSLtrpsvwtvaHMAQEV-----KALDMP----AIDFV----------- 84
Cdd:TIGR02142 21 PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEI---------VLNGRTlfdsrKGIFLPpekrRIGYVfqearlfphls 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 85 LSGDEEYwdiqnklaqpeQLTDSDLAKLHGRFDEIhgysapskaAQLMAglgfLEHQLRLNVASFSGGWRMRLNLARTLM 164
Cdd:TIGR02142 92 VRGNLRY-----------GMKRARPSERRISFERV---------IELLG----IGHLLGRLPGRLSGGEKQRVAIGRALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 165 SRSDLLLLDEPTNHLDL---DAIL-WLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELT 224
Cdd:TIGR02142 148 SSPRLLLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
303-504 |
7.77e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.84 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 303 EPTKMSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGER 368
Cdd:PRK11607 11 KTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeqptagqimldgvDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 369 KASELLNIGYFAQHQMDALDGQASPMLQlARIADKQISE--ATLRSFLGSFGFSGERmdtPcESFSGGERARLALALIVW 446
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFGLKQ-DKLPKAEIASrvNEMLGLVHMQEFAKRK---P-HQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 447 QRPNVLILDEPTNHLDLDMRHALSMALQDFEGAV----VLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvtcVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
322-490 |
7.92e-08 |
|
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: 55.53 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 322 GDKKIaEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDAL----DGQASPMLQL 397
Cdd:TIGR00954 464 GDVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgtlrDQIIYPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 398 ARIaDKQISEATLRSFL------------GSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:TIGR00954 543 DMK-RRGLSDKDLEQILdnvqlthilereGGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|....*
gi 446536636 466 RHALSMALQDFEGAVVLVSHERQLI 490
Cdd:TIGR00954 618 EGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
132-240 |
8.98e-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: 53.49 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 132 MAGLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDWLKAYEGTLILISHDRDF 207
Cdd:cd03299 113 IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEE 192
|
90 100 110
....*....|....*....|....*....|...
gi 446536636 208 LDAITDHILHIENQELTLYTGNYSTFETTRSER 240
Cdd:cd03299 193 AWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-180 |
9.60e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPG-WKIgLTGVNGAGKSTLFAALlgslgadeGSLTRPSVWTVAHMAQEVKAL--- 76
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGeFKL-ITGPSGCGKSTLLKIV--------ASLISPTSGTLLFEGEDISTLkpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 ----------DMPAidfvLSGDEEY------WDIQNKLAQPEQLTDsDLAklhgRFdeihgysapskaaqlmaglGFLEH 140
Cdd:PRK10247 78 iyrqqvsycaQTPT----LFGDTVYdnlifpWQIRNQQPDPAIFLD-DLE----RF-------------------ALPDT 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446536636 141 QLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK10247 130 ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
323-514 |
9.86e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 323 DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDL-------PLLAGERKASE--LLNIGYFAQHqmDALDGQAS- 392
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgTILANNRKPTKqiLKRTGFVTQD--DILYPHLTv 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 393 -------PMLQLARIADKQISEATLRSFLGSFGFsgermdTPCE------SF----SGGERARLALALIVWQRPNVLILD 455
Cdd:PLN03211 158 retlvfcSLLRLPKSLTKQEKILVAESVISELGL------TKCEntiignSFirgiSGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 456 EPTNHLDLDMRHALSMALQDF--EGAVVLVS-HE-RQLIASVCDELLLVHGGKCTeFEGDLQD 514
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLaqKGKTIVTSmHQpSSRVYQMFDSVLVLSEGRCL-FFGKGSD 293
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
330-560 |
9.98e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---RKASELLNIGYFAQHQMDALDGQASPMLQLArIADKQIS 406
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTvdiKGSAALIAISSGLNGQLTGIENIELKGLMMG-LTKEKIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 407 EATLRSFlgSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEptnhldldmrhALSMALQDFEG-------- 478
Cdd:PRK13545 122 EIIPEII--EFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE-----------ALSVGDQTFTKkcldkmne 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 479 ------AVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD----YAKWLREA-----------RQQQINA-QTAIEQN 536
Cdd:PRK13545 189 fkeqgkTIFFISHSLSQVKSFCTKALWLHYGQVKEY-GDIKEvvdhYDEFLKKYnqmsveerkdfREEQISQfQHGLLQE 267
|
250 260
....*....|....*....|....
gi 446536636 537 NSSSAAPAPAKVDKEAQRKEAARR 560
Cdd:PRK13545 268 DQTGRERKRKKGKKTSRKFKKKRV 291
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-226 |
1.08e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 52.67 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrpsVWTVAHMAQEVKAldmpAI 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV----LFDGKPLDIAARN----RI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFV-----LSGDEEYWDIQNKLAQPEQLTDSDLAKlhgRFDEihgysapskaaqLMAGLGFLEHQLRlNVASFSGGWRMR 156
Cdd:cd03269 73 GYLpeergLYPKMKVIDQLVYLAQLKGLKKEEARR---RIDE------------WLERLELSEYANK-RVEELSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-180 |
1.29e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.39 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPSVWT-VAHMAQ-EVKALDMP 79
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRdLYALSEaERRRLLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 AIDFV-----------------------LSGDEEYWDIQNKLAQPEQLTDSDLAklhgRFDEihgysAPSkaaqlmaglg 136
Cdd:PRK11701 90 EWGFVhqhprdglrmqvsaggnigerlmAVGARHYGDIRATAGDWLERVEIDAA----RIDD-----LPT---------- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446536636 137 flehqlrlnvaSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11701 151 -----------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-203 |
1.44e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---TRPSvwTVAHMAQEVKALD-MPAID 82
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTA--TRGDRSRFMAYLGhLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 83 FVLSGDEEYwdiqnklaqpeqltdSDLAKLHGRfdeiHGYSAPSKAaqlMAGLGFLEHQLRLnVASFSGGWRMRLNLART 162
Cdd:PRK13543 95 ADLSTLENL---------------HFLCGLHGR----RAKQMPGSA---LAIVGLAGYEDTL-VRQLSAGQKKRLALARL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446536636 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISH 203
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
311-495 |
1.48e-07 |
|
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: 53.52 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGY----GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP---------LLAGER----KASEL 373
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgitsgeiLFDGEDllklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 374 LN-----IGYFAQHQMDALD-----G-QASPMLQLARIADKQISEATLRSFLGSFGFSG--ERMDT-PCEsFSGGERAR- 438
Cdd:COG0444 81 RKirgreIQMIFQDPMTSLNpvmtvGdQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRyPHE-LSGGMRQRv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 439 -LALALIVwqRPNVLILDEPTNHLDLDMRH---ALSMALQD-FEGAVVLVSHERQLIASVCD 495
Cdd:COG0444 160 mIARALAL--EPKLLIADEPTTALDVTIQAqilNLLKDLQReLGLAILFITHDLGVVAEIAD 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-175 |
1.54e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.72 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHM-----AQEvkaldmP 79
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRifldgedITHLPMHKRARLgigylPQE------A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 AIdFvlsgdeeywdiqnklaqpEQLTDSD--LAKLhgrfdEIHGYSAP---SKAAQLMAGLGfLEHqLRLNVA-SFSGGW 153
Cdd:COG1137 88 SI-F------------------RKLTVEDniLAVL-----ELRKLSKKereERLEELLEEFG-ITH-LRKSKAySLSGGE 141
|
170 180
....*....|....*....|..
gi 446536636 154 RMRLNLARTLMSRSDLLLLDEP 175
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEP 163
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
312-507 |
1.56e-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: 52.62 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGD-KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPL----LAGERKA---- 370
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvssgsilIDGQDIrevtLDSLRRAigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 371 ---SELLN--IGY-FAQHQMDALDGQaspMLQLARIAdkQISEATLRSflgSFGFS---GER--MdtpcesFSGGERARL 439
Cdd:cd03253 81 pqdTVLFNdtIGYnIRYGRPDATDEE---VIEAAKAA--QIHDKIMRF---PDGYDtivGERglK------LSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEG-AVVLVSHERQLIASvCDELLLVHGGKCTE 507
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.59e-07 |
|
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: 52.58 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVS----LRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVKAL 76
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING--------LERPTSGSVLVDGTDLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 77 DmpaidfvlsgDEEYWDIQNKLA---QPEQLTDSDLAklhgrFD------EIHGYS---APSKAAQLMAGLGfLEHQLRL 144
Cdd:cd03258 73 S----------GKELRKARRRIGmifQHFNLLSSRTV-----FEnvalplEIAGVPkaeIEERVLELLELVG-LEDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 145 NVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03258 137 YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEK 216
|
...
gi 446536636 221 QEL 223
Cdd:cd03258 217 GEV 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
340-504 |
1.68e-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: 52.66 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVGDLP---------LLAG-ERKASELL-NIGYFAQHQmDALDGQA-------SPMLQLARI- 400
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVEgggttsgqiLFNGqPRKPDQFQkCVAYVRQDD-ILLPGLTvretltyTAILRLPRKs 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 401 ---ADKQISEATLRSFLGSFGFSGERMdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF- 476
Cdd:cd03234 115 sdaIRKKRVEDVLLRDLALTRIGGNLV----KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLa 190
|
170 180 190
....*....|....*....|....*....|.
gi 446536636 477 -EGAVVLVS-HE-RQLIASVCDELLLVHGGK 504
Cdd:cd03234 191 rRNRIVILTiHQpRSDLFRLFDRILLLSSGE 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-526 |
1.71e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.47 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 323 DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLlAGERKAS--EL--LNIGYFAQHQmdALDGQaSPML--- 395
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINgiELreLDPESWRKHL--SWVGQ-NPQLphg 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 396 ------QLAR--IADKQISEATLRSFLGSFGFSGER-MDTPCE----SFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK11174 438 tlrdnvLLGNpdASDEQLQQALENAWVSEFLPLLPQgLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 463 LDMRHALSMALQD--FEGAVVLVSHERQLIASvCDELLLVHGGKCTEfEGDLQD-------YAKWLREARQQQ 526
Cdd:PRK11174 518 AHSEQLVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ-QGDYAElsqagglFATLLAHRQEEI 588
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
341-561 |
1.84e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 341 GLLGMNGAGKSTLIKSLVGDLPLLAGERK-------ASEL---LNIGYFAQ----------HQmdALDGQAspmlQLARI 400
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpvdAGDIatrRRVGYMSQafslygeltvRQ--NLELHA----RLFHL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 401 ADKQISEAtLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD---LDM--RHALSMALQD 475
Cdd:NF033858 370 PAAEIAAR-VAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvaRDMfwRLLIELSRED 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 476 feGAVVLVS-H-----ERqliasvCDELLLVHGGKCTEfegdlQDYAKWLREARqqqiNAQT-----------AIEQNNS 538
Cdd:NF033858 448 --GVTIFIStHfmneaER------CDRISLMHAGRVLA-----SDTPAALVAAR----GAATleeafiayleeAAGAAAA 510
|
250 260
....*....|....*....|...
gi 446536636 539 SSAAPAPAKVDKEAQRKEAARRR 561
Cdd:NF033858 511 PAAAAAPAAAAAAPAAPAPAPRR 533
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
307-502 |
1.87e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASELLNIG 377
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTAlRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgqptRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 378 YFAQ-HQMD----------ALDGQASPM--LQLARIADKQISEATLrsflgsfgfsgERMDT------PCESFSGGERAR 438
Cdd:PRK15056 82 YVPQsEEVDwsfpvlvedvVMMGRYGHMgwLRRAKKRDRQIVTAAL-----------ARVDMvefrhrQIGELSGGQKKR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 439 LALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQDfEGAVVLVS-HERQLIASVCDELLLVHG 502
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEAriiSLLRELRD-EGKTMLVStHNLGSVTEFCDYTVMVKG 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-203 |
1.95e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvWTvahmAQEVKALD--- 77
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL----WQ----GEPIRRQRdey 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 ---------MPAIDFVLSGDEeywdiqNKLAqpeqltdsdLAKLHGRFDEihgysapSKAAQLMAGLGfLEHQLRLNVAS 148
Cdd:PRK13538 73 hqdllylghQPGIKTELTALE------NLRF---------YQRLHGPGDD-------EALWEALAQVG-LAGFEDVPVRQ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYE---GTLILISH 203
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
310-462 |
2.01e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.80 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 310 PLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG----ERKASELLNIG---YFAQH 382
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtiklDGGDIDDPDVAeacHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 383 QmDALDGQASPMLQL---ARI---ADKQISEAtlrsfLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILD 455
Cdd:PRK13539 81 R-NAMKPALTVAENLefwAAFlggEELDIAAA-----LEAVGLAP-LAHLPFGYLSAGQKRRVALArLLVSNRP-IWILD 152
|
....*..
gi 446536636 456 EPTNHLD 462
Cdd:PRK13539 153 EPTAALD 159
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
307-489 |
2.02e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.51 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIA----EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPL-------------LAGER 368
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQtdvlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTsgdvifngqpmskLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 369 KAsELLN--IGYFAQ-HQM----DALDGQASPMLqlarIADKQISEATLRSF--LGSFGFSGERMDTPCEsFSGGERARL 439
Cdd:PRK11629 81 KA-ELRNqkLGFIYQfHHLlpdfTALENVAMPLL----IGKKKPAEINSRALemLAAVGLEHRANHRPSE-LSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446536636 440 ALALIVWQRPNVLILDEPTNHLDL---DMRHALSMALQDFEG-AVVLVSHERQL 489
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGtAFLVVTHDLQL 208
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-182 |
2.04e-07 |
|
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: 52.03 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrpsvwtvahmaqEVKALDMPAIDFVlsgdeeywDIQNKLA- 99
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-------------EIDGIDISTIPLE--------DLRSSLTi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 100 --QPEQLTDSDLAKLHGRFDEihgYSapskAAQLMAGLGFLEHQLRLnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTN 177
Cdd:cd03369 87 ipQDPTLFSGTIRSNLDPFDE---YS----DEEIYGALRVSEGGLNL-----SQGQRQLLCLARALLKRPRVLVLDEATA 154
|
....*
gi 446536636 178 HLDLD 182
Cdd:cd03369 155 SIDYA 159
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
147-216 |
2.07e-07 |
|
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: 52.15 E-value: 2.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 147 ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLedwlkAYEG-TLILISHDRDFLDAITDHIL 216
Cdd:cd03262 134 AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelvgevLDVMKDL-----AEEGmTMVVVTHEMGFAREVADRVI 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-211 |
2.36e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgadegsLTRPSVWTVahmaqevkalDMPAIDF--V 84
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL------KGTPVAGCV----------DVPDNQFgrE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 85 LSGDEEYWDIQNKLAQPEQLTD---SDLAKLHGRFDEIhgysapskaaqlmaglgflehqlrlnvasfSGGWRMRLNLAR 161
Cdd:COG2401 100 ASLIDAIGRKGDFKDAVELLNAvglSDAVLWLRRFKEL------------------------------STGQKFRFRLAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 162 TLMSRSDLLLLDEPTNHLDLD-----AILWLEDWLKAyEGTLILISHDRDFLDAI 211
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQtakrvARNLQKLARRA-GITLVVATHHYDVIDDL 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-219 |
2.47e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 53.23 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RpsVWTVAHMAQEVK---- 74
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngR--DLFTNLPPRERRvgfv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 75 ----AL--DMPAID---F---VLSGDEEywDIQNKLAqpEQLTDSDLAKLHGRFdeihgysaPskaaqlmaglgfleHQL 142
Cdd:COG1118 81 fqhyALfpHMTVAEniaFglrVRPPSKA--EIRARVE--ELLELVQLEGLADRY--------P--------------SQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 143 rlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAIL------WLEDWLKAYEGTLILISHDRDflDA--ITDH 214
Cdd:COG1118 135 -------SGGQRQRVALARALAVEPEVLLLDEPFGA--LDAKVrkelrrWLRRLHDELGGTTVFVTHDQE--EAleLADR 203
|
250
....*....|
gi 446536636 215 IL-----HIE 219
Cdd:COG1118 204 VVvmnqgRIE 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
334-509 |
2.65e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 334 ITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------------RKASELL-------------NIGYFAQHQm 384
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRimiddcdvakfgltdlRRVLSIIpqspvlfsgtvrfNIDPFSEHN- 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 385 dalDGQASPMLQLARIADkqiseATLRSflgSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLD 464
Cdd:PLN03232 1338 ---DADLWEALERAHIKD-----VIDRN---PFGLDAEVSEGG-ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446536636 465 MRHALSMAL-QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFE 509
Cdd:PLN03232 1406 TDSLIQRTIrEEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
2.82e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.06 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLfqKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---------TRPSVWTVAHMAQ 71
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltaLPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 72 EvkaldmpaidfvlsgdeeywdiqNKL------AQ-------PE-QLTDSDLAKLHgrfdeihgysapsKAAQLMaGL-G 136
Cdd:COG3840 79 E-----------------------NNLfphltvAQniglglrPGlKLTAEQRAQVE-------------QALERV-GLaG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 137 FLEhqlRLNvASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLKAYEGTLILISHDRDflDA-- 210
Cdd:COG3840 122 LLD---RLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPE--DAar 195
|
250
....*....|
gi 446536636 211 ITDHILHIEN 220
Cdd:COG3840 196 IADRVLLVAD 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-180 |
3.07e-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: 51.85 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPsvwtvahmAQEVKALDMPA 80
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID--------GQDIREVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 I---------DFVLSGDEEYWDIQ--NKLAQPEQLTDS-DLAKLHgrfDEI----HGYSApskaaqlMAGlgflEHQLRL 144
Cdd:cd03253 73 LrraigvvpqDTVLFNDTIGYNIRygRPDATDEEVIEAaKAAQIH---DKImrfpDGYDT-------IVG----ERGLKL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 446536636 145 nvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03253 139 -----SGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-507 |
3.10e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 298 TFSFREPTKMSSPLLTLENASIGYGDK--KIAEKIKLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERKASE--- 372
Cdd:PRK11160 325 TFPTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTL-------LQLLTRAWDPQQgei 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 373 LLNigyfaQHQMDALDGQA--SPM-----------------LQLA--RIADKQISEATLRSFLGSFGFSGERMDT----- 426
Cdd:PRK11160 398 LLN-----GQPIADYSEAAlrQAIsvvsqrvhlfsatlrdnLLLAapNASDEALIEVLQQVGLEKLLEDDKGLNAwlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 427 --PcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM-RHALSMALQDFEG-AVVLVSHERQLIASVcDELLLVHG 502
Cdd:PRK11160 473 grQ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDN 548
|
....*
gi 446536636 503 GKCTE 507
Cdd:PRK11160 549 GQIIE 553
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-223 |
3.17e-07 |
|
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: 51.64 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVL-FQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVKALDMPA 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYK--------EELPTSGTIRVNGQDVSDLRGRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 I------------DFVLSGDEEYWDiqnKLAQPEQLTDsdlaklHGRFDeihgysAPSKAAQLMAGLGfLEHQLRLNVAS 148
Cdd:cd03292 73 IpylrrkigvvfqDFRLLPDRNVYE---NVAFALEVTG------VPPRE------IRKRVPAALELVG-LSHKHRALPAE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYE--GTLILIS-HDRDFLDAITDHILHIENQEL 223
Cdd:cd03292 137 LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
307-458 |
3.32e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.80 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSlvgdlplLAGERKASELLNIgyfaqhqmda 386
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGT-------LCGDPRATSGRIV---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 387 LDGQASPMLQLARI------------------------------ADKQISEATLRSFLGSFGFSGERMDTPCESFSGGER 436
Cdd:PRK11614 64 FDGKDITDWQTAKImreavaivpegrrvfsrmtveenlamggffAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQ 143
|
170 180
....*....|....*....|..
gi 446536636 437 ARLALALIVWQRPNVLILDEPT 458
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDEPS 165
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
312-565 |
3.68e-07 |
|
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: 53.76 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGY--GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLvgdLPLLAGE------------------RKAs 371
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSTEgeiqidgvswnsvtlqtwRKA- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 372 ellnIGYFAQhQMDALDGQASPMLQ-LARIADKQI----SEATLRSFLGSFGfsgERMDTPCES----FSGGERARLALA 442
Cdd:TIGR01271 1294 ----FGVIPQ-KVFIFSGTFRKNLDpYEQWSDEEIwkvaEEVGLKSVIEQFP---DKLDFVLVDggyvLSNGHKQLMCLA 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 443 LIVWQRPNVLILDEPTNHLDLDMRHALSMAL-QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEG--DLQDYAKWL 519
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSiqKLLNETSLF 1445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446536636 520 REARQQQINAQTAIEQNNSSSAAPAPAKVdkEAQRKEAARRREQTR 565
Cdd:TIGR01271 1446 KQAMSAADRLKLFPLHRRNSSKRKPQPKI--TALREEAEEEVQNTR 1489
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
312-597 |
4.71e-07 |
|
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: 51.78 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGY--GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLV------GDLPL---------LAGERKASELL 374
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIdgvswnsvpLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 --NIGYFAQHQMDALD--GQASPMlQLARIADKQISEATLRSFLGSFGFSGErmDTPCeSFSGGERARLALALIVWQRPN 450
Cdd:cd03289 83 pqKVFIFSGTFRKNLDpyGKWSDE-EIWKVAEEVGLKSVIEQFPGQLDFVLV--DGGC-VLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 451 VLILDEPTNHLDLDMRHALSMAL-QDFEGAVVLVSHERQLIASVCDELLLVHGGKCtefegdlqdyakWLREARQQQINA 529
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHRIEAMLECQRFLVIEENKV------------RQYDSIQKLLNE 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 530 QTAIEQnnsssaAPAPAKVDKEAQRKEAARRREQTRPirkniekvesQIEKLQprlAEIEEALADTSL 597
Cdd:cd03289 227 KSHFKQ------AISPSDRLKLFPRRNSSKSKRKPRP----------QIQALQ---EETEEEVQDTRL 275
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
332-504 |
4.76e-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: 50.95 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 332 LQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAG---------ERKASELL---NIgyFAQHQMDALDGQA-S 392
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPqsgrvLINGvdvtaappaDRPVSMLFqenNL--FAHLTVEQNVGLGlS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 393 PMLQLARIADKQISEAtlrsfLGSFGFSGERMDTPcESFSGGERARLALA-LIVWQRPnVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03298 97 PGLKLTAEDRQAIEVA-----LARVGLAGLEKRLP-GELSGGERQRVALArVLVRDKP-VLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 446536636 472 ALQDF----EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03298 170 LVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
305-490 |
4.78e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 305 TKMSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGD-----------------LPLLAGE 367
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaykilegdilfkgesiLDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 368 RKA------------------SELLNIGYFAQHQMDALDgQASPMLQLARIADKQISEATLRSFLGSfgfsgermdTPCE 429
Cdd:CHL00131 81 RAHlgiflafqypieipgvsnADFLRLAYNSKRKFQGLP-ELDPLEFLEIINEKLKLVGMDPSFLSR---------NVNE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 430 SFSGGERAR---LALALIvwqRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLI 490
Cdd:CHL00131 151 GFSGGEKKRneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLL 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
278-517 |
5.39e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.80 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 278 RIKQLERMQQLAPAHVDTPFTF---SFREPTKMSSPLLtlenasigygdkkiaEKIKLQITPNSRIGLLGMNGAGKSTLI 354
Cdd:TIGR00958 460 RKPNIPLTGTLAPLNLEGLIEFqdvSFSYPNRPDVPVL---------------KGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 355 KSLV-------GDLpLLAGERkaseLLNIGYFAQHQMDALDGQaSPML-----------QLARIADKQISEATLRSFLGS 416
Cdd:TIGR00958 525 ALLQnlyqptgGQV-LLDGVP----LVQYDHHYLHRQVALVGQ-EPVLfsgsvreniayGLTDTPDEEIMAAAKAANAHD 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 417 FGFSGER-MDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHAL--SMALQDFegAVVLVSHERQL 489
Cdd:TIGR00958 599 FIMEFPNgYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLqeSRSRASR--TVLLIAHRLST 676
|
250 260
....*....|....*....|....*...
gi 446536636 490 IASvCDELLLVHGGKCTEFEGDLQDYAK 517
Cdd:TIGR00958 677 VER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-203 |
7.56e-07 |
|
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: 52.43 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRG-GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT--------------RPSVwtv 66
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILlngfslkdidrhtlRQFI--- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 67 AHMAQEVKALDMPAIDFVLSGDEEywdiqnKLAQPEQLTDSDLAKLHgrfDEIHGYSapskaaqlmagLGFlehQLRLNV 146
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLLLGAKE------NVSQDEIWAACEIAEIK---DDIENMP-----------LGY---QTELSE 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 147 ASF--SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLdaIL---WLEDWLKAYEGTLILISH 203
Cdd:TIGR01193 608 EGSsiSGGQKQRIALARALLTDSKVLILDESTSNLDT--ITekkIVNNLLNLQDKTIIFVAH 667
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
147-225 |
7.83e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.83 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 147 ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---------LDAILWLEdwlkaYEGTLILISHDRDFLDAITDHILH 217
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdLIESLWQQ-----HGFTVLLVTHDVSEAVAMADRVLL 206
|
....*...
gi 446536636 218 IENQELTL 225
Cdd:PRK11247 207 IEEGKIGL 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
332-489 |
8.09e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 50.35 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 332 LQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGE---------RKASELL-------------NIGyFAQHQ 383
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTpasgslTLNGQdhtttppsrRPVSMLFqennlfshltvaqNIG-LGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 384 MDALDgqASPMLQLARIAdKQISeatLRSFLgsfgfsgERMdtPCEsFSGGERARLALA-LIVWQRPnVLILDEPTNHLD 462
Cdd:PRK10771 99 GLKLN--AAQREKLHAIA-RQMG---IEDLL-------ARL--PGQ-LSGGQRQRVALArCLVREQP-ILLLDEPFSALD 161
|
170 180
....*....|....*....|....*..
gi 446536636 463 LDMRHALSMALQDfegavvlVSHERQL 489
Cdd:PRK10771 162 PALRQEMLTLVSQ-------VCQERQL 181
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-223 |
8.28e-07 |
|
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: 49.74 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 9 LRRGGRvlFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaldmpaidfvlsgd 88
Cdd:cd03215 10 LSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT----------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 89 eeywdiqnklaqpeqltdsdlakLHGRfdEIHGYSaPSKAAQlmAGLG-----------FLEHQLRLNVA---SFSGGWR 154
Cdd:cd03215 59 -----------------------LDGK--PVTRRS-PRDAIR--AGIAyvpedrkreglVLDLSVAENIAlssLLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGT-LILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadAGKaVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
311-500 |
8.53e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLNIGYFAQHQ- 383
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 384 ----MDALDGQASPmLQLARIADKQiSEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:PRK11248 81 llpwRNVQDNVAFG-LQLAGVEKMQ-RLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 460 HLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELLLV 500
Cdd:PRK11248 158 ALDAFTREQMQTLLlklwQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-204 |
9.04e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.78 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaldmpa 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 idfvlSGDEEYWDIQNK-LAQ-----------PEQLTDSDLAK--------LHGRF---DEihgysapSKAAQLMAGLGF 137
Cdd:PRK11231 61 -----LGDKPISMLSSRqLARrlallpqhhltPEGITVRELVAygrspwlsLWGRLsaeDN-------ARVNQAMEQTRI 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 138 LEHQLRLnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLKAYEGTLILISHD 204
Cdd:PRK11231 129 NHLADRR-LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-203 |
1.03e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSL---RRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSV-----------WTVA 67
Cdd:TIGR00958 479 IEFQDVSFsypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 68 HMAQEVKALDMPAIDFVLSGDEEYWDIQNKLAQPEQLTDSDLAKLHGRFDEIHGysapSKAAQLmaglgflehqlrlnva 147
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG----EKGSQL---------------- 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 148 sfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISH 203
Cdd:TIGR00958 619 --SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
311-504 |
1.04e-06 |
|
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: 51.75 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP--------LLAGE----RKASELLNIGY 378
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiYWSGSplkaSNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 379 FAQHQmdaldgqaspmlQLARIADKQISEATlrsFLGS-FGFSGERMDTP-----CES------------------FSGG 434
Cdd:TIGR02633 81 VIIHQ------------ELTLVPELSVAENI---FLGNeITLPGGRMAYNamylrAKNllrelqldadnvtrpvgdYGGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 435 ERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-228 |
1.05e-06 |
|
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: 49.96 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 14 RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgaDEGSLTRPSVWTvahMAQEVKALDMP-AIDFVLSGD---- 88
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILF---NGQPRKPDQFQkCVAYVRQDDillp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 89 ----EEYWDIQNKLAQPEQLTDSDLAKLhgrfDEIHGYSApskaaqlmAGLGFLEHQLRLNVasfSGGWRMRLNLARTLM 164
Cdd:cd03234 95 gltvRETLTYTAILRLPRKSSDAIRKKR----VEDVLLRD--------LALTRIGGNLVKGI---SGGERRRVSIAVQLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 165 SRSDLLLLDEPTNHLD----LDAILWLEDWlkAYEGTLILIS-HD-RDFLDAITDHILHIENQELtLYTG 228
Cdd:cd03234 160 WDPKVLILDEPTSGLDsftaLNLVSTLSQL--ARRNRIVILTiHQpRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-211 |
1.07e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.83 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsltrpsvwtvaHMAQEVKALDmpaidfVLS 86
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG------------------HPKYEVTEGE------ILF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 87 GDEeywDIQNklaqpeqLTDSDLAKLhGRF------DEIHGYSapskaaqlmaglgfLEHQLR-LNVaSFSGGWRMRLNL 159
Cdd:cd03217 62 KGE---DITD-------LPPEERARL-GIFlafqypPEIPGVK--------------NADFLRyVNE-GFSGGEKKRNEI 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGT-LILISHDRDFLDAI 211
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYI 170
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
124-204 |
1.13e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.20 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 124 APSKAAQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEGTLIL 200
Cdd:PRK11629 122 INSRALEMLAAVG-LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTAFL 200
|
....*
gi 446536636 201 -ISHD 204
Cdd:PRK11629 201 vVTHD 205
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
344-492 |
1.19e-06 |
|
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: 49.53 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 344 GMNGAGKSTLIK----SLVGDLPL-LAGERKASELLNIGyfaqhqmdALDGQASPMLQLArIADKQISEATLRSFLGSFG 418
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELPPnSKGGAHDPKLIREG--------EVRAQVKLAFENA-NGKKYTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 419 FSGERMDTPCE----SFSGGERA------RLALALIVWQRPNVLILDEPTNHLDLD-MRHALSMALQDFEGA----VVLV 483
Cdd:cd03240 100 CHQGESNWPLLdmrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQknfqLIVI 179
|
....*....
gi 446536636 484 SHERQLIAS 492
Cdd:cd03240 180 THDEELVDA 188
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-186 |
1.21e-06 |
|
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: 51.94 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 24 LHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVKAL----DMPAIDFVLSGDEEYWdiqnkla 99
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgycpQFDAIDDLLTGREHLY------- 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 100 qpeqltdsdlakLHGRFDEIHGYSAPSKAAQLMAGLGFLEHQLRLnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:TIGR01257 2035 ------------LYARLRGVPAEEIEKVANWSIQSLGLSLYADRL-AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
....*....
gi 446536636 180 DLDA--ILW 186
Cdd:TIGR01257 2102 DPQArrMLW 2110
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-181 |
1.21e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.60 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSL---GADEGSLTRPSVWTVAHMAQEVKALD 77
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 MPAIDFVLSgdeeywdiqnKLAQPEQLTDSDLAKLHGRFDEIHGYSAPSK-------AAQLMAGLGFLehqLRLNVASFS 150
Cdd:PRK13547 81 LARLRAVLP----------QAAQPAFAFSAREIVLLGRYPHARRAGALTHrdgeiawQALALAGATAL---VGRDVTTLS 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446536636 151 GGWRMRLNLARTL---------MSRSDLLLLDEPTNHLDL 181
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
308-507 |
1.33e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.48 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 308 SSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDAL 387
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 388 DGQAS-----------PMLQLARI-----ADKQISEATLRSF-------LGSFGFSGERMDTPCESFSGGERARLALALI 444
Cdd:PRK14271 98 EFRRRvgmlfqrpnpfPMSIMDNVlagvrAHKLVPRKEFRGVaqarlteVGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 445 VWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-507 |
1.35e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqeVKALDMPA 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-------------INNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 IDFVLSGDEEYWDIQNKLAQPEQLtdSDLAKLH-GRFD-------EIHGYSAPSKAAQLMAGLGFLEHQLRLNVASFSGG 152
Cdd:PRK09700 72 LDHKLAAQLGIGIIYQELSVIDEL--TVLENLYiGRHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 153 WRMRLNLARTLMSRSDLLLLDEPTNHL---DLDAILWLEDWLKAyEGTLIL-ISHDRDFLDAITDHILHIENQElTLYTG 228
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISHKLAEIRRICDRYTVMKDGS-SVCSG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 229 NYSTFETTRSERLAQqqqafekqqearahlqkfidrfkakatkARQAQSRIKQLermqQLAPAHVDTPFTFSFREPTKMs 308
Cdd:PRK09700 228 MVSDVSNDDIVRLMV----------------------------GRELQNRFNAM----KENVSNLAHETVFEVRNVTSR- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 splltlenasigygDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASELL----NI 376
Cdd:PRK09700 275 --------------DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEirlngkdiSPRSPLDavkkGM 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQHQMdalDGQASPMLQLAR-IA-DKQISEATLRSFLGSFGFSGER---------MDTPCES-------FSGGERAR 438
Cdd:PRK09700 341 AYITESRR---DNGFFPNFSIAQnMAiSRSLKDGGYKGAMGLFHEVDEQrtaenqrelLALKCHSvnqniteLSGGNQQK 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 439 LALALIVWQRPNVLILDEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKaeiYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-216 |
1.36e-06 |
|
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: 51.29 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaLDMP 79
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR----------------LDGA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 AIDFvlsgdeeyWDiqnklaqPEQLTDS------DLAKLHG-------RFDEIHgysaPSK---AAQLmAGLgfleHQ-- 141
Cdd:COG4618 395 DLSQ--------WD-------REELGRHigylpqDVELFDGtiaeniaRFGDAD----PEKvvaAAKL-AGV----HEmi 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 142 LRL----------NVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAIlwleDWLKAYEGTLILISHD 204
Cdd:COG4618 451 LRLpdgydtrigeGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAI----RALKARGATVVVITHR 526
|
250
....*....|..
gi 446536636 205 RDFLdAITDHIL 216
Cdd:COG4618 527 PSLL-AAVDKLL 537
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-204 |
1.44e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.07 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 10 RRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVKALDMPA-------ID 82
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG--------LESPSQGNVSWRGEPLAKLNRAQrkafrrdIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 83 FV----LSGDEEYWDIQNKLAQP-EQLTDSDLAKLHGRFDEIhgysapskaaQLMAGLGfLEHQLRLNvASFSGGWRMRL 157
Cdd:PRK10419 93 MVfqdsISAVNPRKTVREIIREPlRHLLSLDKAERLARASEM----------LRAVDLD-DSVLDKRP-PQLSGGQLQRV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446536636 158 NLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDwLKAYEGT-LILISHD 204
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKK-LQQQFGTaCLFITHD 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
340-486 |
1.66e-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: 50.06 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVGDL-PLLAG------------ERKASELLNigYFAQhqmdALDGQASPML------QLARI 400
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLkPNLGKfddppdwdeildEFRGSELQN--YFTK----LLEGDVKVIVkpqyvdLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 401 ADKQISEATLRSF-LGSFGFSGERM------DTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRhaLSMA- 472
Cdd:cd03236 103 VKGKVGELLKKKDeRGKLDELVDQLelrhvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR--LNAAr 180
|
170
....*....|....*...
gi 446536636 473 ----LQDFEGAVVLVSHE 486
Cdd:cd03236 181 lireLAEDDNYVLVVEHD 198
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
405-507 |
1.71e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.16 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 405 ISEATLRSF--LGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFE----G 478
Cdd:PRK13646 118 LDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenK 197
|
90 100
....*....|....*....|....*....
gi 446536636 479 AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK13646 198 TIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
149-216 |
1.89e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 1.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAYEGT-LILISHDRDFLDAITDHIL 216
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTaIIMITHDLGVVAGICDKVL 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
311-492 |
1.97e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.10 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGY-GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP----LLAGERKASELLN--------- 375
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPsagkIWFSGHDITRLKNrevpflrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 376 IGY-FAQHQ--MD--ALDGQASPMLQLARIAD---KQISEAtlrsfLGSFGFSGERMDTPCEsFSGGERARLALALIVWQ 447
Cdd:PRK10908 81 IGMiFQDHHllMDrtVYDNVAIPLIIAGASGDdirRRVSAA-----LDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 448 RPNVLILDEPTNHLDLDMRHALSMALQDFE--GAVVLV-SHERQLIAS 492
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNrvGVTVLMaTHDIGLISR 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-204 |
2.59e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.70 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtVAHM--AQEVKAL----------------DMPAID 82
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR------VLGYvpFKRRKEFarrigvvfgqrsqlwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 83 -FVLSGdeEYWDIqnklaqPEQLTDSDLAKLHGRFDeihgysapskaaqlmaglgfLEHQLRLNVASFSGGWRMRLNLAR 161
Cdd:COG4586 116 sFRLLK--AIYRI------PDAEYKKRLDELVELLD--------------------LGELLDTPVRQLSLGQRMRCELAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446536636 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EG-TLILISHD 204
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGtTILLTSHD 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
390-507 |
3.11e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 390 QASPMLQLARIADkqiSEATLRSFlgsfgfsgermdtPcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR--- 466
Cdd:PRK10261 145 EAKRMLDQVRIPE---AQTILSRY-------------P-HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqi 207
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446536636 467 -HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK10261 208 lQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
330-526 |
3.43e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.98 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDL------PLLAGERKASEL-LNIGYFAQH-----QMD 385
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDItidtarSLSQQKGLIRQLrQHVGFVFQNfnlfpHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 386 ALDGQASPMLQLARIAdKQISEATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:PRK11264 102 VLENIIEGPVIVKGEP-KEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 466 -RHALSM--ALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEfegdlQDYAKWLREARQQQ 526
Cdd:PRK11264 180 vGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE-----QGPAKALFADPQQP 238
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-220 |
3.54e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 50.16 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS----------LTRPSVWtvAHMA 70
Cdd:COG1132 340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRilidgvdirdLTLESLR--RQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 71 ---QEVkaldmpaidFVLSGDeeywdIQNKLAqpeqltdsdLAKLHGRFDEIHgysapsKAAQLMAGLGF---LEHQLRL 144
Cdd:COG1132 418 vvpQDT---------FLFSGT-----IRENIR---------YGRPDATDEEVE------EAAKAAQAHEFieaLPDGYDT 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 145 NV----ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAilwLEDWLKayEGTLILISHdRdfLDAIT- 212
Cdd:COG1132 469 VVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMK--GRTTIVIAH-R--LSTIRn 540
|
....*....
gi 446536636 213 -DHILHIEN 220
Cdd:COG1132 541 aDRILVLDD 549
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-505 |
3.79e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVGDLP---------LLAGER-KASELLNI-GYFAQHQM--------DALDGQAspMLQLARI 400
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGMPiDAKEMRAIsAYVQQDDLfiptltvrEHLMFQA--HLRMPRR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 401 ADKQISEATLRSFLGSFGF---------SGERMdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:TIGR00955 132 VTKKEKRERVDEVLQALGLrkcantrigVPGRV----KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 446536636 472 ALQDF--EGAVVLVS-HE-RQLIASVCDELLLVHGGKC 505
Cdd:TIGR00955 208 VLKGLaqKGKTIICTiHQpSSELFELFDKIILMAEGRV 245
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
568-622 |
3.88e-06 |
|
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: 44.76 E-value: 3.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 568 RKNIEKVESQIEKLQPRLAEIEEALADTSLYeaNRKDDLLKLMNEQTELKAKLEQ 622
Cdd:pfam16326 7 QRELEELEAEIEKLEEEIAELEAQLADPELY--SDYEKLQELSAELEELEAELEE 59
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
312-504 |
3.90e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.33 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERKASE------------------- 372
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTV-------LRLVAGLEKPTEgqifidgedvthrsiqqrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 373 ---------LL-------NIGYFAQhqmdaldgqaspMLQLARIADKQ-ISEATLRSFLGSFGfsgermDTPCESFSGGE 435
Cdd:PRK11432 80 icmvfqsyaLFphmslgeNVGYGLK------------MLGVPKEERKQrVKEALELVDLAGFE------DRYVDQISGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIrelqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
307-469 |
4.53e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 48.59 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGY-GDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG------------DLPL----LAGER 368
Cdd:PRK13648 3 DKNSIIVFKNVSFQYqSDASFTlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGiekvksgeifynNQAItddnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 369 KasellNIGYFAQH----------QMD---ALDGQASPMLQLARIADKQISEATLRsflgsfgfsgERMDTPCESFSGGE 435
Cdd:PRK13648 83 K-----HIGIVFQNpdnqfvgsivKYDvafGLENHAVPYDEMHRRVSEALKQVDML----------ERADYEPNALSGGQ 147
|
170 180 190
....*....|....*....|....*....|....
gi 446536636 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHAL 469
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-180 |
4.55e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.54 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 14 RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHMAQEVkaldmpaidFvls 86
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSilidgkdVTKLPEYKRAKYIGRV---------F--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 87 gdeeywdiQNKLA--QP-----EQLTdsdLAKLHGRF---------DEIHGYSApsKAAQLmaGLGfLEHQLRLNVASFS 150
Cdd:COG1101 87 --------QDPMMgtAPsmtieENLA---LAYRRGKRrglrrgltkKRRELFRE--LLATL--GLG-LENRLDTKVGLLS 150
|
170 180 190
....*....|....*....|....*....|
gi 446536636 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-214 |
4.98e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.35 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 13 GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahMAQEVKALdMPAIDFVLSGDeEYW 92
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---------IDDEDISL-LPLHARARRGI-GYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 93 DIQNKLAQPEQLTDSDLAKLHGRfDEIHGYSAPSKAAQLMAGLgFLEHqLRLNVA-SFSGGWRMRLNLARTLMSRSDLLL 171
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIR-DDLSAEQREDRANELMEEF-HIEH-LRDSMGqSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 172 LDEPTNHLDLDAILWLEDwlkayegtliLISHDRDFLDA--ITDH 214
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKR----------IIEHLRDSGLGvlITDH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-208 |
5.74e-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: 49.94 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSvwTVAHMAQEVkaldmpaidfvlsgdeeyWdIQNKLAQ 100
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQQA------------------W-IQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 101 PEQLTDSDLAKLHgrfdeihgYSAPSKAAQLMAGLGFLEHQLRLNVA----SFSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:TIGR00957 717 ENILFGKALNEKY--------YQQVLEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190
....*....|....*....|....*....|....*....
gi 446536636 177 NHLD-------LDAILWLEDWLKAyeGTLILISHDRDFL 208
Cdd:TIGR00957 789 SAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYL 825
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
336-493 |
5.89e-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: 46.60 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 336 PNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERKASELLNigyfaqhqmdaldgqaspmlqlariADKQISEATLRSFLG 415
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR---ELGPPGGGVIYID-------------------------GEDILEEVLDQLLLI 52
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 416 SFGFSGErmdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASV 493
Cdd:smart00382 53 IVGGKKA-------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
311-507 |
6.18e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKI----AEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--DLPllaGERKASELLnigyFAQHQM 384
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGliDYP---GRVMAEKLE----FNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 385 DALDGQASPMLQLARIA----------------DKQISEA----------TLRS----FLGSFGFS--GERMDTPCESFS 432
Cdd:PRK11022 76 QRISEKERRNLVGAEVAmifqdpmtslnpcytvGFQIMEAikvhqggnkkTRRQraidLLNQVGIPdpASRLDVYPHQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 433 GGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQDFEG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQiieLLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
310-504 |
6.41e-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: 47.04 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 310 PLLTLENASIGYGDKKIAekikLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLN--IG 377
Cdd:cd03215 3 PVLEVRGLSVKGAVRDVS----FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEitldgkpvtrRSPRDAIRagIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 378 YFAQ--HQMDALDGQAspmlqlariadkqISE-ATLRSFLgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLIL 454
Cdd:cd03215 79 YVPEdrKREGLVLDLS-------------VAEnIALSSLL-----------------SGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 455 DEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03215 129 DEPTRGVDVGAKaeiYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-204 |
7.02e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgADEGSLT---RP-SVWTVAHMA--------QEVKALDMPAIdfvlsgd 88
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQfagQPlEAWSAAELArhraylsqQQTPPFAMPVF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 89 eEYWDiqnkLAQPEQLTDSDLAKLhgrFDEIhgysapskAAQLMaglgfLEHQLRLNVASFSGG-W-RMRL-----NLAR 161
Cdd:PRK03695 88 -QYLT----LHQPDKTRTEAVASA---LNEV--------AEALG-----LDDKLGRSVNQLSGGeWqRVRLaavvlQVWP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446536636 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYE---GTLILISHD 204
Cdd:PRK03695 147 DINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-204 |
7.73e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.42 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLfAALL--------GSLGADEGSLTRPSVWTVAHMAQEVKaldmpaIDFvlsgDEEY- 91
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTL-ARLLtmietptgGELYYQGQDLLKADPEAQKLLRQKIQ------IVF----QNPYg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 92 -----WDIQNKLAQPEQLtDSDLAKLHGRfdeihgysapSKAAQLMAGLGFL-EHQLRLNvASFSGGWRMRLNLARTLMS 165
Cdd:PRK11308 104 slnprKKVGQILEEPLLI-NTSLSAAERR----------EKALAMMAKVGLRpEHYDRYP-HMFSGGQRQRIAIARALML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446536636 166 RSDLLLLDEPTNHLD-------LDAILWLEDWLK-AYegtlILISHD 204
Cdd:PRK11308 172 DPDVVVADEPVSALDvsvqaqvLNLMMDLQQELGlSY----VFISHD 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-507 |
7.75e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.91 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 315 ENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPL-----------LAGERKASELLN-------I 376
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvegevrLFGRNIYSPDVDpievrreV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQHQMD--------------ALDGQASPMLQLARIADKQISEATLRSFLGsfgfsgERMDTPCESFSGGERARLALA 442
Cdd:PRK14267 88 GMVFQYPNPfphltiydnvaigvKLNGLVKSKKELDERVEWALKKAALWDEVK------DRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 443 LIVWQRPNVLILDEPTNHLD---LDMRHALSMALQDfEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
307-504 |
8.27e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.54 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSsplLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLL-AGERKas 371
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsghirfhgtDVSRLhARDRK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 372 ellnIGYFAQH-----QMDALDGQA----------SP--------------MLQLARIADKQISEatlrsflgsfgfsge 422
Cdd:PRK10851 76 ----VGFVFQHyalfrHMTVFDNIAfgltvlprreRPnaaaikakvtqlleMVQLAHLADRYPAQ--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 423 rmdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELL 498
Cdd:PRK10851 137 --------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVV 208
|
....*.
gi 446536636 499 LVHGGK 504
Cdd:PRK10851 209 VMSQGN 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
308-496 |
8.40e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.86 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 308 SSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER------KASELLN 375
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQpdsgeiLLDGEPvrfrspRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 376 IGYFAQH-----QMDALD----GQasPMLQLARIADKQISEATlRSFLGSFGFSgERMDTPCESFSGGER-----ARlAL 441
Cdd:COG1129 81 IAIIHQElnlvpNLSVAEniflGR--EPRRGGLIDWRAMRRRA-RELLARLGLD-IDPDTPVGDLSVAQQqlveiAR-AL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 442 AlivwQRPNVLILDEPTNHLDLD--------MRHalsmaLQDfEG-AVVLVSH---ErqlIASVCDE 496
Cdd:COG1129 156 S----RDARVLILDEPTASLTEReverlfriIRR-----LKA-QGvAIIYISHrldE---VFEIADR 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-239 |
8.46e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 143 RLN--VASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAyEGTLILISHDRDFLDAITDHILH 217
Cdd:PRK14246 146 RLNspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAF 224
|
90 100
....*....|....*....|..
gi 446536636 218 IENQELTLYTGNYSTFETTRSE 239
Cdd:PRK14246 225 LYNGELVEWGSSNEIFTSPKNE 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
314-511 |
9.47e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.81 E-value: 9.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 314 LENASIGYGDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPLLAGERKASELLN----------IGYFAQ 381
Cdd:PRK13647 7 VEDLHFRYKDGTKAlKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNaenekwvrskVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 382 HQMDAL-------DGQASPM-LQLARIADKQISEATLRSfLGSFGFSgermDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK13647 87 DPDDQVfsstvwdDVAFGPVnMGLDKDEVERRVEEALKA-VRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 454 LDEPTNHLDLDMRHALSMALQDF--EGAVVLVS-HERQLIASVCDELLLVHGGKcTEFEGD 511
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGR-VLAEGD 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-180 |
1.06e-05 |
|
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: 47.10 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRG--GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL--------TRPSVW---TVAH 68
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaLADPAWlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 69 MAQEVKALDMPAIDFVLSGDEEywdiqnklAQPEQLTDSdlAKLHGRFDEIhgysapskaAQLMAGLGFLehqLRLNVAS 148
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPG--------MSMERVIEA--AKLAGAHDFI---------SELPEGYDTI---VGEQGAG 138
|
170 180 190
....*....|....*....|....*....|..
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
311-507 |
1.08e-05 |
|
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: 48.56 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGYGDKKIA--EKIKLQITPNSRIGLLGMNGAGKSTLIKSL-------VGDLpLLAGERKASELL-----NI 376
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPalDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGQI-LLDGHDLADYTLaslrrQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQHQMDALDGQASPML--QLARIADKQISEATLRSFLGSF-GFSGERMDTPCES----FSGGERARLALALIVWQRP 449
Cdd:TIGR02203 409 ALVSQDVVLFNDTIANNIAygRTEQADRAEIERALAAAYAQDFvDKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 450 NVLILDEPTNHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLmQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-504 |
1.12e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 24 LHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPSVWTVAHMAQEVKALDMPaidfvlsgdeeywdiQNKLAQ 100
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEiggNPCARLTPAKAHQLGIYLVP---------------QEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 101 PEQ-LTDSDLAKLHGRFDeihgysAPSKAAQLMAGLGFlehQLRLNVASFSggwrmrLNLA--------RTLMSRSDLLL 171
Cdd:PRK15439 99 PNLsVKENILFGLPKRQA------SMQKMKQLLAALGC---QLDLDSSAGS------LEVAdrqiveilRGLMRDSRILI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 172 LDEPTNHL---DLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLyTGNYSTFETTrserlaqqqqaf 248
Cdd:PRK15439 164 LDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL-SGKTADLSTD------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 249 ekqqearahlqKFIDRFKAKATKARQAQSRIKQLErmqqlAPAHvdtpftfsfREPTKMSSPLLTLENASiGYGDKKIAe 328
Cdd:PRK15439 231 -----------DIIQAITPAAREKSLSASQKLWLE-----LPGN---------RRQQAAGAPVLTVEDLT-GEGFRNIS- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 329 kikLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLNIG--YFAQhqmdalDGQASPMLQ 396
Cdd:PRK15439 284 ---LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRimlngkeinaLSTAQRLARGlvYLPE------DRQSSGLYL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 397 LARIA---------------DKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:PRK15439 355 DAPLAwnvcalthnrrgfwiKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446536636 462 DLDMRHAL-----SMALQDFegAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK15439 435 DVSARNDIyqlirSIAAQNV--AVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
340-502 |
1.12e-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: 46.41 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVGDLpLLAGERKASELLNIGYFAQHQmdaldgqaspmlqlariadkqiseatlrsflgsfgf 419
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQL-IPNGDNDEWDGITPVYKPQYI------------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 420 sgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCD 495
Cdd:cd03222 71 ----------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSD 140
|
....*..
gi 446536636 496 ELLLVHG 502
Cdd:cd03222 141 RIHVFEG 147
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-226 |
1.15e-05 |
|
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: 46.76 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 9 LRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpsvwtvahmAQEVKALDMPAIDFvlsgd 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV---------RGRVSSLLGLGGGF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 89 eeywdiqnklaQPEqLTDSDLAKLHGRfdeIHGYSAPSKAAQL-----MAGLG-FLEHQLRlnvaSFSGGWRMRLNLART 162
Cdd:cd03220 96 -----------NPE-LTGRENIYLNGR---LLGLSRKEIDEKIdeiieFSELGdFIDLPVK----TYSSGMKARLAFAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 163 LMSRSDLLLLDEPT----NHLDLDAILWLEDWLKAyEGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:cd03220 157 TALEPDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
430-596 |
1.20e-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: 48.75 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsmalqdFEGAV--VLVSHERQLIASV------CDELLLVH 501
Cdd:TIGR01271 548 TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI------FESCLckLMSNKTRILVTSKlehlkkADKILLLH 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 502 GGKC------TEFEGDLQDYAKWL---------REARQQQINAQT----AIEQNNSSSAAPAPAKVDKEAQRKEAARRRE 562
Cdd:TIGR01271 622 EGVCyfygtfSELQAKRPDFSSLLlgleafdnfSAERRNSILTETlrrvSIDGDSTVFSGPETIKQSFKQPPPEFAEKRK 701
|
170 180 190
....*....|....*....|....*....|....*..
gi 446536636 563 QT---RPIRKNIEKVESQIEKLQPRLAEIEEALADTS 596
Cdd:TIGR01271 702 QSiilNPIASARKFSFVQMGPQKAQATTIEDAVREPS 738
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-204 |
1.30e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 9 LRR--GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLgSLGADEGS----------LTRPSVWTVAHMAQEV--- 73
Cdd:PRK15134 292 LKRtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEiwfdgqplhnLNRRQLLPVRHRIQVVfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 74 --KALDmPAIDfVLSGDEEYWDIQNKLAQPEQLTDsdlaklhgrfdeihgysapsKAAQLMAGLGfLEHQLRLNV-ASFS 150
Cdd:PRK15134 371 pnSSLN-PRLN-VLQIIEEGLRVHQPTLSAAQREQ--------------------QVIAVMEEVG-LDPETRHRYpAEFS 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLedwLKAYEGT----LILISHD 204
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILAL---LKSLQQKhqlaYLFISHD 485
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
307-458 |
1.53e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-------------RKASEl 373
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEilidgkpvrirspRDAIA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 374 LNIGYFAQHQMD------------ALDGQASPMLQLARIADKqiseatLRSFLGSFGFSGErMDTPCESFSGGERARL-- 439
Cdd:COG3845 80 LGIGMVHQHFMLvpnltvaenivlGLEPTKGGRLDRKAARAR------IRELSERYGLDVD-PDAKVEDLSVGEQQRVei 152
|
170 180
....*....|....*....|.
gi 446536636 440 --ALalivWQRPNVLILDEPT 458
Cdd:COG3845 153 lkAL----YRGARILILDEPT 169
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
135-220 |
1.57e-05 |
|
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: 47.40 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 135 LGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIL-WLEDWLKAYEGTLILISHDRDFLDA 210
Cdd:COG4148 121 LG-IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkAEILpYLERLRDELDIPILYVSHSLDEVAR 199
|
90
....*....|
gi 446536636 211 ITDHILHIEN 220
Cdd:COG4148 200 LADHVVLLEQ 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-181 |
1.65e-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: 47.16 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 16 LFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSvwTVAHMAQevKALDMPA-----IDFVLSGDEE 90
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQ--FSWIMPGtikenIIFGVSYDEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 91 YWDIQNKLAQPEQltdsDLAKLhgrfdeihgysaPSKAAQLMAGLGFlehqlrlnvaSFSGGWRMRLNLARTLMSRSDLL 170
Cdd:cd03291 128 RYKSVVKACQLEE----DITKF------------PEKDNTVLGEGGI----------TLSGGQRARISLARAVYKDADLY 181
|
170
....*....|.
gi 446536636 171 LLDEPTNHLDL 181
Cdd:cd03291 182 LLDSPFGYLDV 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
140-212 |
1.68e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.52 E-value: 1.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 140 HQLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD--LDAILWLE--DWLKAYEGTLILISHDRDflDAIT 212
Cdd:PRK11607 148 HQL-------SGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQE--EAMT 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-181 |
1.82e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVkaldMPA-----IDFVLSGDEEYWDIQ 95
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWI----MPGtikdnIIFGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 96 NKLAQPEQltdsDLAKLhgrfdeihgysaPSKAAQLMAGLGFlehqlrlnvaSFSGGWRMRLNLARTLMSRSDLLLLDEP 175
Cdd:TIGR01271 522 IKACQLEE----DIALF------------PEKDKTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSP 575
|
....*.
gi 446536636 176 TNHLDL 181
Cdd:TIGR01271 576 FTHLDV 581
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
298-462 |
1.84e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.65 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 298 TFSFREPTKMSSP-----LLTLENASIGYGDKKIA-EKIKLQITPNSRIGLLGMNGAGKSTLIKSL-------------- 357
Cdd:PRK13657 316 VPDVRDPPGAIDLgrvkgAVEFDDVSFSYDNSRQGvEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqsgrilid 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 358 ---VGDLPLlAGERKasellNIGYFAQHQM---------------DALDGQaspMLQLARIAdkQISEATLRSFLGSFGF 419
Cdd:PRK13657 396 gtdIRTVTR-ASLRR-----NIAVVFQDAGlfnrsiednirvgrpDATDEE---MRAAAERA--QAHDFIERKPDGYDTV 464
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 420 SGERmdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13657 465 VGER----GRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
307-504 |
2.02e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP--------LLAGER------KASE 372
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEElqasniRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 373 LLNIGYFaqHQmdaldgqaspmlQLARIADKQISEATlrsFLGSFGFSGERMD----------------------TPCES 430
Cdd:PRK13549 81 RAGIAII--HQ------------ELALVKELSVLENI---FLGNEITPGGIMDydamylraqkllaqlkldinpaTPVGN 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 431 FSGGERARLALALIVWQRPNVLILDEPTNHL-DLDMRHALSMaLQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLLDI-IRDLKAhgiACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-226 |
2.10e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 46.23 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSvwTVAHMaqevkaLDMPAIdFvlsgdeeywdiqnklaQ 100
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--RVSAL------LELGAG-F----------------H 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 101 PEqLTDSDLAKLHGRfdeIHGYSaPSKAAQLM------AGLG-FLEHQLRlnvaSFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:COG1134 101 PE-LTGRENIYLNGR---LLGLS-RKEIDEKFdeivefAELGdFIDQPVK----TYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 174 EptnhldldailwledWL---------KAYE---------GTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:COG1134 172 E---------------VLavgdaafqkKCLArirelresgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-181 |
2.23e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 46.23 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGwkiGLT---GVNGAGKSTLFAALLGSLGADEGSLT---RPsvwtVAHMAQEVK 74
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKG---GITaliGPNGAGKSTLLSMISRLLPPDSGEVLvdgLD----VATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 75 ALDMpAIdfvlsgdeeywdiqnkLAQPEQ----LTDSDLAKLhGRF----------DEIHgysaPSKAAQLMaGLGFLEH 140
Cdd:COG4604 74 AKRL-AI----------------LRQENHinsrLTVRELVAF-GRFpyskgrltaeDREI----IDEAIAYL-DLEDLAD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 141 ----QLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:COG4604 131 ryldEL-------SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-517 |
2.26e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 342 LLGMNGAGKSTLIKSLVGDLPLLAGERKASEllNIGYFAQHQ--MDA--------LDGQASPMLQLA-RI----ADKQIS 406
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQAwiMNAtvrgnilfFDEEDAARLADAvRVsqleADLAQL 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 407 EATLRSFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDldmRHALSMALQD-FEGAV----- 480
Cdd:PTZ00243 769 GGGLETEIGEKGVN----------LSGGQKARVSLARAVYANRDVYLLDDPLSALD---AHVGERVVEEcFLGALagktr 835
|
170 180 190
....*....|....*....|....*....|....*..
gi 446536636 481 VLVSHERQLIASVcDELLLVHGGKcTEFEGDLQDYAK 517
Cdd:PTZ00243 836 VLATHQVHVVPRA-DYVVALGDGR-VEFSGSSADFMR 870
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
328-500 |
2.46e-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: 45.92 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 328 EKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPLLAGER-KASELLNIG---------YFAQHQMDALDGQASPMLQ 396
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVIlEGKQITEPGpdrmvvfqnYSLLPWLTVRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 397 LARIADKQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL--- 473
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqi 160
|
170 180
....*....|....*....|....*...
gi 446536636 474 -QDFEGAVVLVSHErqliasvCDELLLV 500
Cdd:TIGR01184 161 wEEHRVTVLMVTHD-------VDEALLL 181
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
330-504 |
2.46e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDL-P----------LLAGERKASEL------LNIGY-FAQHQM------- 384
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPtsgtvtigerVITAGKKNKKLkplrkkVGIVFqFPEHQLfeetvek 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 385 DALDGqasPMLQLARIADkqiSEATLRSFLGSFGFSGERMD-TPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLD- 462
Cdd:PRK13634 106 DICFG---PMNFGVSEED---AKQKAREMIELVGLPEELLArSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDp 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 463 ------LDMRHALSmalQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13634 179 kgrkemMEMFYKLH---KEKGLTTVLVTHSMEDAARYADQIVVMHKGT 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-204 |
2.47e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.39 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTR-------PSVwTVAHM 69
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPAlqdvSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtgPGA-DRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 70 AQEvKALdMPaidfvlsgdeeyW-DIQNKLAQPEQLTDSDLAKLHGRfdeihgysapskAAQLMAGLGfLEHQLRLNVAS 148
Cdd:COG4525 82 FQK-DAL-LP------------WlNVLDNVAFGLRLRGVPKAERRAR------------AEELLALVG-LADFARRRIWQ 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAI-------LWLEDWLKAYEGTLiLISHD 204
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGA--LDALtreqmqeLLLDVWQRTGKGVF-LITHS 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
307-504 |
2.49e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.86 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERK--- 369
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfetpdsgrimldgqDITHVPAENRhvn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 370 ---ASELL--------NIGYFAQHQ-----------MDALDgqaspMLQLARIADKQISEatlrsflgsfgfsgermdtp 427
Cdd:PRK09452 90 tvfQSYALfphmtvfeNVAFGLRMQktpaaeitprvMEALR-----MVQLEEFAQRKPHQ-------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 428 cesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM---ALQDFEG-AVVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK09452 145 ---LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHDQEEALTMSDRIVVMRDG 221
|
.
gi 446536636 504 K 504
Cdd:PRK09452 222 R 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
430-490 |
2.65e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 45.78 E-value: 2.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMA-----LQDFEGAVVLVSHERQLI 490
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYL 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-180 |
3.00e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 34 GVNGAGKSTLFAALLGSLGADEGSltrpsVW---TVAHMAQEVKALDMPAIDFVLSGDEEywdiqnklaqpeqltdsDLA 110
Cdd:PTZ00243 693 GATGSGKSTLLQSLLSQFEISEGR-----VWaerSIAYVPQQAWIMNATVRGNILFFDEE-----------------DAA 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 111 KLHgrfDEIHGYSAPSKAAQLMAGLgflEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PTZ00243 751 RLA---DAVRVSQLEADLAQLGGGL---ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
148-180 |
3.60e-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: 44.85 E-value: 3.60e-05
10 20 30
....*....|....*....|....*....|...
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03213 111 GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
307-514 |
3.77e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG------------ERKASELL 374
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinninynklDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 NIGYFAQhqmdaldgQASPMLQLARIADKQISEATLRSFLG----SFGFSGER-------------MDTPCESFSGGERA 437
Cdd:PRK09700 81 GIGIIYQ--------ELSVIDELTVLENLYIGRHLTKKVCGvniiDWREMRVRaammllrvglkvdLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 438 RLALALIVWQRPNVLILDEPTNHL---DLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK--CTefeGDL 512
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvCS---GMV 229
|
..
gi 446536636 513 QD 514
Cdd:PRK09700 230 SD 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-205 |
3.95e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 14 RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPSVWTVAHMAQEVKAldmpaidfvlsgDEEYWD 93
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG--------LLNPEKGEILFERQSIKK------------DLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 94 IQNKLAQPEQLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAgLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:PRK13540 74 KQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCR-LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 446536636 174 EPTNHLDLDAILWLEDWLKAYE---GTLILISHDR 205
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-216 |
4.12e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.73 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 10 RRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALlgslgadeGSLTRPSVWTVAHMAQEVKaldmpaidfvLSGDE 89
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI--------NFLEKPSEGSIVVNGQTIN----------LVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 90 eywDIQNKLAQPEQLT--DSDLAKLHGRFD----------------EIHGYS---APSKAAQLMAGLGFLEHQLRLNVAS 148
Cdd:PRK10619 76 ---DGQLKVADKNQLRllRTRLTMVFQHFNlwshmtvlenvmeapiQVLGLSkqeARERAVKYLAKVGIDERAQGKYPVH 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
403-504 |
4.52e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.51 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 403 KQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsMALqdFEG---- 478
Cdd:PRK13649 118 QEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL-MTL--FKKlhqs 194
|
90 100
....*....|....*....|....*...
gi 446536636 479 --AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13649 195 gmTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-220 |
5.40e-05 |
|
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: 44.79 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVwTVAHMAQEVKALDMPAIDfvlsgdeeywdiQNKLAQ 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-DVTAAPPADRPVSMLFQE------------NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 101 PEQLTDSDLAKLHG-RFDEIHGYSAPSKAAQLmaGLGFLEHQLrlnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:cd03298 85 LTVEQNVGLGLSPGlKLTAEDRQAIEVALARV--GLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446536636 180 D---LDAILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03298 160 DpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
270-556 |
5.87e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.48 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 270 TKARQAQSRIKQLERMQQLAPAHVDtpftfsfREPTKMSSP-LLTLENASIGY--GDKKIAEKIKLQITPNSRIGLLGMN 346
Cdd:TIGR00957 601 VQASVSLKRLRIFLSHEELEPDSIE-------RRTIKPGEGnSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQV 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 347 GAGKSTLIKSLVGDLPLLAGE--RKASellnIGYFAQH--------QMDALDGQA-------SPMLQLARIADKQISEAT 409
Cdd:TIGR00957 674 GCGKSSLLSALLAEMDKVEGHvhMKGS----VAYVPQQawiqndslRENILFGKAlnekyyqQVLEACALLPDLEILPSG 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 410 LRSFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAV-----VLVS 484
Cdd:TIGR00957 750 DRTEIGEKGVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVT 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 485 HERQLIASVcDELLLVHGGKCTEFeGDLQD-------YAKWLRE-ARQQQinaQTAIEQNNSSSAAPApakvDKEAQRKE 556
Cdd:TIGR00957 820 HGISYLPQV-DVIIVMSGGKISEM-GSYQEllqrdgaFAEFLRTyAPDEQ---QGHLEDSWTALVSGE----GKEAKLIE 890
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
432-504 |
7.11e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 7.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-223 |
8.45e-05 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 44.38 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSL---RRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALL-------GSLGADEGSLTR------PSVwt 65
Cdd:cd03248 12 VKFQNVTFaypTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqgGQVLLDGKPISQyehkylHSK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 66 VAHMAQEvkaldmPaidfVLSGDEEYWDIQNKLAQPEQLTDSDLAKLHGRFDEI----HGYS--APSKAAQLmaglgfle 139
Cdd:cd03248 90 VSLVGQE------P----VLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFIselaSGYDteVGEKGSQL-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 140 hqlrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLE----DWLKAYegTLILISHDRDFLDAiTDHI 215
Cdd:cd03248 152 ----------SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQqalyDWPERR--TVLVIAHRLSTVER-ADQI 218
|
....*...
gi 446536636 216 LHIENQEL 223
Cdd:cd03248 219 LVLDGGRI 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-215 |
8.65e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 44.66 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 26 PGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWT--VAHMA-------------QEVKALDMPaidfvlsgdeE 90
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeiLDEFRgselqnyftklleGDVKVIVKP----------Q 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 91 YWDIQnklaqPEQLTDSDLAKLHgRFDEIHgysapsKAAQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLL 170
Cdd:cd03236 95 YVDLI-----PKAVKGKVGELLK-KKDERG------KLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446536636 171 LLDEPTNHLDLD-----AILWLEdwLKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03236 162 FFDEPSSYLDIKqrlnaARLIRE--LAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
429-492 |
8.66e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 8.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 429 ESFSGGERARLALAL--IVWQRPN----VLILDEPTNHLDLDMRHALS----MALQDFEG--AVVLVSHERQLIAS 492
Cdd:PRK01156 800 DSLSGGEKTAVAFALrvAVAQFLNndksLLIMDEPTAFLDEDRRTNLKdiieYSLKDSSDipQVIMISHHRELLSV 875
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
124-240 |
9.03e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 44.62 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 124 APSKAAQLMAGLGFLEHQLRLNVAsFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILwledWLKAYEG 196
Cdd:COG4161 118 AREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqvVEIIR----ELSQTGI 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446536636 197 TLILISHDRDFLDAITDHILHIENQELTLYtGNYSTFETTRSER 240
Cdd:COG4161 193 TQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTEA 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
138-213 |
1.04e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 44.64 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 138 LEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITD 213
Cdd:PRK14258 140 IKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLSD 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-176 |
1.13e-04 |
|
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: 43.96 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHM-------AQEVKA-------LDMP 79
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrdITGLPPHERARAgigyvpeGRRIFPeltveenLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 AidFVLSGDEEYWDIQNKLAqpeqltdsdlakLHGRFDEIHGysapSKAAQLmaglgflehqlrlnvasfSGGWRMRLNL 159
Cdd:cd03224 100 A--YARRRAKRKARLERVYE------------LFPRLKERRK----QLAGTL------------------SGGEQQMLAI 143
|
170
....*....|....*..
gi 446536636 160 ARTLMSRSDLLLLDEPT 176
Cdd:cd03224 144 ARALMSRPKLLLLDEPS 160
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
311-504 |
1.16e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.31 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 311 LLTLENASIGY---GDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVG------DLPLLAGERKASELL-----NI 376
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGlfeefeGKVKIDGELLTAENVwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFAQHQMD-------------ALDGQASPMLQLARIADKQISEATLRSFlgsfgfsgeRMDTPCEsFSGGERARLALAL 443
Cdd:PRK13642 84 GMVFQNPDNqfvgatveddvafGMENQGIPREEMIKRVDEALLAVNMLDF---------KTREPAR-LSGGQKQRVAVAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG----AVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHDLDEAAS-SDRILVMKAGE 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-176 |
1.19e-04 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 43.82 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGG-RVLFQkASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHMaqe 72
Cdd:COG0410 3 MLEVENLHAGYGGiHVLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSirfdgedITGLPPHRIARL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 73 vkaldmpaidfvlsGdeeywdiqnkLAQ-PE------QLT-----------DSDLAKLHGRFDEIHGYsapskaaqlmag 134
Cdd:COG0410 79 --------------G----------IGYvPEgrrifpSLTveenlllgayaRRDRAEVRADLERVYEL------------ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446536636 135 lgF--LEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:COG0410 123 --FprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-218 |
1.22e-04 |
|
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: 44.17 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgaDEGS-LTRPSVW----TVAHMAQEVKA-----------LDMPAI--- 81
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSKTIAG----HPSYeVTSGTILfkgqDLLELEPDERAraglflafqypEEIPGVsnl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFVLSGdeeywdiQNKLAQPEQLTDSDLAKLHGRFDEihgysapskaaqLMAGLGFLEHQLR--LNVAsFSGGWRMRLNL 159
Cdd:TIGR01978 96 EFLRSA-------LNARRSARGEEPLDLLDFEKLLKE------------KLALLDMDEEFLNrsVNEG-FSGGEKKRNEI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISHDRDFLDAITDHILHI 218
Cdd:TIGR01978 156 LQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
149-204 |
1.28e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 44.34 E-value: 1.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---------LdailwLEDwLKAYEG-TLILISHD 204
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaqvlnL-----LED-LQDELGlTYLFISHD 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-241 |
1.29e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 22 MQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpsVWTVAHMAQEVKALdmpAIDFVLSGDE-----EYWDIQN 96
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSH--IELLGRTVQREGRL---ARDIRKSRANtgyifQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 97 KLAQPEQLTDSDLAKLHGRFDEIHGYSAPSKAAQLMA----GLGFLEHQlrlNVASFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAltrvGMVHFAHQ---RVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446536636 173 DEPTNHLDLDAILWLEDWLKAYEG----TLILISHDRDFLDAITDHILHIEnQELTLYTGNYSTFETTRSERL 241
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALR-QGHVFYDGSSQQFDNERFDHL 248
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
430-507 |
1.51e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.01 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASVcDELLLVHGGKCTE 507
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKA-DEILVVEDGEIVE 558
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-180 |
1.55e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.80 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---------TRPSVWTVAHMAQEVKALDMPAIDfvlsgdeey 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhttTPPSRRPVSMLFQENNLFSHLTVA--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 92 wdiQN---KLAQPEQLTDSDLAKLHgrfdeihgysapsKAAQLMAGLGFLEhqlRLNvASFSGGWRMRLNLARTLMSRSD 168
Cdd:PRK10771 90 ---QNiglGLNPGLKLNAAQREKLH-------------AIARQMGIEDLLA---RLP-GQLSGGQRQRVALARCLVREQP 149
|
170
....*....|..
gi 446536636 169 LLLLDEPTNHLD 180
Cdd:PRK10771 150 ILLLDEPFSALD 161
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
127-215 |
1.63e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 44.32 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 127 KAAQLMA--GLGFLE----HQLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA----ILWLEDWLKAYEG 196
Cdd:COG3842 115 RVAELLElvGLEGLAdrypHQL-------SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELGI 187
|
90 100
....*....|....*....|.
gi 446536636 197 TLILISHDRDflDAIT--DHI 215
Cdd:COG3842 188 TFIYVTHDQE--EALAlaDRI 206
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
331-484 |
1.73e-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: 45.00 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 331 KLQIT--PNSRIGLLGMNGAGKSTLIKSLVGDLP-----LLAGERKASELLN-----IGYFAQHQM--DALDgQASPMLQ 396
Cdd:TIGR01257 948 RLNITfyENQITAFLGHNGAGKTTTLSILTGLLPptsgtVLVGGKDIETNLDavrqsLGMCPQHNIlfHHLT-VAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 397 LARIADKQISEATL--RSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHAL-SMAL 473
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLemEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIwDLLL 1105
|
170
....*....|.
gi 446536636 474 QDFEGAVVLVS 484
Cdd:TIGR01257 1106 KYRSGRTIIMS 1116
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-213 |
1.87e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRR--GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEVK-ALD 77
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRrVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 78 M-PAIDFVLSGDeeywdIQNKLAQPEQLTDSDLAKLHGRfdeihgysAPSKAAQLMAGLGfLEHQLRLNVASFSGGWRMR 156
Cdd:PLN03232 1314 IiPQSPVLFSGT-----VRFNIDPFSEHNDADLWEALER--------AHIKDVIDRNPFG-LDAEVSEGGENFSVGQRQL 1379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 157 LNLARTLMSRSDLLLLDEPTNHLDL--DAILWLEDWLKAYEGTLILISHDrdfLDAITD 213
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVDVrtDSLIQRTIREEFKSCTMLVIAHR---LNTIID 1435
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
34-220 |
2.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 43.57 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 34 GVNGAGKSTLFAALLGSLGADEGS-------LTRPSVWTVAHMAQEVkaLDMPAIDFVLSG--DEEYWDIQNKlaqpeql 104
Cdd:PRK13650 40 GHNGSGKSTTVRLIDGLLEAESGQiiidgdlLTEENVWDIRHKIGMV--FQNPDNQFVGATveDDVAFGLENK------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 105 tDSDLAKLHGRFDEihgysapskAAQLMAGLGFLEHQlrlnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---- 180
Cdd:PRK13650 111 -GIPHEEMKERVNE---------ALELVGMQDFKERE----PARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegr 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446536636 181 LDAILWLEDWLKAYEGTLILISHDRDFLdAITDHILHIEN 220
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKN 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-226 |
2.12e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 43.64 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 29 KIGLTGVNGAGKSTLFAALLGSLGADEGS-LTRPSVWTVAHMaQEVKALdmPAIDFVLSGDEEYwdiqnklaQPEQLTDS 107
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSvLIRGEPITKENI-REVRKF--VGLVFQNPDDQIF--------SPTVEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 108 DLAKLHGRFDEIHGYSAPSKAAQLMAglgfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDA 183
Cdd:PRK13652 101 AFGPINLGLDEETVAHRVSSALHMLG----LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 184 ILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
141-204 |
2.41e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.23 E-value: 2.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 141 QLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILISHD 204
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
150-203 |
2.49e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.05 E-value: 2.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLedwLKAY--EGTLILISH 203
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILEL---LAEHaqNKTVLMITH 532
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
312-474 |
2.55e-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: 42.99 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 312 LTLENASIGYGDKKIA--EKIKLQITPNSRIGLLGMNGAGKSTLIKSL-----------------VGDLPLlagerkASE 372
Cdd:cd03251 1 VEFKNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdsgrilidghdVRDYTL------ASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 373 LLNIGYFAQhqmDAL--DGQASPMLQLAR--IADKQISEAT----LRSFLGSF--GFS---GERMDTpcesFSGGERARL 439
Cdd:cd03251 75 RRQIGLVSQ---DVFlfNDTVAENIAYGRpgATREEVEEAAraanAHEFIMELpeGYDtviGERGVK----LSGGQRQRI 147
|
170 180 190
....*....|....*....|....*....|....*
gi 446536636 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQ 474
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALE 182
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
334-508 |
2.68e-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: 42.23 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 334 ITPNSRIGLLGMNGAGKSTLIKSLV---------GDLpLLAGERKASELLNIGYFAQHQmdaldgqaspmlqlariaDKQ 404
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAgrktagvitGEI-LINGRPLDKNFQRSTGYVEQQ------------------DVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 405 ISEATLRSFLgsfgfsgeRMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNhlDLDMRHALSMA-----LQDfEGA 479
Cdd:cd03232 91 SPNLTVREAL--------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTS--GLDSQAAYNIVrflkkLAD-SGQ 159
|
170 180 190
....*....|....*....|....*....|..
gi 446536636 480 VVLVS-HE-RQLIASVCDELLLVH-GGKCTEF 508
Cdd:cd03232 160 AILCTiHQpSASIFEKFDRLLLLKrGGKTVYF 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
138-240 |
2.70e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.08 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 138 LEHQLRLNVASF--------SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLI---LISHDRD 206
Cdd:PRK11124 123 EKLLERLRLKPYadrfplhlSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVE 202
|
90 100 110
....*....|....*....|....*....|....
gi 446536636 207 FLDAITDHILHIENQELtLYTGNYSTFETTRSER 240
Cdd:PRK11124 203 VARKTASRVVYMENGHI-VEQGDASCFTQPQTEA 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
149-204 |
2.71e-04 |
|
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: 43.50 E-value: 2.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDaiLwLEDwLKAYEG-TLILISHD 204
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqiLN--L-LKD-LQRELGlAILFITHD 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-223 |
2.79e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.94 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTLFAALlgslgadeGSLTRPSVWTVAHMAQEVKALDMPAIDFVLSgdEEYWDIQNKLAQ 100
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKPTSGTYRVAGQDVATLDADALAQLRR--EHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 101 PEQLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK10535 98 LSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLG-LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446536636 181 ------LDAILwleDWLKAYEGTLILISHDRDfLDAITDHILHIENQEL 223
Cdd:PRK10535 177 shsgeeVMAIL---HQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEI 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
427-527 |
2.84e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 427 PCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
90 100
....*....|....*....|....
gi 446536636 504 KCTefeGDLQDyakwlREARQQQI 527
Cdd:PRK13549 482 KLK---GDLIN-----HNLTQEQV 497
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
114-180 |
3.05e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.57 E-value: 3.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 114 GRFDEIHGYSAPSKAAQLMAGLGFLEHQLRLnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:NF000106 111 GR*LDLSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
305-462 |
3.14e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 43.06 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 305 TKMSSPLLTLENASIGYGD--KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERK------ASELL-- 374
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiSKENLke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 ---NIGYFAQH----------QMDALDGQASPMLQLARIADKqISEATLRSFLGSFgfsgerMDTPCESFSGGERARLAL 441
Cdd:PRK13632 81 irkKIGIIFQNpdnqfigatvEDDIAFGLENKKVPPKKMKDI-IDDLAKKVGMEDY------LDKEPQNLSGGQKQRVAI 153
|
170 180
....*....|....*....|.
gi 446536636 442 ALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLD 174
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
119-233 |
3.63e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.92 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 119 IHGYSAPSKAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-----------LDAilwl 187
Cdd:PRK13631 147 VKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgehemmqliLDA---- 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446536636 188 edwlKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTF 233
Cdd:PRK13631 223 ----KANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
143-241 |
4.39e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 143 RLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIE 219
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
|
90 100
....*....|....*....|..
gi 446536636 220 NQELtlyTGNYSTFETTRSERL 241
Cdd:PRK10982 466 NGLV---AGIVDTKTTTQNEIL 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
309-504 |
4.43e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 309 SPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------RKASELLNI 376
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkevtfngPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 377 GYFaqHQmdaldgqaspmlQLARIADKQISEATL--RSFLGSFG-FSGERM-----------------DTPCESFSGGER 436
Cdd:PRK10762 82 GII--HQ------------ELNLIPQLTIAENIFlgREFVNRFGrIDWKKMyaeadkllarlnlrfssDKLVGELSIGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 437 ARLALALIVWQRPNVLILDEPTNHL-DLDMRHALSM--ALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVirELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-203 |
4.57e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.52 E-value: 4.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446536636 143 RLN--VASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILISH 203
Cdd:PRK14267 142 RLNdyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-204 |
4.93e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 30 IGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEvkaldmPAIDFVLSGDEEYWDI---QNKLAQPEQLTD 106
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEE------ASVELEFEHGGKRYRIerrQGEFAEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 107 SDLAKLHGRFDEIHGY------------SAPSKAAQLMAGLGFLEHQLRL-----NVASFSGGWRMRLNLARTLMsrsdl 169
Cdd:COG0419 100 SERKEALKRLLGLEIYeelkerlkeleeALESALEELAELQKLKQEILAQlsgldPIETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*
gi 446536636 170 LLLDepTNHLDLDAILWLEDWLKAyegtLILISHD 204
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
127-223 |
5.00e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 127 KAAQLMAGLGF---LEHQLRL----NVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLKAyEG 196
Cdd:PRK11176 452 EAARMAYAMDFinkMDNGLDTvigeNGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTEserAIQAALDELQK-NR 530
|
90 100
....*....|....*....|....*....
gi 446536636 197 TLILISHDrdfLDAI--TDHILHIENQEL 223
Cdd:PRK11176 531 TSLVIAHR---LSTIekADEILVVEDGEI 556
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
300-507 |
5.33e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.71 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 300 SFREPTKMSSPLLTLENASIGYGDKKIAekikLQITPNSRIGLLGMNGAGKSTLIKSL--------------------VG 359
Cdd:PRK10070 21 AFKYIEQGLSKEQILEKTGLSLGVKDAS----LAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptrgqvlidgvdiakIS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 360 DLPLLAGERKASELLNIGYFAQHQMDALDGQASPMlQLARIADKQISEATLRSfLGSFGFSGERMDTPCEsFSGGERARL 439
Cdd:PRK10070 97 DAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGM-ELAGINAEERREKALDA-LRQVGLENYAHSYPDE-LSGGMRQRV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446536636 440 ALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK10070 174 GLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
432-504 |
5.48e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.41 E-value: 5.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 432 SGGERARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIAsVCDELLLVHGGK 504
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-180 |
5.64e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.99 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPSVWTVAHMAQEvkaldmpA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 81 IDFVLSGDEEYWDIQNKLAQPEQLTDSDLAKLHGRfdeihgysapskAAQLMAGLGFLEHQLRLnVASFSGGWRMRLNLA 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEI------------AHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGIA 140
|
170 180
....*....|....*....|
gi 446536636 161 RTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALD 160
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
303-462 |
5.75e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 41.95 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 303 EPTKMSSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSL-----------------VGDLPLLA 365
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgarvegeilLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 366 GERKASEL-LNIGYFAQhqmdaldgQASP--M---------LQLARIADK----QISEATLRSflgsfgfSG------ER 423
Cdd:COG1117 83 PDVDVVELrRRVGMVFQ--------KPNPfpKsiydnvaygLRLHGIKSKseldEIVEESLRK-------AAlwdevkDR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446536636 424 MDTPCESFSGGERARL----ALALivwqRPNVLILDEPTNHLD 462
Cdd:COG1117 148 LKKSALGLSGGQQQRLciarALAV----EPEVLLMDEPTSALD 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
314-458 |
6.02e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 314 LENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERK----ASELL--------------- 374
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL-------LSLIAGARKiqqgRVEVLggdmadarhrravcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 375 ---------------------NIGYFAQhqmdaLDGQASPMLQlARIADkqISEAT-LRSFLgsfgfsgermDTPCESFS 432
Cdd:NF033858 77 riaympqglgknlyptlsvfeNLDFFGR-----LFGQDAAERR-RRIDE--LLRATgLAPFA----------DRPAGKLS 138
|
170 180
....*....|....*....|....*...
gi 446536636 433 GGERARLAL--ALIvwQRPNVLILDEPT 458
Cdd:NF033858 139 GGMKQKLGLccALI--HDPDLLILDEPT 164
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
340-507 |
6.74e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.08 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 340 IGLLGMNGAGKSTLIKSLVGDLPLLAGE----RKASELLNIGYFAQH-QMDALDGQAS--PMLQLARIAD---------- 402
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGEllidDHPLHFGDYSYRSQRiRMIFQDPSTSlnPRQRISQILDfplrlntdle 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 403 -----KQISEaTLRSFlgsfGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQ 474
Cdd:PRK15112 122 peqreKQIIE-TLRQV----GLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQlinLMLELQ 196
|
170 180 190
....*....|....*....|....*....|....
gi 446536636 475 DFEG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK15112 197 EKQGiSYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
307-507 |
6.81e-04 |
|
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: 42.75 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 307 MSSPLLTLENASIGYGD----KKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP----------LLAGErkasE 372
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaahpsgsiLFDGQ----D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 373 LLN-------------IGYFAQHQMDALDgqasPmlqLARIAdKQISEATLRSFlgsfGFSGE----------------- 422
Cdd:COG4172 78 LLGlserelrrirgnrIAMIFQEPMTSLN----P---LHTIG-KQIAEVLRLHR----GLSGAaararalellervgipd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 423 ---RMDT-PCEsFSGGERAR----LALALivwqRPNVLILDEPTNHLD-------LDmrhaLSMALQDFEG-AVVLVSHE 486
Cdd:COG4172 146 perRLDAyPHQ-LSGGQRQRvmiaMALAN----EPDLLIADEPTTALDvtvqaqiLD----LLKDLQRELGmALLLITHD 216
|
250 260
....*....|....*....|.
gi 446536636 487 RQLIASVCDELLLVHGGKCTE 507
Cdd:COG4172 217 LGVVRRFADRVAVMRQGEIVE 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
308-497 |
8.06e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 308 SSPLLTLENASIGYGDKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkaselLNIGYFAQH---QM 384
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS------ILIDGQEMRfasTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 385 DALDG---------QASPMLQLAR------------IADKQISEATLRSFLGSFgfsGERMD--TPCESFSGGERARLAL 441
Cdd:PRK11288 75 AALAAgvaiiyqelHLVPEMTVAEnlylgqlphkggIVNRRLLNYEAREQLEHL---GVDIDpdTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 442 ALIVWQRPNVLILDEPTNHL---DLDMRHALSMALQDfEGAVVL-VSHERQLIASVCDEL 497
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRA-EGRVILyVSHRMEEIFALCDAI 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
132-206 |
8.17e-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: 41.86 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 132 MAGLGFLEHQLrlnVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLKAyegTLILISHD 204
Cdd:cd03294 147 LVGLEGWEHKY---PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAELQK---TIVFITHD 220
|
..
gi 446536636 205 RD 206
Cdd:cd03294 221 LD 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
149-223 |
8.83e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.94 E-value: 8.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446536636 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL----KAYEGTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
329-492 |
9.02e-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: 40.77 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 329 KIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDlpllAGERKASELLNIgyFAQHQMDALDgqaspmlQLARIADKQISEA 408
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPK--FSRNKLIFID-------QLQFLIDVGLGYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 409 TLrsflgsfgfsGERMDTpcesFSGGERARLALA--LIVWQRPNVLILDEPTNHLDL-DMRHALSM--ALQDFEGAVVLV 483
Cdd:cd03238 80 TL----------GQKLST----LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQqDINQLLEVikGLIDLGNTVILI 145
|
....*....
gi 446536636 484 SHERQLIAS 492
Cdd:cd03238 146 EHNLDVLSS 154
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-204 |
1.09e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 14 RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADegsltrpsvwtVAHMAQEVKALDMPAIDFVLSGDEEYWD 93
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAG-----------VRQTAGRVLLDGKPVAPCALRGRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 94 IQN-KLAQPEQLTDSDLAKLHGRFDEIHGYSAPSKAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:PRK10418 85 MQNpRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 446536636 173 DEPTNHLDLDA---ILWLEDWLKAYEGT-LILISHD 204
Cdd:PRK10418 165 DEPTTDLDVVAqarILDLLESIVQKRALgMLLVTHD 200
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
362-498 |
1.25e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 362 PLLAGERKASELLNIGYFAQHQMDALDGQA----SPMLQLARIADKqiSEAtlrsfLGSFGFSGERMDTPCESFSGGERA 437
Cdd:PRK00635 744 PSCLGKRFLPQVLEVRYKGKNIADILEMTAyeaeKFFLDEPSIHEK--IHA-----LCSLGLDYLPLGRPLSSLSGGEIQ 816
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 438 RLALA---LIVWQRPNVLILDEPTNHLDLDMRHALSMALQD--FEGAVVLVSHERQLIASVCDELL 498
Cdd:PRK00635 817 RLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSltHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
138-180 |
1.30e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.55 E-value: 1.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446536636 138 LEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11000 123 LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
431-546 |
1.44e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 431 FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVS----HERQLIA---SVCDELLLVH 501
Cdd:NF000106 145 YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTtqymEEAEQLAhelTVIDRGRVIA 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446536636 502 GGKCTEFEGDLQDYAKWLREARQQQINAQT-AIEQNNSSSAAPAPA 546
Cdd:NF000106 225 DGKVDELKTKVGGRTLQIRPAHAAELDRMVgAIAQAGLDGIAGATA 270
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-204 |
1.50e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.85 E-value: 1.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446536636 143 RLNVASF--SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG--TLILISHD 204
Cdd:PRK14271 156 RLSDSPFrlSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-209 |
1.52e-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: 40.00 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 134 GLGFLehQLRLNVASFSGGWRMRLNLARTLMSRSD--LLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFL 208
Cdd:cd03238 75 GLGYL--TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidLGnTVILIEHNLDVL 152
|
.
gi 446536636 209 D 209
Cdd:cd03238 153 S 153
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
1.61e-03 |
|
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: 40.40 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSltrpsVWTVAHMAQEVKALDMpAI 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGT-----ILFGGEDATDVPVQER-NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 82 DFVLsgdeeywdiQNkLAQPEQLTDSDLAKLHGRfdEIHGYSAPSKA---AQLMAGLGFLE---------HQLrlnvasf 149
Cdd:cd03296 77 GFVF---------QH-YALFRHMTVFDNVAFGLR--VKPRSERPPEAeirAKVHELLKLVQldwladrypAQL------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG----TLILISHDRDFLDAITDHIL 216
Cdd:cd03296 138 SGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVV 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
140-507 |
1.65e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 140 HQLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWL-KAYEGTLILISHDRDFLDAITDHI 215
Cdd:PRK10261 167 HQL-------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 216 lhienqeLTLYTGnySTFETTRSERLaqqqqafekqqearahlqkfidrFKAKATKARQA-QSRIKQLERMQQLapahvD 294
Cdd:PRK10261 240 -------LVMYQG--EAVETGSVEQI-----------------------FHAPQHPYTRAlLAAVPQLGAMKGL-----D 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 295 TPFTF---SFREPTKMSS-----------PLLTLENASIGYG-----------DKKIAEKIKLQITPNSRIGLLGMNGAG 349
Cdd:PRK10261 283 YPRRFpliSLEHPAKQEPpieqdtvvdgePILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 350 KST-------LIKSLVGDLpLLAGER----KASELL----NIGYFAQHQMDALDGQA----SPM--LQLARIADKQISEA 408
Cdd:PRK10261 363 KSTtgrallrLVESQGGEI-IFNGQRidtlSPGKLQalrrDIQFIFQDPYASLDPRQtvgdSIMepLRVHGLLPGKAAAA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 409 TLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQ-DFEGAVVLVS 484
Cdd:PRK10261 442 RVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQiinLLLDLQrDFGIAYLFIS 521
|
410 420
....*....|....*....|...
gi 446536636 485 HERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK10261 522 HDMAVVERISHRVAVMYLGQIVE 544
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
147-220 |
1.69e-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: 40.53 E-value: 1.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 147 ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL----KAYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:TIGR01184 113 GQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDVDEALLLSDRVVMLTN 190
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-180 |
1.79e-03 |
|
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: 41.24 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLH--PGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpsvwtvahmaqevkaLDMP 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLViePGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIL----------------LDGH 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 80 AI-DFVLSgdeeywDIQNKLAQPEQ---LTDSDLAK--LHGRFDEIHgySAPSKAAQLMAGLGFLEHQLRL--------N 145
Cdd:TIGR02203 395 DLaDYTLA------SLRRQVALVSQdvvLFNDTIANniAYGRTEQAD--RAEIERALAAAYAQDFVDKLPLgldtpigeN 466
|
170 180 190
....*....|....*....|....*....|....*
gi 446536636 146 VASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
150-216 |
1.90e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 40.80 E-value: 1.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWL-EDWLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgRDEILNKiKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
330-505 |
1.91e-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: 40.61 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 330 IKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASellnigyfaqhqmdaldGQASPMLQLARIADKQISEAT 409
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-----------------GRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 410 LrsflgsFGFS----------------------GERMDTPCE----SFSGGERARLALALIVWQRPNVLILDEPTNHLDL 463
Cdd:cd03291 119 I------FGVSydeyryksvvkacqleeditkfPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446536636 464 DMRHALsmalqdFEGAV--VLVSHERQLIAS------VCDELLLVHGGKC 505
Cdd:cd03291 193 FTEKEI------FESCVckLMANKTRILVTSkmehlkKADKILILHEGSS 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-223 |
1.93e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.58 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 21 SMQLHPGWKIGLTGVNGAGKSTL---FAALLgslgadegsltRPSVWTVA----HMAQEVKALDMPAIDFVLSGDEEYWD 93
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLmqhFNALL-----------KPSSGTITiagyHITPETGNKNLKKLRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 94 IQnkLAQPEQLTDSDLAKLHGRFDEihgYSAPSKAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:PRK13641 96 AQ--LFENTVLKDVEFGPKNFGFSE---DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446536636 174 EPTNHLDLDAILWLEDWLKAYEG---TLILISHDRDFLDAITDHILHIENQEL 223
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-215 |
2.08e-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: 40.30 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT-------------RPsVWTV-- 66
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILldgkditnlpphkRP-VNTVfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 67 -----AHMaqevkaldmpaidfvlsgdeeywDIQNKLAQPEQLTDSDLAKLHGRFDEihgysapskaAQLMAGLGFLEHQ 141
Cdd:cd03300 80 nyalfPHL-----------------------TVFENIAFGLRLKKLPKAEIKERVAE----------ALDLVQLEGYANR 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 142 lrlNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDWLKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03300 127 ---KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHDQEEALTMSDRI 201
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-216 |
2.10e-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: 41.15 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 134 GLGFLehQLRLNVASFSGGWRMRLNLARTLMSRSD---LLLLDEPTNHLDLDAILWLED---WLKAYEGTLILISHDrdf 207
Cdd:TIGR00630 817 GLGYI--RLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEvlqRLVDKGNTVVVIEHN--- 891
|
90
....*....|.
gi 446536636 208 LDAI--TDHIL 216
Cdd:TIGR00630 892 LDVIktADYII 902
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-203 |
2.14e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 2.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 143 RLNV--ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAI-----LWLEdwLKAyEGTLILISH 203
Cdd:PRK14247 139 RLDApaGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTakiesLFLE--LKK-DMTIVLVTH 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
124-206 |
2.15e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.45 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 124 APSKAAQLMAGLGFLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLKAYEGTLIL 200
Cdd:PRK13651 141 AKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIIL 220
|
....*.
gi 446536636 201 ISHDRD 206
Cdd:PRK13651 221 VTHDLD 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
138-215 |
2.17e-03 |
|
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: 39.93 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 138 LEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNhlDLDAILWLE------DWLKAYEGTLILISHDRDFLDAI 211
Cdd:cd03301 120 IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS--NLDAKLRVQmraelkRLQQRLGTTTIYVTHDQVEAMTM 197
|
....
gi 446536636 212 TDHI 215
Cdd:cd03301 198 ADRI 201
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
519-622 |
2.22e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 519 LREARQQQINAQTAIEQNNSSSAApapAKVDKEAQRKEAARRREQTRPIRKNIEKVESQIEKLQPRLAEIEEALADTSLY 598
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQLQA---AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144
|
90 100
....*....|....*....|....
gi 446536636 599 EANRKDDLLKLMNEQTELKAKLEQ 622
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAA 168
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-60 |
2.47e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 2.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446536636 18 QKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTR 60
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDR 83
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
432-462 |
2.50e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.45 E-value: 2.50e-03
10 20 30
....*....|....*....|....*....|.
gi 446536636 432 SGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-215 |
2.56e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.77 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 14 RVLfQKASMQLHPGwKI-GLTGVNGAGKSTLFAALLGSLGADEGSLT---RPSVWTVAHMA---------QEVkAL--DM 78
Cdd:COG1129 18 KAL-DGVSLELRPG-EVhALLGENGAGKSTLMKILSGVYQPDSGEILldgEPVRFRSPRDAqaagiaiihQEL-NLvpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 79 PAIDFVLSGDEeywdiqnklaqpeqltdsdlAKLHGRFD--EIHgysapSKAAQLMAGLGfLEHQLRLNVASFSGGWRMR 156
Cdd:COG1129 95 SVAENIFLGRE--------------------PRRGGLIDwrAMR-----RRARELLARLG-LDIDPDTPVGDLSVAQQQL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWL----EDwLKAyEG-TLILISHdrdFLD---AITDHI 215
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLfriiRR-LKA-QGvAIIYISH---RLDevfEIADRV 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-504 |
2.86e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 325 KIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLNIGYFAQHQMDALDGQASPM 394
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSilfqgkeidfKSSKEALENGISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 395 --LQLAR-------IADKQISEATLRSFlgsfgfsgERMDTPCE------SFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:PRK10982 92 dnMWLGRyptkgmfVDQDKMYRDTKAIF--------DELDIDIDprakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446536636 460 HL-DLDMRHALSM--ALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK10982 164 SLtEKEVNHLFTIirKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
148-240 |
3.20e-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: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQel 223
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDRIHVFEGE-- 148
|
90
....*....|....*..
gi 446536636 224 tlyTGNYSTFETTRSER 240
Cdd:cd03222 149 ---PGVYGIASQPKGTR 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-218 |
4.70e-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: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 32 LTGVNGAGKSTLFAALLGslgadegsltrpsvwtvaHMAQEVKA----------LDMPaID-------Fvlsgdeeywdi 94
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMG------------------HPKYEVTSgsilldgediLELS-PDeraragiF----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 95 qnkLA--QPEQ---LTDSDL---AKLHGRFDEIHGYSAPSKAAQLMAGLG----FLEhqlR-LNVaSFSGGWRMRLNLAR 161
Cdd:COG0396 81 ---LAfqYPVEipgVSVSNFlrtALNARRGEELSAREFLKLLKEKMKELGldedFLD---RyVNE-GFSGGEKKRNEILQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISHDRDFLDAITDHILHI 218
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILDYIKPDFVHV 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
310-462 |
4.71e-03 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 39.46 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 310 PLLTLENASIGYG----DKKIAEKIKLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG--------------ERkas 371
Cdd:COG4525 2 SMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGeitldgvpvtgpgaDR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 372 ellniGYFAQHQ-----MDALDGQASPmLQLA---RIADKQISEATLRsFLGSFGFSGERMDtpceSFSGGERARLALAL 443
Cdd:COG4525 79 -----GVVFQKDallpwLNVLDNVAFG-LRLRgvpKAERRARAEELLA-LVGLADFARRRIW----QLSGGMRQRVGIAR 147
|
170
....*....|....*....
gi 446536636 444 IVWQRPNVLILDEPTNHLD 462
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
150-216 |
6.04e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 6.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446536636 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAyEG-TLILISHDRDFLDAITDHIL 216
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAkkeIYQLINQFKA-EGlSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
432-485 |
6.07e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 38.92 E-value: 6.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446536636 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG----AVVLVSH 485
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH 203
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
524-623 |
6.10e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 524 QQQINAQTA-IEQNNSSSAApapakvdkeaqrkEAARRREQTRPIRKNIEKVESQIEKLQPRLAEIEEALADTSlyeanr 602
Cdd:PHA02562 194 QQQIKTYNKnIEEQRKKNGE-------------NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS------ 254
|
90 100
....*....|....*....|.
gi 446536636 603 kDDLLKLMNEQTELKAKLEQY 623
Cdd:PHA02562 255 -AALNKLNTAAAKIKSKIEQF 274
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
432-507 |
7.71e-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: 38.29 E-value: 7.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446536636 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
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|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
127-223 |
8.36e-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: 38.44 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 127 KAAQLMAGLG-----FLE---HQLrlnvasfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYE--- 195
Cdd:cd03295 113 RADELLALVGldpaeFADrypHEL-------SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQqel 185
|
90 100
....*....|....*....|....*....
gi 446536636 196 -GTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03295 186 gKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
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|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
147-206 |
8.46e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 38.91 E-value: 8.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446536636 147 ASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK----AYEGTLILISHDRD 206
Cdd:PRK10851 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlheELKFTSVFVTHDQE 198
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|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
135-181 |
8.79e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 38.70 E-value: 8.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446536636 135 LGfLEHQLRLNVASFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:PRK11144 116 LG-IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-203 |
8.87e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 8.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLE----DWLKAYEGTLILISH 203
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH 1417
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
133-216 |
9.86e-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: 38.36 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536636 133 AGLGFLehQLRLNVASFSGGWRMRLNLARTLMSRSD---LLLLDEPTNHL---DLDAILWLEDWLKAYEGTLILISHDRD 206
Cdd:cd03271 156 VGLGYI--KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
90
....*....|
gi 446536636 207 FLdAITDHIL 216
Cdd:cd03271 234 VI-KCADWII 242
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