|
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: 723.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKALDMPA 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLSGDEEFWDIQNKLAQPDQLTD-FELAKLHGRFDEIHGYSAPSKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNL 159
Cdd:PRK10636 81 LEYVIDGDREYRQLEAQLHDANERNDgHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFETTRSE 239
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 240 RLAQQQQAFEKQQETRAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDTPFTFSFREPTKMSSPLLTLDNASI 319
Cdd:PRK10636 241 RLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 320 GYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDALDGHASPMLQLAR 399
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLAR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 400 IADKQiSEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA 479
Cdd:PRK10636 401 LAPQE-LEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 480 VVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDYAKWLREARQQQINAQTAVAQNNSSSaapapAKVDKEAQRKEaAR 559
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANS-----AQARKDQKRRE-AE 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 560 RREQTRPIRKNIEKVESQIEKLQPQLAKIEESLADTSLYEAARKDDLLKLMNEQTELKAKLEQ 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: 686.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 4 FDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKALD-MPAID 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDdLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 83 FVLSGDEEFWDIQNKLAQPDQLTDF------ELAKLHGRFDEIHGYSAPSKAAQLMAGLGFLENQLRLNVESFSGGWRMR 156
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEpdedleRLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFETT 236
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 237 RSERLAQQQQAFEKQQETRAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDTPFTFSFREPTKMSSPLLTLDN 316
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKKVLELEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 317 ASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQmDALDGHASPMLQ 396
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDKTVLDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 397 LARIADKQiSEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF 476
Cdd:COG0488 400 LRDGAPGG-TEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 492309081 477 EGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDYAKW 518
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-520 |
1.90e-122 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 379.59 E-value: 1.90e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALlgSLGADEGSltrPTGWTVAHMAQEVKALDMPAI 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM--AMHAIDGI---PKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 DFVLSGDEE---FWDIQNKLAQPDQLTDFE----------------------LAKLHGRFDEIHGYSAPSKAAQLMAGLG 136
Cdd:PLN03073 253 QCVLNTDIErtqLLEEEAQLVAQQRELEFEtetgkgkgankdgvdkdavsqrLEEIYKRLELIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 137 FLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:PLN03073 333 FTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 217 HIENQELTLYTGNYSTFETTRSERLAQQQQAFEKQQETRAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDTP 296
Cdd:PLN03073 413 HLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 297 FTFSFREPT-KMSSPLLTLDNASIGY-GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELL 374
Cdd:PLN03073 493 YKFEFPTPDdRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 NIGYFAQHQMDALDGHASPMLQLARIAdKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCF-PGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLL 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 455 DEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDYAKWLR 520
Cdd:PLN03073 652 DEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQ 717
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-515 |
2.69e-102 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 321.46 E-value: 2.69e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKAL-DMP 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFeEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 AIDFVLSGDEEFWDIQNK----LAQPDQLTD--FELAKLHGRFDEIHGYSAPSKAAQLMAGLGFLENQLRLNVESFSGGW 153
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQErdriYALPEMSEEdgMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 154 RMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTF 233
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 234 ETTRS---ERLAQQQQAFEKQQetrAHLQKFIDRFKAKATKARQAQSRIKQLERMQ--QLAPAHVDTPFtFSFREPTKMS 308
Cdd:PRK15064 241 MTAATqarERLLADNAKKKAQI---AELQSFVSRFSANASKAKQATSRAKQIDKIKleEVKPSSRQNPF-IRFEQDKKLH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 309 SPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDALD 388
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 GHASPMLQLARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:PRK15064 397 NDLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIES 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 492309081 469 LSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGDLQDY 515
Cdd:PRK15064 477 LNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-520 |
5.10e-80 |
|
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: 263.72 E-value: 5.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQE--------VKALDMPAIDF 83
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEpqldptktVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 84 VLSGDEEFWDIQNKLAQPDQltDF-----ELAKLHGRFDEIHGYSAPSKAAQLMaglgfleNQLRL-----NVESFSGGW 153
Cdd:TIGR03719 96 IKDALDRFNEISAKYAEPDA--DFdklaaEQAELQEIIDAADAWDLDSQLEIAM-------DALRCppwdaDVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 154 RMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTF 233
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 234 ETTRSERLAQQQQafekqqeTRAHLQKFIDR---FKAKATKARQAQS--RIKQLERMQQLApahvdtpftFSFREPT--- 305
Cdd:TIGR03719 247 LEQKQKRLEQEEK-------EESARQKTLKReleWVRQSPKGRQAKSkaRLARYEELLSQE---------FQKRNETaei 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 306 ------KMSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYF 379
Cdd:TIGR03719 311 yippgpRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 AQHQmDALDGHA------SPMLQLARIADKQISEatlRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:TIGR03719 391 DQSR-DALDPNKtvweeiSGGLDIIKLGKREIPS---RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 454 LDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHG-GKCTEFEGDLQDYAKWLR 520
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGdSHVEWFEGNFSEYEEDKK 534
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-586 |
3.38e-76 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 255.65 E-value: 3.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 16 LFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEV-KALDMPAIDFVLSGDEE---- 90
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPpRNVEGTVYDFVAEGIEEqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 91 ---FWDIQNKLAQ-PDQLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNveSFSGGWRMRLNLARTLMSR 166
Cdd:PRK11147 98 lkrYHDISHLVETdPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLG-LDPDAALS--SLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 167 SDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFETTRSERLAQQQQ 246
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVEEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 247 AFEKQQETRAHLQKFIdRFKAKATKARQaQSRIKQL-----ERMQQL-----APAHVDTpftfsfrepTKMSSPLL-TLD 315
Cdd:PRK11147 255 QNAEFDRKLAQEEVWI-RQGIKARRTRN-EGRVRALkalrrERSERRevmgtAKMQVEE---------ASRSGKIVfEME 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQmDALDGHASPML 395
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR-AELDPEKTVMD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 396 QLARiaDKQISEATLR-----SFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:PRK11147 403 NLAE--GKQEVMVNGRprhvlGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 471 MALQDFEGAVVLVSHERQLIASVCDELLLVHG-GKCTEFEGDLQDyakwlreARQQQINAQtavAQNNSSSAAPAPAKVD 549
Cdd:PRK11147 481 ELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGnGKIGRYVGGYHD-------ARQQQAQYL---ALKQPAVKKKEEAAAP 550
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 492309081 550 KEAQRKEAARR------RE-QTRPIRknIEKVESQIEKLQPQLA 586
Cdd:PRK11147 551 KAETVKRSSKKlsyklqRElEQLPQL--LEDLEAEIEALQAQVA 592
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-521 |
2.30e-72 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 243.49 E-value: 2.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLF---AallgslGAD---EGSLTRPTGWTVAHMAQEVKaLD-------- 77
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLrimA------GVDkefEGEARPAPGIKVGYLPQEPQ-LDpektvren 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 -MPAIDFVLSGDEEFWDIQNKLAQPDqlTDF-----ELAKLHGRFDEIHGYSAPSKAAQLMaglgfleNQLRL-----NV 146
Cdd:PRK11819 91 vEEGVAEVKAALDRFNEIYAAYAEPD--ADFdalaaEQGELQEIIDAADAWDLDSQLEIAM-------DALRCppwdaKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 147 ESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 227 TGNYSTFETTRSERLaqqqqafEKQQETRAHLQKFIDR---FKAKATKARQAQS--RIKQLERMQQLApahvdtpftFSF 301
Cdd:PRK11819 242 EGNYSSWLEQKAKRL-------AQEEKQEAARQKALKReleWVRQSPKARQAKSkaRLARYEELLSEE---------YQK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 302 REPT---------KMSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASE 372
Cdd:PRK11819 306 RNETneifippgpRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 373 LLNIGYFAQHQmDALDGHA------SPMLQLARIADKQISEatlRSFLGSFGFSGERMDTPCESFSGGERARLALALIVW 446
Cdd:PRK11819 386 TVKLAYVDQSR-DALDPNKtvweeiSGGLDIIKVGNREIPS---RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLK 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 447 QRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHG-GKCTEFEGDLQDYAKWLRE 521
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGdSQVEWFEGNFQEYEEDKKR 537
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-222 |
8.24e-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: 183.42 E-value: 8.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQevkaldmpai 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 dfvlsgdeefwdiqnklaqpdqltdfelaklhgrfdeihgysapskaaqlmaglgflenqlrlnvesFSGGWRMRLNLAR 161
Cdd:cd03221 71 -------------------------------------------------------------------LSGGEKMRLALAK 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQE 222
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-234 |
1.12e-53 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 191.82 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKALDmpa 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELD--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 idfvlsGDEEFWDiqnklaqpdqltdfELAKLHGRFDEIHgysapskAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLA 160
Cdd:COG0488 392 ------PDKTVLD--------------ELRDGAPGGTEQE-------VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTFE 234
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
312-504 |
2.37e-49 |
|
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: 168.40 E-value: 2.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQhqmdaldgha 391
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 392 spmlqlariadkqiseatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 492309081 472 ALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
314-602 |
8.14e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 172.94 E-value: 8.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 314 LDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQ--------MD 385
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPpldddltvLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 386 A-LDGH-----------------ASPMLQLARIADKQI---------SEATLRSFLGSFGFSGERMDTPCESFSGGERAR 438
Cdd:COG0488 81 TvLDGDaelraleaeleeleaklAEPDEDLERLAELQEefealggweAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 439 LALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGdlqDYAKW 518
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPG---NYSAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 519 LrEARQQQINAQtavaqnnsssaapapakvDKEAQRKEAARRREQTRpIRKNIEK------VES---QIEKLQPQLAKIE 589
Cdd:COG0488 238 L-EQRAERLEQE------------------AAAYAKQQKKIAKEEEF-IRRFRAKarkakqAQSrikALEKLEREEPPRR 297
|
330
....*....|...
gi 492309081 590 ESLADTSLYEAAR 602
Cdd:COG0488 298 DKTVEIRFPPPER 310
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-507 |
1.67e-35 |
|
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: 140.42 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADegslTRPTGwTVAHMAQEVKALDM----PAID 82
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHG----GRISG-EVLLDGRDLLELSEalrgRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 83 FVLsgdeefwdiQNKLAQPDQLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLART 162
Cdd:COG1123 87 MVF---------QDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVG-LERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 163 LMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIENQELTlytgnystfETTRS 238
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIV---------EDGPP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 239 ERLaqqqqafekqqetrahlqkfidrfkakatkarqaqsrikqLERMQQLAPAHVDTPFTFSFREPTKMSSPLLTLDNAS 318
Cdd:COG1123 228 EEI----------------------------------------LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 319 IGY-----GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERKASELLNIGYF 379
Cdd:COG1123 268 KRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSLRELRRRVQMV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 AQHQMDALDghasPM----------LQLARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALA--LIVwq 447
Cdd:COG1123 348 FQDPYSSLN----PRmtvgdiiaepLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAraLAL-- 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 448 RPNVLILDEPTNHLDLDMRHA---LSMALQD-FEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:COG1123 422 EPKLLILDEPTSALDVSVQAQilnLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
307-527 |
4.32e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 4.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------RKASELLNIGYFA 380
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTvrlfgkPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 381 QH-QMDA-------------LDGHaSPMLQLARIADKQISEATLRSfLGSFGFSGERMDTpcesFSGGE--RARLALALI 444
Cdd:COG1121 82 QRaEVDWdfpitvrdvvlmgRYGR-RGLFRRPSRADREAVDEALER-VGLEDLADRPIGE----LSGGQqqRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 445 vwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCteFEGDLQDY--AKWL 519
Cdd:COG1121 156 --QDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVltPENL 231
|
....*...
gi 492309081 520 REARQQQI 527
Cdd:COG1121 232 SRAYGGPV 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
311-504 |
5.96e-32 |
|
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: 124.39 E-value: 5.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASEL-LNIGYF 379
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlasLSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 AQHQMDALD------------GHASPMLQLARiADKQISEATLRSfLGSFGFSgermDTPCESFSGGERAR--LALALIv 445
Cdd:COG1120 81 PQEPPAPFGltvrelvalgryPHLGLFGRPSA-EDREAVEEALER-TGLEHLA----DRPVDELSGGERQRvlIARALA- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 446 wQRPNVLILDEPTNHLDLdmRHALSM-----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 |
1.40e-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: 129.67 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpTGWTV--AHMAQEVKALDmp 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE--IGETVklAYVDQSRDALD-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 aidfvlsGDEEFWD-IQNKLaqpDQLtdfelaklhgrfdEIHGYSAPSKAaqLMAGLGFLENQLRLNVESFSGGWRMRLN 158
Cdd:TIGR03719 399 -------PNKTVWEeISGGL---DII-------------KLGKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVH 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIE-NQELTLYTGNYSTFETTR 237
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEEDK 533
|
....
gi 492309081 238 SERL 241
Cdd:TIGR03719 534 KRRL 537
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-220 |
6.52e-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: 119.89 E-value: 6.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPTGWTVAHMAQEVKAL- 76
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngEPIRDAREDYRRRLAYLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DMPAIDFVLSGDE--EFWdiqnklaqpdqltdfelAKLHGRFDeihgysAPSKAAQLMAGLGfLENQLRLNVESFSGGWR 154
Cdd:COG4133 82 HADGLKPELTVREnlRFW-----------------AALYGLRA------DREAIDEALEAVG-LAGLADLPVRQLSAGQK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISHDRDFLDAitDHILHIEN 220
Cdd:COG4133 138 RRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAA--ARVLDLGD 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
313-506 |
1.15e-29 |
|
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: 115.61 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 313 TLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASEL-LNIGYFAQ 381
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEilldgkdlasLSPKELaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 hqmdALDghaspMLQLARIADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03214 81 ----ALE-----LLGLAHLADRPFNE-----------------------LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492309081 462 DLDMRHALsMAL-----QDFEGAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:cd03214 129 DIAHQIEL-LELlrrlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-241 |
1.34e-28 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 120.61 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpTGWTV--AHMAQEVKALDmp 79
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK--IGETVklAYVDQSRDALD-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 aidfvlsgdeefwdiqnklaqPDQlTDFElaKLHGRFDEIH--GYSAPSKAaqLMAGLGFLENQLRLNVESFSGGWRMRL 157
Cdd:PRK11819 401 ---------------------PNK-TVWE--EISGGLDIIKvgNREIPSRA--YVGRFNFKGGDQQKKVGVLSGGERNRL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIE-NQELTLYTGNYSTFETT 236
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEYEED 534
|
....*
gi 492309081 237 RSERL 241
Cdd:PRK11819 535 KKRRL 539
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-241 |
1.41e-28 |
|
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: 114.57 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPtGWTVAHMAQEVKAldmpA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GEDVRKEPREARR----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IdFVLSGDEEFWDIqnklaqpdqLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLA 160
Cdd:COG4555 76 I-GVLPDERGLYDR---------LTVRENIRYFAELYGLFDEELKKRIEELIELLG-LEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHILHIENQELtLYTGNYSTF-ETT 236
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALCDRVVILHKGKV-VAQGSLDELrEEI 223
|
....*
gi 492309081 237 RSERL 241
Cdd:COG4555 224 GEENL 228
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
216-301 |
9.89e-28 |
|
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: 106.50 E-value: 9.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 216 LHIENQELTLYTGNYSTFETTRSERLAQQQQAFEKQQETRAHLQKFIDRFKAKATKARQAQSRIKQLERMQQLAPAHVDT 295
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*.
gi 492309081 296 PfTFSF 301
Cdd:pfam12848 81 P-KLRF 85
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
321-504 |
1.53e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.31 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELL-NIGYFAQHqmDALDGH 390
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedvaRDPAEVRrRIGYVPQE--PALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 ASPMLQLARIA-----DKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:COG1131 88 LTVRENLRFFArlyglPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492309081 466 RHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1131 167 RRELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
312-504 |
1.82e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.29 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkaseLLN---------------I 376
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI----YLDgkplsampppewrrqV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GYFAQhQMDALDGHASPMLQLA-RIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILD 455
Cdd:COG4619 77 AYVPQ-EPALWGGTVRDNLPFPfQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492309081 456 EPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-223 |
2.19e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.21 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---------RPTGW--TVAHMA 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPEWrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 71 QEVKALDMPAIDFvlsgdeefwdiqnkLAQPDQLTdfelaklHGRFDeihgysaPSKAAQLMAGLGFLENQLRLNVESFS 150
Cdd:COG4619 81 QEPALWGGTVRDN--------------LPFPFQLR-------ERKFD-------RERALELLERLGLPPDILDKPVERLS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA----ILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:COG4619 133 GGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
314-505 |
2.62e-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: 106.85 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 314 LDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPL------LAGERKASELLNIGYFAQH-QMD- 385
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtsgsirVFGKPLEKERKRIGYVPQRrSIDr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 386 ------------ALDGHASPMLQLARiADKQISEATLRsFLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLI 453
Cdd:cd03235 82 dfpisvrdvvlmGLYGHKGLFRRLSK-ADKAKVDEALE-RVGLSELADRQIGE----LSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 454 LDEPTNHLDLDMRHA---LSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:cd03235 156 LDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
9.09e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.30 E-value: 9.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKALdmpaI 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV-LGEDVARDPAEVRRR----I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 DFVLsgdEEFwdiqnklAQPDQLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLAR 161
Cdd:COG1131 76 GYVP---QEP-------ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHIL 216
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVA 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
312-504 |
1.46e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 103.63 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELL-NIGYFAQ 381
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEikvlgkdikKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HqmdaldghasPMLqlariadkqISEATLRSFLgsfgfsgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03230 81 E----------PSL---------YENLTVRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492309081 462 DLDMRHALSMALQDF---EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03230 127 DPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
307-530 |
7.44e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 109.65 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSspLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------------- 367
Cdd:PRK11147 1 MS--LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivarlqqdpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 368 -------------RKASELLNIGYFAQHQMdALDGHASPMLQLARIADK-------QIsEATLRSFLGSFGFSGermDTP 427
Cdd:PRK11147 79 vegtvydfvaegiEEQAEYLKRYHDISHLV-ETDPSEKNLNELAKLQEQldhhnlwQL-ENRINEVLAQLGLDP---DAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 428 CESFSGG--ERARLALALIVwqRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PRK11147 154 LSSLSGGwlRKAALGRALVS--NPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
250 260 270
....*....|....*....|....*....|
gi 492309081 506 TEFEGDLQDY----AKWLR-EARQqqiNAQ 530
Cdd:PRK11147 232 VSYPGNYDQYllekEEALRvEELQ---NAE 258
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
311-504 |
7.65e-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: 103.78 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELL----NIGYFa 380
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpdsgsiLIDGEDVRKEPRearrQIGVL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 381 qhqmdaLDGHASP-------MLQ-LARIADKQISEATLR--SFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPN 450
Cdd:COG4555 80 ------PDERGLYdrltvreNIRyFAELYGLFDEELKKRieELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 451 VLILDEPTNHLDLDMRHALS---MALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLReilRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
313-504 |
2.35e-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: 99.63 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 313 TLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkasellnigyfaqhqmdaldghas 392
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 393 pmlqlARIADKQISEATLRSFLGSFGFsgermdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMA 472
Cdd:cd00267 56 -----ILIDGKDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 492309081 473 LQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd00267 123 LRELaeEGrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-223 |
6.90e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 98.62 E-value: 6.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahmaqevkaldmpai 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 dfvlsgdeefwdiqnklaqpdqltdfelaklhgrfdeIHGYSAPSKAAQLMAGLGFL--ENQL--RLNVE---SFSGGWR 154
Cdd:cd03230 59 -------------------------------------VLGKDIKKEPEEVKRRIGYLpeEPSLyeNLTVRenlKLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILI-SHDRDFLDAITDHILHIENQEL 223
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkEGKTILLsSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-220 |
1.73e-23 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 97.32 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 3 QFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahmaqevkaldmpaID 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------------------ID 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 83 FVLSGDEEFWDIQNKLAQPDQLtdfelaklhgrfdeihgysapskaaqlmaglgflenqlrlnvesfSGGWRMRLNLART 162
Cdd:cd00267 60 GKDIAKLPLEELRRRIGYVPQL---------------------------------------------SGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
310-493 |
1.79e-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: 98.71 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 310 PLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASELL--NIGYF 379
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepiRDAREDYrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 AQHqmDALDGHASP--MLQL-ARIADKQISEATLRSFLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILD 455
Cdd:COG4133 81 GHA--DGLKPELTVreNLRFwAALYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALArLLLSPAP-LWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492309081 456 EPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASV 493
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-223 |
2.85e-23 |
|
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: 98.37 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 3 QFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPTGWT---VAHMAQEVKAL 76
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgKPLEKErkrIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 -DMP--AIDFVLSGdeefwdiqnklaqpdqltdfelakLHGRFDEIHGYSAPSKAAQLMA----GLGFLENQlrlNVESF 149
Cdd:cd03235 81 rDFPisVRDVVLMG------------------------LYGHKGLFRRLSKADKAKVDEAlervGLSELADR---QIGEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIeNQEL 223
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPktqEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
322-526 |
3.30e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 104.05 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPLLaGERKASELLNIGYFAQ------------------- 381
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKEFE-GEARPAPGIKVGYLPQepqldpektvrenveegva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HQMDALD-------GHASPMLQLARIADKQ-----ISEAT----LRSFLgsfgfsgER-M--------DTPCESFSGGER 436
Cdd:PRK11819 97 EVKAALDrfneiyaAYAEPDADFDALAAEQgelqeIIDAAdawdLDSQL-------EIaMdalrcppwDAKVTKLSGGER 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 437 ARLALALIVWQRPNVLILDEPTNHLDldmrhALSMA-----LQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEGd 511
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD-----AESVAwleqfLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEG- 243
|
250
....*....|....*..
gi 492309081 512 lqDYAKWL--REARQQQ 526
Cdd:PRK11819 244 --NYSSWLeqKAKRLAQ 258
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
4.05e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT------RPTGWTVAHMAQEVK 74
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 75 A-LDMPA--IDFVLSGdeefwdiqnklaqpdqltdfeLAKLHGRFdeiHGYSAPSKAA--QLMAGLGfLENQLRLNVESF 149
Cdd:COG1121 86 VdWDFPItvRDVVLMG---------------------RYGRRGLF---RRPSRADREAvdEALERVG-LEDLADRPIGEL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHI 218
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAateEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-220 |
6.33e-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: 97.15 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 3 QFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT----RPTGWTVAHMAQEVkal 76
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkDLTKLSLKELRRKV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 dmpaiDFVLsgdeefwdiQNklaqPD-QL-----TD---FELAKLHGRFDEIHgysapSKAAQLMAGLGfLENQLRLNVE 147
Cdd:cd03225 78 -----GLVF---------QN----PDdQFfgptvEEevaFGLENLGLPEEEIE-----ERVEEALELVG-LEGLRDRSPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
312-504 |
3.70e-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: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIA-EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELL-NIGY- 378
Cdd:COG1122 1 IELENLSFSYPGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkditkKNLRELRrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 --FAQHQM-------D-ALdghaSPM-LQLAR-IADKQISEAtlrsfLGSFGFSgERMDTPCESFSGGERARLALALIVW 446
Cdd:COG1122 81 fqNPDDQLfaptveeDvAF----GPEnLGLPReEIRERVEEA-----LELVGLE-HLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 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 |
4.24e-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: 94.84 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 314 LDNASIGYGDKQIA--EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqMDALDGHA 391
Cdd:cd03225 2 LKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL--------------VDGKDLTK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 392 SPMLQLARI-------ADKQISEATLRS---F-LGSFGFSGERM-----------------DTPCESFSGGERARLALAL 443
Cdd:cd03225 68 LSLKELRRKvglvfqnPDDQFFGPTVEEevaFgLENLGLPEEEIeerveealelvgleglrDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-209 |
6.24e-22 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 100.41 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFD--QVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKALDmP 79
Cdd:PRK11147 318 IVFEmeNVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD-P 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 ---AIDFVLSGDEEfwdiqnklaqpdqltdfelAKLHGRFDEIHGY-----SAPSKAaqlmaglgflenqlRLNVESFSG 151
Cdd:PRK11147 397 ektVMDNLAEGKQE-------------------VMVNGRPRHVLGYlqdflFHPKRA--------------MTPVKALSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHDRDFLD 209
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-177 |
7.30e-22 |
|
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: 92.33 E-value: 7.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRptgwtvahMAQEVKALDMPA----IDFVLSGDEEFwdiqn 96
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL--------DGQDLTDDERKSlrkeIGYVFQDPQLF----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 97 klaqpDQLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLG---FLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:pfam00005 72 -----PRLTVRENLRLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 492309081 174 EPTN 177
Cdd:pfam00005 147 EPTA 150
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-504 |
2.14e-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: 97.95 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGadegslTRPT-GWTVAHMA--QEVKALDM 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQ------YEPTsGRIIYHVAlcEKCGYVER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 79 PA-----------------IDFVLSGDEEFWDIQNKLAQPDQLT------DFELAKLHGRFDEIhGYSAPS---KAAQLM 132
Cdd:TIGR03269 75 PSkvgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfalygdDTVLDNVLEALEEI-GYEGKEavgRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 133 AGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-LDAIL---WLEDWLKAYEGTLILISHDRDFL 208
Cdd:TIGR03269 154 EMVQ-LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLvhnALEEAVKASGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 209 DAITDHILHIENQELTLytgnystfETTRSERLaqqqqafekqqetrahlQKFIDRFKA--KATKARQAQSRIKqlerMQ 286
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKE--------EGTPDEVV-----------------AVFMEGVSEveKECEVEVGEPIIK----VR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 287 QLAPAHVdtpftfsfreptkmssplltldnaSIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG 366
Cdd:TIGR03269 284 NVSKRYI------------------------SVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 367 E---RKASELLN---------------IGYFaqHQMDALDGHASPMLQLARIADKQISE--ATLRSF--LGSFGFSGER- 423
Cdd:TIGR03269 340 EvnvRVGDEWVDmtkpgpdgrgrakryIGIL--HQEYDLYPHRTVLDNLTEAIGLELPDelARMKAVitLKMVGFDEEKa 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 424 ---MDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDE 496
Cdd:TIGR03269 418 eeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
....*...
gi 492309081 497 LLLVHGGK 504
Cdd:TIGR03269 498 AALMRDGK 505
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
330-459 |
8.45e-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: 8.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----------RKASELLNIGYFAQHqmDALDGH-------- 390
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQD--PQLFPRltvrenlr 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 391 --ASPMLQLARIADKQISEAtlRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:pfam00005 82 lgLLLKGLSKREKDARAEEA--LEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-204 |
1.59e-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: 91.26 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP-TGWTVAHMAQEVkAL 76
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlASLSRRELARRI-AY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 dmpaidfvlsgdeefwdiqnkLAQ----PDQLTDFELAkLHGRFDEIHGYSAPSK-----AAQLMA--GLGFLENQlrlN 145
Cdd:COG1120 80 ---------------------VPQeppaPFGLTVRELV-ALGRYPHLGLFGRPSAedreaVEEALErtGLEHLADR---P 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 146 VESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EG-TLILISHD 204
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLareRGrTVVMVLHD 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-223 |
1.63e-20 |
|
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: 90.85 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGsltrptgwtvahmaqEVKALDMPA 80
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG---------------EVLVDGKDI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 idfvlsGDEEFWDI--------QNklaqPD-QLtdfelaklhgrF-----DEI------HGYS---APSKAAQLMAGLGf 137
Cdd:COG1122 66 ------TKKNLRELrrkvglvfQN----PDdQL-----------FaptveEDVafgpenLGLPreeIRERVEEALELVG- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 138 LENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFLDAITDH 214
Cdd:COG1122 124 LEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADR 203
|
....*....
gi 492309081 215 ILHIENQEL 223
Cdd:COG1122 204 VIVLDDGRI 212
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
312-504 |
1.82e-20 |
|
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: 91.41 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGE-----RKASELLNIGYFA 380
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvDLAGVdlhglSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 381 QHQMDALDGHASPMLQLARI-------ADKQISEATLRSFLGSFG---FSGERMDTpcesFSGGERARLALALIVWQRPN 450
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIphrslwaGDSPHDAAVVDRALARTElshLADRDMST----LSGGERQRVHVARALAQEPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 451 VLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVS-HERQLIASVCDELLLVHGGK 504
Cdd:TIGR03873 158 LLLLDEPTNHLDVRAQLETLALVRELaaTGVTVVAAlHDLNLAASYCDHVVVLDGGR 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
312-510 |
1.87e-20 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 89.94 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQItPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLN-IGYFAQ 381
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTiridgqdvlKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HQM--------DALDGHASpmlqLARIADKQISEATLRSfLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:cd03264 80 EFGvypnftvrEFLDYIAW----LKGIPSKEVKARVDEV-LELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 454 LDEPTNHLDLDMRHALSMALQDF-EGAVVLVS-HERQLIASVCDELLLVHGGKCTeFEG 510
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
282-507 |
2.21e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 95.22 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 282 LERMQQLAPAHVDTPFTFSFREPTkmSSPLLTLDNASIGY--GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG 359
Cdd:COG4987 306 ARRLNELLDAPPAVTEPAEPAPAP--GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 360 DLPLLAGE-----RKASELL------NIGYFAQhqmdalDGH--ASPMLQLARIADKQISEATLRSFLGSFGFSG----- 421
Cdd:COG4987 384 FLDPQSGSitlggVDLRDLDeddlrrRIAVVPQ------RPHlfDTTLRENLRLARPDATDEELWAALERVGLGDwlaal 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 422 -ERMDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsmaLQDFEGA-----VVLVSHERQLIA 491
Cdd:COG4987 458 pDGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEAlagrtVLLITHRLAGLE 534
|
250
....*....|....*.
gi 492309081 492 SVcDELLLVHGGKCTE 507
Cdd:COG4987 535 RM-DRILVLEDGRIVE 549
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-504 |
2.38e-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: 89.58 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLNIGYFAQHQmdALDGHA 391
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEitfdgksyqKNIEALRRIGALIEAP--GFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 392 SPMLQLARIAD-KQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD----LDMR 466
Cdd:cd03268 88 TARENLRLLARlLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgiKELR 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 492309081 467 hALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03268 167 -ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
309-507 |
4.76e-20 |
|
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: 93.81 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 309 SPLLTLDNASIGY--GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP---------LLAGE--RKASELL- 374
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdlLELSEALr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 --NIGYFAQHQMDALDG-----HASPMLQLARIADKQISEATLRSfLGSFGFsGERMDTPCESFSGGERARLALALIVWQ 447
Cdd:COG1123 82 grRIGMVFQDPMTQLNPvtvgdQIAEALENLGLSRAEARARVLEL-LEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 448 RPNVLILDEPTNHLDLDMRH---ALSMALQDFEG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAeilDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
312-504 |
9.80e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.89 E-value: 9.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQ--IAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqmdaLDG 389
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR-----------------LDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 390 HASpmlqlariadKQISEATLRSFLGSFG-----FSGERMDTpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLD 464
Cdd:cd03246 64 ADI----------SQWDPNELGDHVGYLPqddelFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492309081 465 MRHALSMALQDFEGA---VVLVSHERQLIASvCDELLLVHGGK 504
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
312-504 |
3.48e-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: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGD--KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkasellnIgyfaqhqmdALDG 389
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE--------I---------LIDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 390 HASPMLQLARIAdKQISEATLRSFLgsfgFSGermdTPCES-FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:cd03228 64 VDLRDLDLESLR-KNIAYVPQDPFL----FSG----TIRENiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 492309081 469 LSMALQDFEG--AVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:cd03228 135 ILEALRALAKgkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
7-216 |
4.66e-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: 87.18 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPTGWTVAHMAQEVKALDMPAIDfvls 86
Cdd:TIGR03873 7 VSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-LAGVDLHGLSRRARARRVALVE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 87 gdeefwdiQNKLAQPDqLTDFELAKLhGR--FDEIHGYSAPSKAAQLMAGLGF--LENQLRLNVESFSGGWRMRLNLART 162
Cdd:TIGR03873 82 --------QDSDTAVP-LTVRDVVAL-GRipHRSLWAGDSPHDAAVVDRALARteLSHLADRDMSTLSGGERQRVHVARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLK--AYEGTLILIS-HDRDFLDAITDHIL 216
Cdd:TIGR03873 152 LAQEPKLLLLDEPTNHLDVRAQLETLALVRelAATGVTVVAAlHDLNLAASYCDHVV 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
270-485 |
5.07e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 90.88 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 270 TKARQAQSRIKQLERMQQLAPAHVD-TPFTFSFREPTkmssplLTLDNASIGYGDKQIAEK-IRLQITPNSRIGLLGMNG 347
Cdd:TIGR02868 298 TRVRAAAERIVEVLDAAGPVAEGSApAAGAVGLGKPT------LELRDLSAGYPGAPPVLDgVSLDLPPGERVAILGPSG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 348 AGKSTLIKSLVGDLPLLAGE----------RKASELLN-IGYFAQhqmdalDGH--ASPMLQLARIADKQISEATLRSFL 414
Cdd:TIGR02868 372 SGKSTLLATLAGLLDPLQGEvtldgvpvssLDQDEVRRrVSVCAQ------DAHlfDTTVRENLRLARPDATDEELWAAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 415 GSFGFS------GERMDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA-LSMALQDFEG-AVVL 482
Cdd:TIGR02868 446 ERVGLAdwlralPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADElLEDLLAALSGrTVVL 525
|
...
gi 492309081 483 VSH 485
Cdd:TIGR02868 526 ITH 528
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
5.90e-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: 90.60 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRR--GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---------RPTGW--TVAH 68
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 69 MAQEVkaldmpaidFVLSGDeefwdIQN--KLAQPDqLTDFELAKlhgrfdeihgysapskAAQLmAGLGFLENQLR--L 144
Cdd:COG4987 414 VPQRP---------HLFDTT-----LREnlRLARPD-ATDEELWA----------------ALER-VGLGDWLAALPdgL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 145 NV------ESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIlwLEDWLKAYEG-TLILISHDRDFLDAItDH 214
Cdd:COG4987 462 DTwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQAL--LADLLEALAGrTVLLITHRLAGLERM-DR 538
|
250
....*....|
gi 492309081 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 ... |
2-215 |
7.13e-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: 85.35 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT-RPTGWTVAHMAQEVKA--LDM 78
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDGKSYQKNIEALRRIGalIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 79 PAIDFVLSGDEEFwdiqnKLaqpdqltdfeLAKLHGRFDEIHgysapskaAQLMAGLGfLENQLRLNVESFSGGWRMRLN 158
Cdd:cd03268 81 PGFYPNLTARENL-----RL----------LARLLGIRKKRI--------DEVLDVVG-LKDSAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
309-504 |
9.37e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.29 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 309 SPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP--------LLaGERKASELL-----N 375
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrLF-GERRGGEDVwelrkR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 376 IGYFAQHQMDALDGHASP----------MLQLAR-IADKQISEAtlRSFLGSFGFSgERMDTPCESFSGGERAR--LALA 442
Cdd:COG1119 80 IGLVSPALQLRFPRDETVldvvlsgffdSIGLYRePTDEQRERA--RELLELLGLA-HLADRPFGTLSQGEQRRvlIARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 443 LIvwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG--AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1119 157 LV--KDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
314-550 |
1.37e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 89.92 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 314 LDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSL---------------------VGD------------ 360
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkncqilhveqevVGDdttalqcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 361 ---LPLLAGE----RKASELLNIGYFAQHQMDALDGHASPML--QLARI------ADKQISEATLRSFLGSFGFSGERMD 425
Cdd:PLN03073 260 ierTQLLEEEaqlvAQQRELEFETETGKGKGANKDGVDKDAVsqRLEEIykrlelIDAYTAEARAASILAGLSFTPEMQV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 426 TPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 492309081 506 TEFEGDLQDYAKwlreARQQQINAQTAVAQNNSSSAAPAPAKVDK 550
Cdd:PLN03073 420 VTYKGDYDTFER----TREEQLKNQQKAFESNERSRSHMQAFIDK 460
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-219 |
2.21e-18 |
|
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: 84.41 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 11 RGGRVL--FQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS--LTRPTGWT-VAHmAQEVKALDM------- 78
Cdd:COG4778 19 QGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGWVdLAQ-ASPREILALrrrtigy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 79 -----------PAIDFVlsgdeefwdiqnklAQP--DQLTDFELAKlhgrfdeihgysapSKAAQLMAglgflenqlRLN 145
Cdd:COG4778 98 vsqflrviprvSALDVV--------------AEPllERGVDREEAR--------------ARARELLA---------RLN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 146 VES---------FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAyEGTLIL-ISHDRDFLDAIT 212
Cdd:COG4778 141 LPErlwdlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKA-RGTAIIgIFHDEEVREAVA 219
|
....*..
gi 492309081 213 DHILHIE 219
Cdd:COG4778 220 DRVVDVT 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
309-505 |
4.33e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.40 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 309 SPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQ--HQMDA 386
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 387 LDGHASPMLQL-ARIADKQISEATLRSflgsfgFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:PRK09544 82 LPLTVNRFLRLrPGTKKEDILPALKRV------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 466 RHAL----SMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PRK09544 156 QVALydliDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHIC 199
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
4.73e-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: 82.10 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSltrptgwtvahmaqevkaldmpaidfV 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE--------------------------I 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 85 LSGDEEFWDIQNKlaqpdqltdfELAKLhgrfdeIhGYsapskAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLM 164
Cdd:cd03214 57 LLDGKDLASLSPK----------ELARK------I-AY-----VPQALELLG-LAHLADRPFNELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 165 SRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
5.80e-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: 87.51 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRR-GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrptgwTVAHmaQEVKALDMPA 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI------LING--VDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLSgdeefWDIQN------------KLAQPDqLTDFEL---AKLHGRFDEIhgysapskaAQLMAGLGFL--ENQLR 143
Cdd:COG4988 409 WRRQIA-----WVPQNpylfagtirenlRLGRPD-ASDEELeaaLEAAGLDEFV---------AALPDGLDTPlgEGGRG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 144 LnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD--AILW--LEDWLKAYegTLILISHDRDFLDAItDHILHIE 219
Cdd:COG4988 474 L-----SGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKGR--TVILITHRLALLAQA-DRILVLD 545
|
....*
gi 492309081 220 NQELT 224
Cdd:COG4988 546 DGRIV 550
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
310-505 |
6.00e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 310 PLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGER----------KASEL-LNIGY 378
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwSPAELaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 FAQH-------------QMDALDgHASPMLQLARIADKQISEATL-----RSFLgsfgfsgermdtpceSFSGGERARLA 440
Cdd:PRK13548 81 LPQHsslsfpftveevvAMGRAP-HGLSRAEDDALVAAALAQVDLahlagRDYP---------------QLSGGEQQRVQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 441 LALI---VWQ---RPNVLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:PRK13548 145 LARVlaqLWEpdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
314-514 |
6.46e-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: 83.32 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 314 LDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASE------LLNIGYF 379
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgediSGLSEaelyrlRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 AQH-----QMDALDGHASPMLQLARIADKQISEATlRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLIL 454
Cdd:cd03261 83 FQSgalfdSLTVFENVAFPLREHTRLSEEEIREIV-LEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 455 DEPTNHLD---LDMRHALSMALQDFEGA-VVLVSHERQLIASVCDELLLVHGGKcTEFEGDLQD 514
Cdd:cd03261 161 DEPTAGLDpiaSGVIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGK-IVAEGTPEE 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-462 |
6.84e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 86.99 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSL----GADEGSLTRPTGWTVAHMAQEVkal 76
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELpllsGERQSQFSHITRLSFEQLQKLV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 dmpaidfvlsgDEEFWDIQNKLAQPDQlTDFelaklhGRFD-EI--HGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGW 153
Cdd:PRK10938 80 -----------SDEWQRNNTDMLSPGE-DDT------GRTTaEIiqDEVKDPARCEQLAQQFG-ITALLDRRFKYLSTGE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 154 RMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG---TLILISHDRDFLDAITDHILHIENQELTLyTGny 230
Cdd:PRK10938 141 TRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLAE-TG-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 231 stfetTRSERLaqqqqafekqqetrahlqkfidrfkakatkarqAQSRIKQLERMQQLAPAHVDTPFTFSFREPTKMSSP 310
Cdd:PRK10938 218 -----EREEIL---------------------------------QQALVAQLAHSEQLEGVQLPEPDEPSARHALPANEP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP-------LLAGERKAS-ELL-----NIG 377
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgysndlTLFGRRRGSgETIwdikkHIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFA-QHQMD----------ALDGHASPMLQLARIADKQISEAtlRSFLGSFGFSGERMDTPCESFSGGERaRLAL---AL 443
Cdd:PRK10938 340 YVSsSLHLDyrvstsvrnvILSGFFDSIGIYQAVSDRQQKLA--QQWLDILGIDKRTADAPFHSLSWGQQ-RLALivrAL 416
|
490
....*....|....*....
gi 492309081 444 IvwQRPNVLILDEPTNHLD 462
Cdd:PRK10938 417 V--KHPTLLILDEPLQGLD 433
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
341-504 |
6.91e-18 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 82.94 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 341 GLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLNIGYFAQHqmDALDGHASPM--LQL-ARIadKQISE 407
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPTSGTayingysirtDRKAARQSLGYCPQF--DALFDELTVRehLRFyARL--KGLPK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 408 ATLRS----FLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVV 481
Cdd:cd03263 108 SEIKEevelLLRVLGLTDKA-NKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSII 186
|
170 180
....*....|....*....|...
gi 492309081 482 LVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03263 187 LTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
312-510 |
8.35e-18 |
|
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: 81.59 E-value: 8.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYG--DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkasellnigyfaqhqmdALDG 389
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----------------TLDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 390 HasPMLQLARIADKQISEATLRSFLgsfgFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD-LDMRHA 468
Cdd:cd03247 64 V--PVSDLEKALSSLISVLNQRPYL----FDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492309081 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 |
1.34e-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: 81.94 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkasellnigYFAQHQMDALDGH- 390
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV---------LFDGKPLDIAARNr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 ----------------ASPMLQLARIADKQISEA--TLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVL 452
Cdd:cd03269 72 igylpeerglypkmkvIDQLVYLAQLKGLKKEEArrRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 453 ILDEPTNHLD-LDMRHALS--MALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03269 151 ILDEPFSGLDpVNVELLKDviRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
1.77e-17 |
|
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: 81.65 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPTGWTVAHMAQEVKAldmpAI 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-VAGHDVVREPREVRR----RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 DFVLSgdeefwdiqnKLAQPDQLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGFLENQLRLnVESFSGGWRMRLNLAR 161
Cdd:cd03265 76 GIVFQ----------DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 162 TLMSRSDLLLLDEPTNHLDLDAI--LW--LEDWLKAYEGTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
311-504 |
2.31e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.09 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERkasellnigYFAQHQMDALDGH 390
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEV---------RLNGRPLAAWSPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 aspmlQLARI--------------------------------ADKQISEATLrsflgsfgfsgERMDtpCESF------- 431
Cdd:COG4559 72 -----ELARRravlpqhsslafpftveevvalgraphgssaaQDRQIVREAL-----------ALVG--LAHLagrsyqt 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 432 -SGGERAR--LALALI-VWQ----RPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASVCDELLLV 500
Cdd:COG4559 134 lSGGEQQRvqLARVLAqLWEpvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLL 213
|
....
gi 492309081 501 HGGK 504
Cdd:COG4559 214 HQGR 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
311-508 |
2.59e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 81.40 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEK----IRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERKASE 372
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalddVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiifdgkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 373 LLNIGYFAQHQMDALD-----GH--ASPML-QLARIADKQISEATLRSFLGsFGFSGERMDT-PCEsFSGGERAR--LAL 441
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprmtiGEqiAEPLRiHGKLSKKEARKEAVLLLLVG-VGLPEEVLNRyPHE-LSGGQRQRvaIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 442 ALIVwqRPNVLILDEPTNHLDLDMRH---ALSMALQD-FEGAVVLVSHERQLIASVCDELLLVHGGKCTEF 508
Cdd:cd03257 159 ALAL--NPKLLIADEPTSALDVSVQAqilDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-220 |
2.76e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 79.73 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGR--VLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahmaqevkaldmp 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 aidfvlsgdeefWDIQNklaqpdqLTDFELAKLHGRFdeihGYsAPSKAaQLMAGLgflenqLRLNVesFSGGWRMRLNL 159
Cdd:cd03228 61 ------------IDGVD-------LRDLDLESLRKNI----AY-VPQDP-FLFSGT------IRENI--LSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 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 ... |
313-504 |
4.49e-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: 79.99 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 313 TLDNASIGYGDKQ-IAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-------RKASELL-NIGYFAQHQ 383
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpIKAKERRkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 384 MDALDGhASPMLQLaRIADKQISE--ATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03226 81 DYQLFT-DSVREEL-LLGLKELDAgnEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 462 DLdmRHALSMA-----LQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03226 158 DY--KNMERVGelireLAAQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
311-522 |
5.26e-17 |
|
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: 81.00 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYG----DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----RKASELLNIGYFAQ 381
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HQMDALDGHAS--PMLQLA-------RIADKQISEATLRSFLGSFGFSGERMD-TPcESFSGGERARLAL--ALIVwqRP 449
Cdd:COG1124 81 VQMVFQDPYASlhPRHTVDrilaeplRIHGLPDREERIAELLEQVGLPPSFLDrYP-HQLSGGQRQRVAIarALIL--EP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 450 NVLILDEPTNHLDLDMR----HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE-------FEGDLQDYAKW 518
Cdd:COG1124 158 ELLLLDEPTSALDVSVQaeilNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEeltvadlLAGPKHPYTRE 237
|
....
gi 492309081 519 LREA 522
Cdd:COG1124 238 LLAA 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
1.12e-16 |
|
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: 80.08 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP-TGWTVAHMA------ 70
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgRDiTGLPPHRIArlgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 71 --QEVKAL-DMPAIDFVLSGdeefwdIQNKLAQPDQLTDFELAKLHGRFDEIHgysapSKAAQLMAGLGfLENQLRLNVE 147
Cdd:COG0411 84 tfQNPRLFpELTVLENVLVA------AHARLGRGLLAALLRLPRARREEREAR-----ERAEELLERVG-LADRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPT---NHLDLDAILWLEDWLKAYEG-TLILISHDRDFLDAITDHIL 216
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
312-504 |
1.14e-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: 79.10 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLNIGYFAQH 382
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 -----QMDALDGHASPmLQLARIADKQISEATLRSfLGSFGFSGERMDTPcESFSGGERARLALA--LIVwqRPNVLILD 455
Cdd:cd03259 81 yalfpHLTVAENIAFG-LKLRGVPKAEIRARVREL-LELVGLEGLLNRYP-HELSGGQQQRVALAraLAR--EPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492309081 456 EPTNHLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03259 156 EPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
302-507 |
1.50e-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: 83.27 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 302 REPTKMSSPLLTLDNASIGYGD-KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyFA 380
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL---------IN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 381 QHQMDALDgHASPMLQLA-----------------RIADKQISEATLRSFLGSFGFSG------ERMDTPCES----FSG 433
Cdd:COG4988 398 GVDLSDLD-PASWRRQIAwvpqnpylfagtirenlRLGRPDASDEELEAALEAAGLDEfvaalpDGLDTPLGEggrgLSG 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 434 GERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEG-AVVLVSHERQLIASvCDELLLVHGGKCTE 507
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGrTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
312-504 |
1.58e-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: 78.79 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIA--EKIRLQITPNSRIGLLGMNGAGKSTLIKslvgdlpLLAGERKASE---LL------------ 374
Cdd:cd03245 3 IEFRNVSFSYPNQEIPalDNVSLTIRAGEKVAIIGRVGSGKSTLLK-------LLAGLYKPTSgsvLLdgtdirqldpad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 ---NIGYFAQHQM-------DALdghaspMLQLARIADKQISEATLRSFLGSF------GFS---GERMDtpceSFSGGE 435
Cdd:cd03245 76 lrrNIGYVPQDVTlfygtlrDNI------TLGAPLADDERILRAAELAGVTDFvnkhpnGLDlqiGERGR----GLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHeRQLIASVCDELLLVHGGK 504
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGR 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
312-504 |
2.33e-16 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 82.96 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIA--EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------------RKasel 373
Cdd:COG2274 474 IELENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRilidgidlrqidpaslRR---- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 374 lNIGYFAQHqmDAL------------DGHASP--MLQLARIAdkQISEATLR------SFLGSFGfsgermdtpcESFSG 433
Cdd:COG2274 550 -QIGVVLQD--VFLfsgtirenitlgDPDATDeeIIEAARLA--GLHDFIEAlpmgydTVVGEGG----------SNLSG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 434 GERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL-ADRIIVLDKGR 686
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
2.81e-16 |
|
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: 78.97 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTlfaaLLGSLGADEgsltRPTGwtvahmAQEVKALDMPA 80
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDL----PPTY------GNDVRLFGERR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 idfvlsGDEEFWDIQNKL-----AQPDQLTDFELAK---LHGRFDEIHGYSAPS-----KAAQLMAGLGF--LENQLrln 145
Cdd:COG1119 69 ------GGEDVWELRKRIglvspALQLRFPRDETVLdvvLSGFFDSIGLYREPTdeqreRARELLELLGLahLADRP--- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 146 VESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK--AYEG--TLILISHDRDFLDAITDHILHIEN 220
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDklAAEGapTLVLVTHHVEEIPPGITHVLLLKD 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
320-499 |
2.82e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.27 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 320 GYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQmdALD----------- 388
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRS--EVPdslpltvrdlv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 -----GHASPMLQLARIADKQISEATLRsfLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDL 463
Cdd:NF040873 79 amgrwARRGLWRRLTRDDRAAVDDALER--VGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 492309081 464 DMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLL 499
Cdd:NF040873 153 ESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
312-508 |
4.10e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 77.99 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELL----------------- 374
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLldgkdiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 -NIGYFAQH----QMDALDGHASPmLQLARIADKQISEATLRSFLGSFGFSGERMD-TPCESFSGGERARLALA--LIVw 446
Cdd:cd03260 81 rRVGMVFQKpnpfPGSIYDNVAYG-LRLHGIKLKEELDERVEEALRKAALWDEVKDrLHALGLSGGQQQRLCLAraLAN- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 447 qRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVCDELLLVHGGKCTEF 508
Cdd:cd03260 159 -EPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
4.93e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 77.30 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 7 VSLRRGGRVLfQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKALDMPAIDFVLS 86
Cdd:cd03226 7 FSYKKGTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 87 GD---EEFwDIQNKLAqpdqltdfelaklhgrfdeihgYSAPSKAAQLMAGLGFLENQLRlNVESFSGGWRMRLNLARTL 163
Cdd:cd03226 86 TDsvrEEL-LLGLKEL----------------------DAGNEQAETVLKDLDLYALKER-HPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 164 MSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-502 |
5.25e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 26 PGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGW------------------------TVAHMAQEV----KALD 77
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWdevlkrfrgtelqnyfkklyngeiKVVHKPQYVdlipKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 MPAIDFVLSGDEefwdiqnklaqpdqltdfelaklHGRFDEIhgysapskAAQLmaglgFLENQLRLNVESFSGGWRMRL 157
Cdd:PRK13409 178 GKVRELLKKVDE-----------------------RGKLDEV--------VERL-----GLENILDRDISELSGGELQRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 158 NLARTLMSRSDLLLLDEPTNHLDL-------DAILWLedwlkAYEGTLILISHDRDFLDAITDHIlHIenqeltLY--TG 228
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIREL-----AEGKYVLVVEHDLAVLDYLADNV-HI------AYgePG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 229 NYSTFETTRSerlaqqqqafekqqeTRAHLQKFIDRFkakatkARQAQSRIKqlermqqlapahvDTPFTFSFREPT--K 306
Cdd:PRK13409 290 AYGVVSKPKG---------------VRVGINEYLKGY------LPEENMRIR-------------PEPIEFEERPPRdeS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDkqiaekIRL-----QITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASelLNIGYFAQ 381
Cdd:PRK13409 336 ERETLVEYPDLTKKLGD------FSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISYKPQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HQMDALDGHASPMLqlariadKQISEATLRSFLGS---FGFSGER-MDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:PRK13409 408 YIKPDYDGTVEDLL-------RSITDDLGSSYYKSeiiKPLQLERlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 492309081 458 TNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHG 502
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
321-504 |
1.56e-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: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELL-NIGYFAQHQM--DALD 388
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvREPREVRrRIGIVFQDLSvdDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 GHASpMLQLARIADKQISEATLR--SFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:cd03265 90 GWEN-LYIHARLYGVPGAERRERidELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492309081 467 HAL----SMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03265 168 AHVweyiEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGR 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
316-507 |
1.79e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 76.28 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKS------------LVGDLPLLAGERKASEL-LNIGYFAQH 382
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCinkleeitsgdlIVDGLKVNDPKVDERLIrQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 -----QMDALDGHASPMLQLaRIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:PRK09493 86 fylfpHLTALENVMFGPLRV-RGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492309081 458 TNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
310-506 |
2.63e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 310 PLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkaselLNIGYFAQHQMDA--L 387
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT------VLVAGDDVEALSAraA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 388 DGHASPMLQLARIA----DKQISEATLRSFLGSFGFSGER-----------------MDTPCESFSGGERARLALALIVW 446
Cdd:PRK09536 76 SRRVASVPQDTSLSfefdVRQVVEMGRTPHRSRFDTWTETdraaveramertgvaqfADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 447 QRPNVLILDEPTNHLDLDmrHA-----LSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK09536 156 QATPVLLLDEPTASLDIN--HQvrtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-223 |
2.64e-15 |
|
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: 74.17 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALDMp 79
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG--------LLRPTSGRVRLDGADISQWDP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 aidfvlsgdEEFWDIQNKLAQPDQLTDFELAklhgrfDEIhgysapskaaqlmaglgflenqlrlnvesFSGGWRMRLNL 159
Cdd:cd03246 72 ---------NELGDHVGYLPQDDELFSGSIA------ENI-----------------------------LSGGQRQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLdAITDHILHIENQEL 223
Cdd:cd03246 108 ARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
320-523 |
2.83e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 320 GYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----RKASeLLNIG-------------YF-- 379
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRvevngRVSA-LLELGagfhpeltgreniYLng 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 -----AQHQMDALdghaspmlqLARIADkqiseatlrsflgsfgFS--GERMDTPCESFSGGERARLALALIVWQRPNVL 452
Cdd:COG1134 114 rllglSRKEIDEK---------FDEIVE----------------FAelGDFIDQPVKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 453 ILDEptnhldldmrhALS-----------MALQDF---EGAVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD---- 514
Cdd:COG1134 169 LVDE-----------VLAvgdaafqkkclARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD-GDPEEviaa 236
|
....*....
gi 492309081 515 YAKWLREAR 523
Cdd:COG1134 237 YEALLAGRE 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
300-509 |
3.16e-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: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 300 SFREPTKMSSPLLTLDNAS--IGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----RKASEL 373
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvtvrGRVSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 374 LNIGYFaqhqmdaLDGHAS---------PMLQLARIADKQISEATLrsflgsfGFS--GERMDTPCESFSGGERARLALA 442
Cdd:cd03220 89 LGLGGG-------FNPELTgreniylngRLLGLSRKEIDEKIDEII-------EFSelGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 443 LIVWQRPNVLILDEPTNHLDLD--------MRHALSMAlqdfeGAVVLVSHERQLIASVCDELLLVHGGKCTEFE 509
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAfqekcqrrLRELLKQG-----KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-220 |
4.19e-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: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRG----GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKAL 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG--------LERPWSGEVTFDGRPVTRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DMPA----IDFVlsgdeeFWD----------IQNKLAQPdqltdfelAKLHGRFDeihgysAPSKAAQLMAGLGFLENQL 142
Cdd:COG1124 73 RRKAfrrrVQMV------FQDpyaslhprhtVDRILAEP--------LRIHGLPD------REERIAELLEQVGLPPSFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 143 RLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHI 218
Cdd:COG1124 133 DRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqAEILNLLKDLREERGlTYLFVSHDLAVVAHLCDRVAVM 212
|
..
gi 492309081 219 EN 220
Cdd:COG1124 213 QN 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
321-504 |
4.43e-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: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDL-P---------LLAGERKASELLNIGY-FAQHQ-----M 384
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPtsgevrvagLVPWKRRKKFLRRIGVvFGQKTqlwwdL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 385 DALDGHAspmlQLARIADkqISEATLRSFLGsfGFS-----GERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:cd03267 111 PVIDSFY----LLAAIYD--LPPARFKKRLD--ELSelldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492309081 460 HLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03267 183 GLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
272-525 |
4.59e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 78.25 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 272 ARQAQSRIKQLERMQQLAPAHVDTPftfsfrEPTkmssPLLTLDNASIGY--GDKQIAEKIRLQITPNSRIGLLGMNGAG 349
Cdd:COG4618 301 ARQAYRRLNELLAAVPAEPERMPLP------RPK----GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 350 KSTLIKSLVGDLPLLAGE---------RKASELL--NIGYFAQH-------------QMDALDGHAspMLQLARIADkqI 405
Cdd:COG4618 371 KSTLARLLVGVWPPTAGSvrldgadlsQWDREELgrHIGYLPQDvelfdgtiaeniaRFGDADPEK--VVAAAKLAG--V 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 406 SEATLR------SFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--E 477
Cdd:COG4618 447 HEMILRlpdgydTRIGEGGAR----------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaR 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 492309081 478 GA-VVLVSHERQLIAsVCDELLLVHGGKCTEFeGDLQDYAKWLREARQQ 525
Cdd:COG4618 517 GAtVVVITHRPSLLA-AVDKLLVLRDGRVQAF-GPRDEVLARLARPAAA 563
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
311-510 |
5.59e-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: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDK----QIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERKASELlnigyfaqhqmDA 386
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG---LLEPDAGFATV-----------DG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 387 LDGHASPMLQLARIA---------DKQISEATLRSFLGSFGFSG-----------------ERMDTPCESFSGGERARLA 440
Cdd:cd03266 67 FDVVKEPAEARRRLGfvsdstglyDRLTARENLEYFAGLYGLKGdeltarleeladrlgmeELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 441 LALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKcTEFEG 510
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTHIMQEVERLCDRVVVLHRGR-VVYEG 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
5.81e-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: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLR----RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPTGWTVAHMAQEVKAl 76
Cdd:cd03266 1 MITADALTKRfrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT-VDGFDVVKEPAEARR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 dmpAIDFVLSGDEEFwdiqnklaqpDQLTDFELAKLHGRFdeiHGYsapsKAAQLMAGLGFLENQLRLN------VESFS 150
Cdd:cd03266 79 ---RLGFVSDSTGLY----------DRLTARENLEYFAGL---YGL----KGDELTARLEELADRLGMEelldrrVGGFS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHI 215
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGKCILFStHIMQEVERLCDRV 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
312-504 |
6.19e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERK----------ASELL-NIGYFA 380
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlsSRQLArRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 381 QHQMdALDGHA---------SPMLQL-ARIA--DKQISE-ATLRSFLGSFGfsgermDTPCESFSGGERARLALALIVWQ 447
Cdd:PRK11231 83 QHHL-TPEGITvrelvaygrSPWLSLwGRLSaeDNARVNqAMEQTRINHLA------DRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 448 RPNVLILDEPTNHLDLD-----MRhaLSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINhqvelMR--LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
312-458 |
8.43e-15 |
|
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: 74.01 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLN---IGYF 379
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrditGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 AQHQMdaLDGHASPM--LQL-ARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDE 456
Cdd:cd03224 81 PEGRR--IFPELTVEenLLLgAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
..
gi 492309081 457 PT 458
Cdd:cd03224 159 PS 160
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-206 |
1.13e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.65 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQevkaldmpaidfvlsgdeef 91
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 92 wdiqnKLAQPDQL--TDFELAKLhGRFDEI-----HGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLM 164
Cdd:NF040873 63 -----RSEVPDSLplTVRDLVAM-GRWARRglwrrLTRDDRAAVDDALERVG-LADLAGRQLGELSGGQRQRALLAQGLA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492309081 165 SRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG---TLILISHDRD 206
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-507 |
1.16e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.31 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 323 DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASEllNIGYFAQH--QMDAL------------- 387
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDifQIDAIklrkevgmvfqqp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 388 ---------DGHASPmLQLARIADK----QISEATLRSfLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:PRK14246 100 npfphlsiyDNIAYP-LKSHGIKEKreikKIVEECLRK-VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 455 DEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-204 |
1.22e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.02 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwTVAHMAQEVKALDMPAIDFVLSGDEEF 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT-----LDGVPVSSLDQDEVRRRVSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 92 WD---IQN-KLAQPDqLTDFELAKLHGRFD-EIHGYSAPSKAAQLMAGLGflenqlrlnvESFSGGWRMRLNLARTLMSR 166
Cdd:TIGR02868 421 FDttvRENlRLARPD-ATDEELWAALERVGlADWLRALPDGLDTVLGEGG----------ARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492309081 167 SDLLLLDEPTNHLDLDAIL-WLEDWLKAYEG-TLILISHD 204
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-502 |
1.26e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.13 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 30 IGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWtvahmaQEVkaldmpaIDFvLSGDE---EFWDIQN---KLAQPDQ 103
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPSW------DEV-------LKR-FRGTElqdYFKKLANgeiKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 104 LTDF----------ELAKlhgRFDEiHGysapsKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:COG1245 168 YVDLipkvfkgtvrELLE---KVDE-RG-----KLDELAEKLG-LENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 174 EPTNHLDL-------DAILWLEDWLKAyegtLILISHDRDFLDAITDHIlHIenqeltLY--TGNYSTFETTRSerlaqq 244
Cdd:COG1245 238 EPSSYLDIyqrlnvaRLIRELAEEGKY----VLVVEHDLAILDYLADYV-HI------LYgePGVYGVVSKPKS------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 245 qqafekqqeTRAHLQKFID--------RFKakatkarqaqsrikqlermqqlapahvDTPFTFSFREPT--KMSSPLLTL 314
Cdd:COG1245 301 ---------VRVGINQYLDgylpeenvRIR---------------------------DEPIEFEVHAPRreKEEETLVEY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 315 DNASIGYGDkqiaekIRL-----QITPNSRIGLLGMNGAGKSTLIKslvgdlpLLAGERKASE-----LLNIGYFAQH-- 382
Cdd:COG1245 345 PDLTKSYGG------FSLeveggEIREGEVLGIVGPNGIGKTTFAK-------ILAGVLKPDEgevdeDLKISYKPQYis 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 ------QMDALDGHASPM-------------LQLARIADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALAL 443
Cdd:COG1245 412 pdydgtVEEFLRSANTDDfgssyykteiikpLGLEKLLDKNVKD-----------------------LSGGELQRVAIAA 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLV-SHERQLIASVCDELLLVHG 502
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenRGKTAMVvDHDIYLIDYISDRLMVFEG 531
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-218 |
1.55e-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: 76.56 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahmaqeVKALDMPA 80
Cdd:TIGR02857 322 LEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA-------------VNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLSGDEEFWDIQNKLAQPDQLTD-FELAKLHGRFDEIHGYSAPSKAAQLMAGLGF-LENQLRLNVESFSGGWRMRLN 158
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAEnIRLARPDASDAEIREALERAGLDEFVAALPQgLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 159 LARTLMSRSDLLLLDEPTNHLDLD-AILWLEDWLKAYEG-TLILISHDRDFLdAITDHILHI 218
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAEtEAEVLEALRALAQGrTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-504 |
1.80e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 302 REPTKMSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKAS 371
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgvpvpaRARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 372 ELLNIGYFAqhQMDALDGHASPMLQLA------RIADKQIsEATLRSFLgSFGFSGERMDTPCESFSGGERARLALALIV 445
Cdd:PRK13536 112 ARARIGVVP--QFDNLDLEFTVRENLLvfgryfGMSTREI-EAVIPSLL-EFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 446 WQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLArgkTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-220 |
2.82e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPTGWTVAHMAQEVKALdm 78
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgEPVPSRARHARQRVGVV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 79 PAIDFVlsgDEEFWDIQNKLaqpdqltdfelakLHGRFdeiHGYSAPSKAAQLMAGLGF--LENQLRLNVESFSGGWRMR 156
Cdd:PRK13537 86 PQFDNL---DPDFTVRENLL-------------VFGRY---FGLSAAAARALVPPLLEFakLENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 157 LNLARTLMSRSDLLLLDEPTNHLDLDA--ILW--LEDWLkAYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
10-216 |
3.00e-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: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 10 RRGGRVL--FQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-LTRPTG-WT--VAHMAQEVKALDMPAIDF 83
Cdd:TIGR02324 15 QQGGVRLpvLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRiLVRHEGaWVdlAQASPREVLEVRRKTIGY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 84 VlsgdEEFWDIQNKLAQPDQLTdfELAKLHGRFDEIhgysAPSKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTL 163
Cdd:TIGR02324 95 V----SQFLRVIPRVSALEVVA--EPLLERGVPREA----ARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 164 MSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:TIGR02324 165 IADYPILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVADRVM 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
312-504 |
4.06e-14 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 70.68 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-----------DLPLLAGERKASELL--NIGY 378
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleepdsgsiliDGEDLTDLEDELPPLrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 -FAQHQ----MDALDGHASPMlqlariadkqiseatlrsflgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLI 453
Cdd:cd03229 81 vFQDFAlfphLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 454 LDEPTNHLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-220 |
5.04e-14 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 75.26 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR--RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---------RPTGWT--VAH 68
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASLRrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 69 MAQEVK----------ALDMPAIDfvlsgDEEFWDIqnklaqpdqltdFELAKLHgrfDEIhgysapskaAQLMAGLgfl 138
Cdd:COG2274 554 VLQDVFlfsgtireniTLGDPDAT-----DEEIIEA------------ARLAGLH---DFI---------EALPMGY--- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 139 ENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAIL-WLEDWlkayegTLILISHDRDFLdA 210
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDaeteaiiLENLRrLLKGR------TVIIIAHRLSTI-R 674
|
250
....*....|
gi 492309081 211 ITDHILHIEN 220
Cdd:COG2274 675 LADRIIVLDK 684
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
307-514 |
5.17e-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: 71.93 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER----KASEL--- 373
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpdsgeiLVDGQDitglSEKELyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 374 -LNIGY-FaqhQMDAL-------DGHASPMLQLARIADKQISEATLRSfLGSFGFSG--ERMdtPCEsFSGGERARLALA 442
Cdd:COG1127 81 rRRIGMlF---QGGALfdsltvfENVAFPLREHTDLSEAEIRELVLEK-LELVGLPGaaDKM--PSE-LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 443 --LIVwqRPNVLILDEPT-----------NHLDLDMRHALSMalqdfegAVVLVSHERQLIASVCDELLLVHGGKCtEFE 509
Cdd:COG1127 154 raLAL--DPEILLYDEPTagldpitsaviDELIRELRDELGL-------TSVVVTHDLDSAFAIADRVAVLADGKI-IAE 223
|
....*
gi 492309081 510 GDLQD 514
Cdd:COG1127 224 GTPEE 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
320-505 |
6.00e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 70.66 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 320 GYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERKASELLnigyfaqhqmdaLDGHASPMLQLAR 399
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG---RRTGLGVSGEVL------------INGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 400 IA------DKQISEATLRSFLGsfgFSGErmdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL 473
Cdd:cd03213 83 IIgyvpqdDILHPTLTVRETLM---FAAK-----LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 492309081 474 QDF--EGAVVLVS-HE-RQLIASVCDELLLVHGGKC 505
Cdd:cd03213 155 RRLadTGRTIICSiHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
307-504 |
6.47e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG----------ERKASELLNI 376
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgepvpSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GYFAQhqMDALDghaspmlqlariADKQISEaTLRSFLGSFGFSG-----------------ERMDTPCESFSGGERARL 439
Cdd:PRK13537 83 GVVPQ--FDNLD------------PDFTVRE-NLLVFGRYFGLSAaaaralvppllefakleNKADAKVGELSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA---VVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgktILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-181 |
9.20e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 71.73 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP-TGWTVAHMAQevkal 76
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngRPlADWSPAELAR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 dMPAIdfvlsgdeefwdiqnkLAQPDQLT-DF------ELAKLHGRFDEIHGYSAPSKAAQLmAGLGFLENQLRLnveSF 149
Cdd:PRK13548 77 -RRAV----------------LPQHSSLSfPFtveevvAMGRAPHGLSRAEDDALVAAALAQ-VDLAHLAGRDYP---QL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 492309081 150 SGGWRMRLNLARTLMSRSD------LLLLDEPTNHLDL 181
Cdd:PRK13548 136 SGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDL 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-220 |
1.39e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 70.31 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS---------------LTRPTGW 64
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSvlldgtdirqldpadLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 65 tvahMAQEVK----------ALDMPAIDfvlsgDEEFWDIQNKLAqpdqLTDFelAKLHGrfdeiHGYsapskaaqlmag 134
Cdd:cd03245 83 ----VPQDVTlfygtlrdniTLGAPLAD-----DERILRAAELAG----VTDF--VNKHP-----NGL------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 135 lgflENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG--TLILISHDRDFLDaIT 212
Cdd:cd03245 131 ----DLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD-LV 205
|
....*...
gi 492309081 213 DHILHIEN 220
Cdd:cd03245 206 DRIIVMDS 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
1.66e-13 |
|
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: 70.23 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKAL 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF-DGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DMPAIDFVlsgdeeFWDIQNKLaQP-----DQLTdfELAKLHGRfdeIHGYSAPSKAA-QLMAGLGFLENQLRLNVESFS 150
Cdd:cd03257 80 RRKEIQMV------FQDPMSSL-NPrmtigEQIA--EPLRIHGK---LSKKEARKEAVlLLLVGVGLPEEVLNRYPHELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKA-YEGTLILISHDRDFLDAITDHIL 216
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVA 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
2.26e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 69.70 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtVAHmaQEVKAL--- 76
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL------VNG--QDLSRLkrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DMPA----IDFVLsgdeefwdiqnklaqpdQltDFELakLHGR--FD------EIHGYSAPSKAAQLMAGL---GfLENQ 141
Cdd:COG2884 73 EIPYlrrrIGVVF-----------------Q--DFRL--LPDRtvYEnvalplRVTGKSRKEIRRRVREVLdlvG-LSDK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 142 LRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILI-SHDRDFLDAITDHILHI 218
Cdd:COG2884 131 AKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGTTVLIaTHDLELVDRMPKRVLEL 210
|
....*.
gi 492309081 219 ENQELT 224
Cdd:COG2884 211 EDGRLV 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
332-504 |
2.55e-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: 69.77 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 332 LQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGE----RKASEL--LNIGYFAQH-----QMDALD------ 388
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRptsgsvLFDGEditgLPPHEIarLGIGRTFQIprlfpELTVLEnvmvaa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 --GHASPMLQLARIADKQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:cd03219 101 qaRTGSGLLLARARREEREARERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492309081 467 HALS---MALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03219 180 EELAeliRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
307-504 |
2.61e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.67 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----RKASELL----NIG 377
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRilldgRDVTGLPpekrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQHqmDALDGHaspM---------LQLARIADKQIsEATLRSFLGSFGFSG--ERMdtPCEsFSGGERARLALA--LI 444
Cdd:COG3842 81 MVFQD--YALFPH---LtvaenvafgLRMRGVPKAEI-RARVAELLELVGLEGlaDRY--PHQ-LSGGQQQRVALAraLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 445 VwqRPNVLILDEPTNHLDL----DMRHALSMALQDFEGAVVLVSHErQLIA-SVCDELLLVHGGK 504
Cdd:COG3842 152 P--EPRVLLLDEPLSALDAklreEMREELRRLQRELGITFIYVTHD-QEEAlALADRIAVMNDGR 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
312-504 |
2.65e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.78 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIaeKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG---------------ERKASELlni 376
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGrilwngqdltalppaERPVSML--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 gyFAQH----QMDALDGHA---SPMLQLARIADKQISEATLRSFLGSFGfsgERMdtpCESFSGGERARLALA-LIVWQR 448
Cdd:COG3840 77 --FQENnlfpHLTVAQNIGlglRPGLKLTAEQRAQVEQALERVGLAGLL---DRL---PGQLSGGQRQRVALArCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 449 PnVLILDEPTNHLDLDMRH---ALSMALQDFEGAVVL-VSHERQLIASVCDELLLVHGGK 504
Cdd:COG3840 149 P-ILLLDEPFSALDPALRQemlDLVDELCRERGLTVLmVTHDPEDAARIADRVLLVADGR 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
312-492 |
2.71e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 69.70 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIA-EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------RKASELL--NI 376
Cdd:COG2884 2 IRFENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlkRREIPYLrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GY-FAQHQ----MDALDGHASPmLQLARIADKQIsEATLRSFLGSFGFSGeRMDTPCESFSGGERARLAL--ALIVwqRP 449
Cdd:COG2884 82 GVvFQDFRllpdRTVYENVALP-LRVTGKSRKEI-RRRVREVLDLVGLSD-KAKALPHELSGGEQQRVAIarALVN--RP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492309081 450 NVLILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIAS 492
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDR 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
328-514 |
3.29e-13 |
|
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: 69.53 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 328 EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGE--RKASEllNIGYFAQH-----QMDA 386
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGKelRKARR--RIGMIFQHfnllsSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 387 LDGHASPmLQLARIADKQISEATLRsFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLD---- 462
Cdd:cd03258 100 FENVALP-LEIAGVPKAEIEERVLE-LLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDpett 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 463 ---LDMRHALSmalQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEfEGDLQD 514
Cdd:cd03258 177 qsiLALLRDIN---RELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE-EGTVEE 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
307-504 |
4.28e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 70.95 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSsplLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLP--LLAGERka 370
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGletpdsgrivlngrDLFtnLPPRER-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 371 sellNIGYFAQH-----QMD-------ALDGHASPMLQLARIADKQISEATLRSFlgsfgfsGERMdtPCEsFSGGERAR 438
Cdd:COG1118 76 ----RVGFVFQHyalfpHMTvaeniafGLRVRPPSKAEIRARVEELLELVQLEGL-------ADRY--PSQ-LSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 439 LALA--LIVwqRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG1118 142 VALAraLAV--EPEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-219 |
4.53e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.15 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRR-GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVK----- 74
Cdd:COG4178 362 ALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYlplgt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 75 ---ALDMPaidfvlsgdeefwdiqnklAQPDQLTDFELAK-LHgrfdeihgysapskaaqlMAGLGFLENqlRLNVES-- 148
Cdd:COG4178 442 lreALLYP-------------------ATAEAFSDAELREaLE------------------AVGLGHLAE--RLDEEAdw 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 149 ---FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKA--YEGTLILISHdRDFLDAITDHILHIE 219
Cdd:COG4178 483 dqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-223 |
6.00e-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: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALlgslgadeGSLTRPTGWTVAHMAQEVKALD 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQAlkgvSLSIEKGEFVAIVGPSGSGKSTLLNIL--------GGLDRPTSGEVRVDGTDISKLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 MPAID--------FVlsgdeeFwdiQNKLAQPDqLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESF 149
Cdd:cd03255 73 EKELAafrrrhigFV------F---QSFNLLPD-LTALENVELPLLLAGVPKKERRERAEELLERVG-LGDRLNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AIL-WLEDWLKAYEGTLILISHDRDfLDAITDHILHIENQEL 223
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkEVMeLLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
7.29e-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: 71.47 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVS----LRRGGRVlfqKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPTGWT 65
Cdd:COG1123 260 LLEVRNLSkrypVRGKGGV---RAvddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSilfdgkdLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 66 VAHMAQEV--------KALD--MPAidfvlsGDEefwdiqnkLAQPdqltdfelAKLHGRFDEIhgySAPSKAAQLMAGL 135
Cdd:COG1123 337 LRELRRRVqmvfqdpySSLNprMTV------GDI--------IAEP--------LRLHGLLSRA---ERRERVAELLERV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 136 GFLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIL-WLEDWLKAYEGTLILISHDRDFLDAI 211
Cdd:COG1123 392 GLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqAQILnLLRDLQRELGLTYLFISHDLAVVRYI 471
|
....*
gi 492309081 212 TDHIL 216
Cdd:COG1123 472 ADRVA 476
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
308-502 |
7.34e-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: 68.91 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 308 SSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER----KASELL--- 374
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRDitglPPHRIArlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 ------NIGYF------------AQHQMDALDGHASPMLQLARIADKQISEATLRsFLGSFGFsGERMDTPCESFSGGER 436
Cdd:COG0411 81 iartfqNPRLFpeltvlenvlvaAHARLGRGLLAALLRLPRARREEREARERAEE-LLERVGL-ADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 437 ARLALALIVWQRPNVLILDEPTNHLDLDMRHALS---MALQDFEG-AVVLVSHERQLIASVCDELL-LVHG 502
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAeliRRLRDERGiTILLIEHDMDLVMGLADRIVvLDFG 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-504 |
7.82e-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: 67.90 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 324 KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASE-------LLNIGY-FAQHQ---- 383
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgtdiSKLSEkelaafrRRHIGFvFQSFNllpd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 384 MDALDGHASPMLqLARIADKQIsEATLRSFLGSFGFsGERMDTPCESFSGGERARLALA--LIvwQRPNVLILDEPTNHL 461
Cdd:cd03255 97 LTALENVELPLL-LAGVPKKER-RERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIAraLA--NDPKIILADEPTGNL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492309081 462 DLDMRHA---LSMALQDFEG-AVVLVSHERQLiASVCDELLLVHGGK 504
Cdd:cd03255 172 DSETGKEvmeLLRELNKEAGtTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-220 |
8.55e-13 |
|
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: 66.83 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKALDmPAI 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-DGEDLTDLEDELPPLR-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 DFVlsgdeefwdIQNklaqpdqltdfelaklhgrfdeihgysapskaAQLMAGLGFLEN-QLRLnvesfSGGWRMRLNLA 160
Cdd:cd03229 79 GMV---------FQD--------------------------------FALFPHLTVLENiALGL-----SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK---AYEG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKslqAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
312-514 |
9.22e-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: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLN-IGY------ 378
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILApdsgevLWDGEPLDPEDRRrIGYlpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 -------------FAQ-HQMDALDghaspmlqlariADKQISEatlrsFLGSFGFsGERMDTPCESFSGGE--RARLALA 442
Cdd:COG4152 82 lypkmkvgeqlvyLARlKGLSKAE------------AKRRADE-----WLERLGL-GDRANKKVEELSKGNqqKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 443 LIvwQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGA-VVLVSHERQLIASVCDELLLVHGGKcTEFEGDLQD 514
Cdd:COG4152 144 LL--HDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTtVIFSSHQMELVEELCDRIVIINKGR-KVLSGSVDE 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
308-500 |
9.64e-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: 70.78 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 308 SSPLLTLDNASIGYGDKQIAEK-IRLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPLLAGERkASELL 374
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRpVSFTVPPGERVALVGPSGAGKSTLLNLLlgfvdptegsiaVNGVPLADADA-DSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 NIGYFAQH-QMdaLDGHASPMLQLAR--IADKQISEATLRSFLGSFGFS-GERMDTPCES----FSGGERARLALALIVW 446
Cdd:TIGR02857 397 QIAWVPQHpFL--FAGTIAENIRLARpdASDAEIREALERAGLDEFVAAlPQGLDTPIGEggagLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 447 QRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIAsVCDELLLV 500
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
324-506 |
1.07e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 324 KQIAEKIRL-----QITPNSRIGLLGMNGAGKSTLIKSLVGDLP-----LLAG----ERKASELLNI-GYFAQHQMDALD 388
Cdd:PRK03695 4 NDVAVSTRLgplsaEVRAGEILHLVGPNGAGKSTLLARMAGLLPgsgsiQFAGqpleAWSAAELARHrAYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 GHASPMLQLARIADKQI--SEATLRSFLGSFGFsGERMDTPCESFSGGE--RARLALA-LIVWQRPN----VLILDEPTN 459
Cdd:PRK03695 84 MPVFQYLTLHQPDKTRTeaVASALNEVAEALGL-DDKLGRSVNQLSGGEwqRVRLAAVvLQVWPDINpagqLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492309081 460 HLDLDMRHALSMALQDFE---GAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCqqgIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
324-505 |
1.11e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.33 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 324 KQIAEKIRL-----QITPNSRIGLLGMNGAGKSTLIKSLVGDLP-----LLAGER----KASELLNI-GYFAQHQMdald 388
Cdd:COG4138 4 NDVAVAGRLgpisaQVNAGELIHLIGPNGAGKSTLLARMAGLLPgqgeiLLNGRPlsdwSAAELARHrAYLSQQQS---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 gHASPM-------LQLARIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGE--RARLALALI-VWQRPN----VLIL 454
Cdd:COG4138 80 -PPFAMpvfqylaLHQPAGASSEAVEQLLAQLAEALGLE-DKLSRPLTQLSGGEwqRVRLAAVLLqVWPTINpegqLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492309081 455 DEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-222 |
1.45e-12 |
|
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: 66.86 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 32 LTGVNGAGKSTLFAALLGSL-GadEGSLTRPTGWTVAHMAQEVKALDMPAIDFVLSGDEEFwDIQNKLAQPDQLtdfelA 110
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALtG--ELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKY-TITRSLAILENV-----I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 111 KLH-GRFDEIhgysapskaaqLMAGLGFLenqlrlnvesfSGGWRM------RLNLARTLMSRSDLLLLDEPTNHLDLDA 183
Cdd:cd03240 99 FCHqGESNWP-----------LLDMRGRC-----------SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 184 I-LWLEDWLKAYEGT----LILISHDRDFLDAItDHILHIENQE 222
Cdd:cd03240 157 IeESLAEIIEERKSQknfqLIVITHDEELVDAA-DHIYRVEKDG 199
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
1.65e-12 |
|
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: 67.53 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALdmpai 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVG--------LLRPDSGEVLIDGEDISGL----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 dfvlsGDEEFWDIQNKL-------AQPDQLTDFE----LAKLHGRFDEihgysaPSKAAQLMAGLGF--LENQLRLNVES 148
Cdd:cd03261 68 -----SEAELYRLRRRMgmlfqsgALFDSLTVFEnvafPLREHTRLSE------EEIREIVLEKLEAvgLRGAEDLYPAE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDwlkAYEGTLILISHDRDFLDAITDHIL 216
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKK---ELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
2.06e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKaldmpa 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLsgdeefwdiqnklaqPDQLTDFELAKLHGRFDEIHGYSAPSKAAQLmaglgflenqLRLNVESFSGGWRMRLNLA 160
Cdd:PRK09544 78 LDTTL---------------PLTVNRFLRLRPGTKKEDILPALKRVQAGHL----------IDAPMQKLSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTL----ILISHDRDFLDAITDHIL 216
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVL 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-184 |
2.13e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTL---FAALL----GSLGADEGSLTRPTGWTVAHMAQEV 73
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrlIAGLLppaaGTIKLDGGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 74 KALDmPAidfvLSGDE--EFWdiqnklaqpdqltdfelAKLHGRFDeihgySAPSKAAQLMaGLGFLENqlrLNVESFSG 151
Cdd:PRK13539 82 NAMK-PA----LTVAEnlEFW-----------------AAFLGGEE-----LDIAAALEAV-GLAPLAH---LPFGYLSA 130
|
170 180 190
....*....|....*....|....*....|...
gi 492309081 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAI 184
Cdd:PRK13539 131 GQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
316-507 |
2.69e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIA--EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------------RKASELLNIGY 378
Cdd:PRK10584 13 KKSVGQGEHELSilTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEvslvgqplhqmdeeaRAKLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 FAQHQM-----DALDGHASPMLqLARIADKQiSEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK10584 93 VFQSFMliptlNALENVELPAL-LRGESSRQ-SRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 454 LDEPTNHLD-------LDMRHALSmalQDFEGAVVLVSHERQLiASVCDELLLVHGGKCTE 507
Cdd:PRK10584 170 ADEPTGNLDrqtgdkiADLLFSLN---REHGTTLILVTHDLQL-AARCDRRLRLVNGQLQE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
322-507 |
3.88e-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: 67.14 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERKASELLNIGYFAQHQMDAL 387
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlekpaqgtvsfrgqDLYQLDRKQRRAFRRDVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 388 DGHAS-------PMLQLARIaDKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNH 460
Cdd:TIGR02769 102 NPRMTvrqiigePLRHLTSL-DESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492309081 461 LDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:TIGR02769 181 LDMVLQAVILELLrklqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
309-458 |
3.89e-12 |
|
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: 66.54 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 309 SPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASEL--LNI 376
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSirfdgeditgLPPHRIarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GY-------FAQhqmdaldghaspM-----LQLARIA--DKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLAL- 441
Cdd:COG0410 81 GYvpegrriFPS------------LtveenLLLGAYArrDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIg 148
|
170
....*....|....*...
gi 492309081 442 -ALIvwQRPNVLILDEPT 458
Cdd:COG0410 149 rALM--SRPKLLLLDEPS 164
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-204 |
6.02e-12 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 65.66 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgaDEGSLTRPTGwTVAHMAQEVKALDMPAI 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLN--DLIPGAPDEG-EVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 D--------------FVLSgdeefwdIQNKLAQPDQLTDfelAKLHGRFDEIhgysapSKAAQLMAGLgFLENQLRLNVE 147
Cdd:cd03260 78 ElrrrvgmvfqkpnpFPGS-------IYDNVAYGLRLHG---IKLKEELDER------VEEALRKAAL-WDEVKDRLHAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK--AYEGTLILISHD 204
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
312-495 |
6.98e-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: 65.67 E-value: 6.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGD-KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLN----I 376
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlidgtdinkLKGKALRQlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GYFAQH-----QMDALD-------GHAS---PMLQLARIADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLAL 441
Cdd:cd03256 81 GMIFQQfnlieRLSVLEnvlsgrlGRRStwrSLFGLFPKEEKQRALAALER-VGLLDKAYQRADQ----LSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 442 ALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVS-HERQLIASVCD 495
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYAD 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
285-504 |
7.18e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 285 MQQLaPAHVDTPFTfsfreptkmssplltLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIK--------- 355
Cdd:PRK10575 1 MQEY-TNHSDTTFA---------------LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKmlgrhqpps 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 356 ---SLVGDLPLLAGERKASELlNIGYFAQhQMDALDGHASPML----------QLAR--IADKQISEATLrSFLGSFGFS 420
Cdd:PRK10575 65 egeILLDAQPLESWSSKAFAR-KVAYLPQ-QLPAAEGMTVRELvaigrypwhgALGRfgAADREKVEEAI-SLVGLKPLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 421 GERMDtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLD-------LDMRHALSmalQDFEGAVVLVSHERQLIASV 493
Cdd:PRK10575 142 HRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqvdvLALVHRLS---QERGLTVIAVLHDINMAARY 214
|
250
....*....|.
gi 492309081 494 CDELLLVHGGK 504
Cdd:PRK10575 215 CDYLVALRGGE 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-215 |
7.65e-12 |
|
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: 65.22 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVahmaqevkaldmpaidFVL--SGDEEFWDIQNKL 98
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTG--------ELRPTSGTA----------------YINgySIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 99 -------AQPDQLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGFLENQLRLnVESFSGGWRMRLNLARTLMSRSDLLL 171
Cdd:cd03263 78 gycpqfdALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKR-ARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492309081 172 LDEPTnhLDLDA----ILWleDWLKAYEG--TLILISHDRDFLDAITDHI 215
Cdd:cd03263 157 LDEPT--SGLDPasrrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-216 |
7.72e-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: 65.54 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL----TRPTGWT---VAHMA-----QE 72
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLPpheIARLGigrtfQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 73 VKAL-DMPAIDFVLSGdeefwdiqnklAQPDQLTDFELAKLHGRFDEihgysAPSKAAQLMAGLGfLENQLRLNVESFSG 151
Cdd:cd03219 84 PRLFpELTVLENVMVA-----------AQARTGSGLLLARARREERE-----ARERAEELLERVG-LADLADRPAGELSY 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 152 GWRMRLNLARTLMSRSDLLLLDEPT---NHLDLDAIL-WLEDwLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAeLIRE-LRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-181 |
1.06e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.52 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP-TGWTVAHMAQevkal 76
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngRPlAAWSPWELAR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 dMPAIdfvlsgdeefwdiqnkLAQPDQLT-DF---ELAKLhGRfdEIHGYSAPSK---AAQLMA--GLGFLENQlrlNVE 147
Cdd:COG4559 76 -RRAV----------------LPQHSSLAfPFtveEVVAL-GR--APHGSSAAQDrqiVREALAlvGLAHLAGR---SYQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492309081 148 SFSGGWRMRLNLARTL-------MSRSDLLLLDEPTNHLDL 181
Cdd:COG4559 133 TLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
328-502 |
1.07e-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: 68.50 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 328 EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKA---SELLNIGYFAQH-----QMDALDG------HASP 393
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagkSILTNISDVHQNmgycpQFDAIDDlltgreHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 394 MLQLARIADKQISEATLRSfLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHAL---S 470
Cdd:TIGR01257 2036 YARLRGVPAEEIEKVANWS-IQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwntI 2113
|
170 180 190
....*....|....*....|....*....|...
gi 492309081 471 MALQDFEGAVVLVSHERQLIASVCDEL-LLVHG 502
Cdd:TIGR01257 2114 VSIIREGRAVVLTSHSMEECEALCTRLaIMVKG 2146
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-203 |
1.28e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPTGWTVAHMAQEVKALD--MP 79
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT-VLGVPVPARARLARARIgvVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 AIDFVlsgDEEFWDIQNKLaqpdqltdfelakLHGRFdeiHGYSAPSKAAQLMAGLGF--LENQLRLNVESFSGGWRMRL 157
Cdd:PRK13536 121 QFDNL---DLEFTVRENLL-------------VFGRY---FGMSTREIEAVIPSLLEFarLESKADARVSDLSGGMKRRL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492309081 158 NLARTLMSRSDLLLLDEPTNHLDLDA--ILW--LEDWLkAYEGTLILISH 203
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLL-ARGKTILLTTH 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-228 |
1.38e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 64.66 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 18 QKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT----RPTGWTVAHMAQevkaldmpaIDFVLSGDEEF-W 92
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglVPWKRRKKFLRR---------IGVVFGQKTQLwW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 93 DIQ-----NKLAQPDQLTDFELAKlhgRFDEIhgysapskaAQLMAglgfLENQLRLNVESFSGGWRMRLNLARTLMSRS 167
Cdd:cd03267 109 DLPvidsfYLLAAIYDLPPARFKK---RLDEL---------SELLD----LEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 168 DLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQELtLYTG 228
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
321-504 |
1.57e-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: 64.09 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPLLAGERKASEL-LNIGYFAQH----- 382
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdsgtiiIDGLKLTDDKKNINELrQKVGMVFQQfnlfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 QMDALDGHASPmLQLARIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03262 90 HLTVLENITLA-PIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492309081 463 LDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03262 168 PELVGEVLDVMKDLaeEGmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
323-491 |
1.85e-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: 64.30 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 323 DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAGER-------KASELLNI--GYFAQ--HQM- 384
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGlDNPtsgevLFNGQSlsklssnERAKLRNKklGFIYQfhHLLp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 385 --DALDGHASPMLqlarIADKQISEATLRSF--LGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNH 460
Cdd:TIGR02211 97 dfTALENVAMPLL----IGKKSVKEAKERAYemLEKVGL-EHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 492309081 461 LD-------LDMRHALSmalQDFEGAVVLVSHERQLIA 491
Cdd:TIGR02211 172 LDnnnakiiFDLMLELN---RELNTSFLVVTHDLELAK 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
316-504 |
1.87e-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: 64.28 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAGERKASELL---NIGYFAQHQmdA 386
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPdsgtiLFGGEDATDVPVqerNVGFVFQHY--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 387 LDGHASPMLQLA-----RIADKQISEATLR----SFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:cd03296 85 LFRHMTVFDNVAfglrvKPRSERPPEAEIRakvhELLKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492309081 458 TNHLDLDMRHALSMALQDFEGAV----VLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-504 |
2.14e-11 |
|
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: 66.77 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLG----------------SLGADEGSLTRPTGWTVAHmaQEVKAL-DMPAIDF 83
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASNIRDTERAGIVIIH--QELTLVpELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 84 VLSGdeefwdiqNKLAQPDQLTDFELAKLhgrfdeihgysapsKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTL 163
Cdd:TIGR02633 99 IFLG--------NEITLPGGRMAYNAMYL--------------RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 164 MSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHILHIENQEltlytgnystfettrser 240
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ------------------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 241 laqqqqafekqqetraHLqkfidrfkakATKARQAQSR---IKQL--ERMQQLAPahvdtpftfsfREPTKMSSPLLTLD 315
Cdd:TIGR02633 219 ----------------HV----------ATKDMSTMSEddiITMMvgREITSLYP-----------HEPHEIGDVILEAR 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGD---KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPllaGERKASELLNigyfaQHQMDALDGHAS 392
Cdd:TIGR02633 262 NLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP---GKFEGNVFIN-----GKPVDIRNPAQA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 393 PMLQLARIAD--------------KQISEATLRSF-----------LGSFGFSGERM-------DTPCESFSGGERARLA 440
Cdd:TIGR02633 334 IRAGIAMVPEdrkrhgivpilgvgKNITLSVLKSFcfkmridaaaeLQIIGSAIQRLkvktaspFLPIGRLSGGNQQKAV 413
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 441 LALIVWQRPNVLILDEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKyeiYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-507 |
2.86e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.16 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYfAQHQMDALDGH- 390
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQ-DIFKMDVIELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 --------ASPM------------LQLARIA-DKQISEATLRSFLGSFGFSGE---RMDTPCESFSGGERARLALALIVW 446
Cdd:PRK14247 83 rvqmvfqiPNPIpnlsifenvalgLKLNRLVkSKKELQERVRWALEKAQLWDEvkdRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 447 QRPNVLILDEPTNHLDLDMR---HALSMALQDfEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTakiESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-504 |
3.18e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLL---AGE---------RKASELL-NIGY-FAQHQ--------MDAL 387
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---ILvptSGEvrvlgyvpfKRRKEFArRIGVvFGQRSqlwwdlpaIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 388 DghaspmLqLARIADkqISEATLRSFLGSF--GFS-GERMDTPCESFSGGERAR--LALALIvwQRPNVLILDEPTNHLD 462
Cdd:COG4586 118 R------L-LKAIYR--IPDAEYKKRLDELveLLDlGELLDTPVRQLSLGQRMRceLAAALL--HRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492309081 463 LDMRHalsmALQDF-------EGA-VVLVSHERQLIASVCDELLLVHGGK 504
Cdd:COG4586 187 VVSKE----AIREFlkeynreRGTtILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
318-507 |
3.63e-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: 66.30 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 318 SIGYGDKqIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkaselLNIGYFAQHQMD--ALDGHASPML 395
Cdd:TIGR01193 482 SYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE------ILLNGFSLKDIDrhTLRQFINYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 396 QLARIADKQISEATLrsfLGSF-GFSGERMDTPCE------------------------SFSGGERARLALALIVWQRPN 450
Cdd:TIGR01193 555 QEPYIFSGSILENLL---LGAKeNVSQDEIWAACEiaeikddienmplgyqtelseegsSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 451 VLILDEPTNHLDLDMRHALS---MALQDfeGAVVLVSHeRQLIASVCDELLLVHGGKCTE 507
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVnnlLNLQD--KTIIFVAH-RLSVAKQSDKIIVLDHGKIIE 688
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-502 |
4.03e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.58 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 334 ITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErKASELLNIGYFAQH------------QMDALDGH----------A 391
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-IEIELDTVSYKPQYikadyegtvrdlLSSITKDFythpyfkteiA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 392 SPmLQLARIADKQISEatlrsflgsfgfsgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03237 101 KP-LQIEQILDREVPE-----------------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*
gi 492309081 472 ALQDF----EGAVVLVSHERQLIASVCDELLLVHG 502
Cdd:cd03237 157 VIRRFaennEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
322-506 |
4.20e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.05 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLN-----IGYFAQHQMDALdgh 390
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKptsgsvLIRGEPITKENIRevrkfVGLVFQNPDDQI--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 ASPMLQlARIA--------DKQISEATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13652 92 FSPTVE-QDIAfgpinlglDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 463 LDMRHALSMALQDFEG----AVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK13652 170 PQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-180 |
4.59e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 62.60 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWkIGLTGVNGAGKSTLFAALLGSLGADEGSLTRptgwtvahmaQEVKALDMPai 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRI----------DGQDVLKQP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 dfvlsgdEEFWDIQNKLAQ----PDQLTDFE----LAKLHGrfdeIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGW 153
Cdd:cd03264 68 -------QKLRRRIGYLPQefgvYPNFTVREfldyIAWLKG----IPSKEVKARVDEVLELVN-LGDRAKKKIGSLSGGM 135
|
170 180
....*....|....*....|....*..
gi 492309081 154 RMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-225 |
5.37e-11 |
|
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: 61.95 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahmaqevkaldmp 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 aidfvlsgdeefwdiqnklaqpdqLTDFELAKLHGRFDeiHGYSAPSKAAQLMAGlgflenQLRLNV-ESFSGGWRMRLN 158
Cdd:cd03247 61 ------------------------LDGVPVSDLEKALS--SLISVLNQRPYLFDT------TLRNNLgRRFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 159 LARTLMSRSDLLLLDEPTNHLD-LDAILWLEDWLKAYEG-TLILISHDrdfLDAIT--DHILHIENQELTL 225
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKDkTLIWITHH---LTGIEhmDKILFLENGKIIM 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-180 |
5.86e-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: 66.09 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKALD-MPAIDFVLSG--- 87
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGvIPQKVFIFSGtfr 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 88 ----------DEEFWDIQNKLAQ-------PDQLtDFELaklhgrfdEIHGYSAPSKAAQLMAglgflenqlrlnvesfs 150
Cdd:TIGR01271 1310 knldpyeqwsDEEIWKVAEEVGLksvieqfPDKL-DFVL--------VDGGYVLSNGHKQLMC----------------- 1363
|
170 180 190
....*....|....*....|....*....|
gi 492309081 151 ggwrmrlnLARTLMSRSDLLLLDEPTNHLD 180
Cdd:TIGR01271 1364 --------LARSILSKAKILLLDEPSAHLD 1385
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
312-505 |
6.39e-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: 61.40 E-value: 6.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGD-KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHqmdaldgh 390
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 asPMLqlariadkqiSEATLRSFLgsfgfsgermdtpC----ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:cd03223 73 --PYL----------PLGTLREQL-------------IypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*....
gi 492309081 467 HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKC 505
Cdd:cd03223 128 DRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
312-514 |
6.47e-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: 62.68 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------------RKASelLNIG 377
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKilidgqdithlpmhERAR--LGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQHqmdaldghAS------------PMLQLARIADKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIV 445
Cdd:TIGR04406 80 YLPQE--------ASifrkltveenimAVLEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 446 WQRPNVLILDEPTNHLD----LDMRHALSMaLQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTeFEGDLQD 514
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDpiavGDIKKIIKH-LKERGIGVLITDHNVRETLDICDRAYIISDGKVL-AEGTPAE 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
312-490 |
7.23e-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: 61.77 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDlP---------LLAGErkasELLNI------ 376
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyevtegeiLFKGE----DITDLppeera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 --GYFAQHQmdaldghaSPMlqlariadkQISEATLRSFLGSFGfsgermdtpcESFSGGERARLALALIVWQRPNVLIL 454
Cdd:cd03217 76 rlGIFLAFQ--------YPP---------EIPGVKNADFLRYVN----------EGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....*....
gi 492309081 455 DEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLI 490
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLreEGkSVLIITHYQRLL 167
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
309-507 |
7.64e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 309 SPLLTLDNASIGY---------GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLA 365
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGlespsqgnvswrgePLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 366 GERKASELLNIGYFAQHQMDALDGH-------ASPMLQLARIaDKQISEATLRSFLGSFGFSGERMDTPCESFSGGE--R 436
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRktvreiiREPLRHLLSL-DKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQlqR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 437 ARLALALIVwqRPNVLILDEPTNHLDLdMRHALSMAL-----QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK10419 160 VCLARALAV--EPKLLILDEAVSNLDL-VLQAGVIRLlkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
312-485 |
7.80e-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: 62.10 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIA----EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLNIGYFAQ 381
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HqmDALDGHASPM------LQLARIADKQISEATlRSFLGSFGFSGERMDTPCEsFSGGERARLALA--LIVwqRPNVLI 453
Cdd:cd03293 81 Q--DALLPWLTVLdnvalgLELQGVPKAEARERA-EELLELVGLSGFENAYPHQ-LSGGMRQRVALAraLAV--DPDVLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 492309081 454 LDEPTNHLD----LDMRHALSMALQDFEGAVVLVSH 485
Cdd:cd03293 155 LDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTH 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
8.62e-11 |
|
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: 62.15 E-value: 8.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKALDMPAI 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILI-DGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 DFVLsgdeeFwdiqnklaqpDQLTDFE-----LAKLHGRFDEIHgysapSKAAQLMAGLGfLENQLRLNVESFSGGWRMR 156
Cdd:cd03259 80 DYAL-----F----------PHLTVAEniafgLKLRGVPKAEIR-----ARVRELLELVG-LEGLLNRYPHELSGGQQQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 157 LNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03259 139 VALARALAREPSLLLLDEPLSALDAKLREELREELKELqrelGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
312-506 |
8.89e-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: 60.91 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKA----SELLNIGYFAQ 381
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKpdsgeiLVDGKEVSfaspRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HQMdaldghaspmlqlariadkqiseatlrsflgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLILDEPTNHL 461
Cdd:cd03216 81 YQL-----------------------------------------------SVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 462 DLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:cd03216 114 TPAEVERLFKVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
335-504 |
9.38e-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: 61.93 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 335 TPNSRIGLLGMNGAGKSTLIKSLVG------------DLPLLAGERK---ASELLNIGYFAQHQmdALDGHASPMLQLA- 398
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGlekpdggtivlnGTVLFDSRKKinlPPQQRKIGLVFQQY--ALFPHLNVRENLAf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 399 -----RIADKQISEATLrsfLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL 473
Cdd:cd03297 99 glkrkRNREDRISVDEL---LDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 492309081 474 ----QDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03297 175 kqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
330-510 |
9.43e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.14 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------RKASELLNI----GYFAQHqmdaldghasPMLQ 396
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditDKKVKLSDIrkkvGLVFQY----------PEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 397 LAR------IA---------DKQISEATLRSfLGSFGFSGERM--DTPCEsFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:PRK13637 96 LFEetiekdIAfgpinlglsEEEIENRVKRA-MNIVGLDYEDYkdKSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 460 HLDLDMRHALSMALQD----FEGAVVLVSHERQLIASVCDELLLVHGGKCtEFEG 510
Cdd:PRK13637 174 GLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKC-ELQG 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
325-508 |
1.15e-10 |
|
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: 61.66 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 325 QIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqMDALDGHASPMLQLAR----I 400
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE--------------IDGIDISTIPLEDLRSsltiI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 401 A-DKQISEATLRSFLGSFG-------FSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMA 472
Cdd:cd03369 88 PqDPTLFSGTIRSNLDPFDeysdeeiYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 492309081 473 L-QDFEGAVVL-VSHERQLIASvCDELLLVHGGKCTEF 508
Cdd:cd03369 168 IrEEFTNSTILtIAHRLRTIID-YDKILVMDAGEVKEY 204
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
312-504 |
1.23e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 61.33 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQ-----ITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASEllNIGYFAQhqmda 386
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKdinleVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQ----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 387 ldghaSPMLQlariadkqisEATLRS---FlgsfgfsGERMDTP--------CE---------------------SFSGG 434
Cdd:cd03250 74 -----EPWIQ----------NGTIREnilF-------GKPFDEEryekvikaCAlepdleilpdgdlteigekgiNLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 435 ERARLALALIVWQRPNVLILDEPTNHLDLD-----MRHALSMALQDfEGAVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHvgrhiFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-206 |
1.49e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 61.34 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGAD---EGSLtRPTGWTVAHMAQEVKALD 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV-LLNGRRLTALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 MPAIDFVLsgdeeF--WDIQNKLAqpdqltdFELAklhgrfdeiHGYSAPSKAAQLM-----AGLGFLENQlrlNVESFS 150
Cdd:COG4136 80 ILFQDDLL-----FphLSVGENLA-------FALP---------PTIGRAQRRARVEqaleeAGLAGFADR---DPATLS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDW----LKAYEGTLILISHDRD 206
Cdd:COG4136 136 GGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE 195
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
1.67e-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: 61.53 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALDmpa 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG--------LLRPDSGEILVDGQDITGLS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 idfvlsgDEEFWDIQNKL-------AQPDQLTDFE-LA---KLHGRFDEihgysapSKAAQL------MAGLGFLEN--- 140
Cdd:COG1127 74 -------EKELYELRRRIgmlfqggALFDSLTVFEnVAfplREHTDLSE-------AEIRELvlekleLVGLPGAADkmp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 141 -QLrlnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD------LDA-ILWLEDWLKAyegTLILISHDRDFLDAIT 212
Cdd:COG1127 140 sEL-------SGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDElIRELRDELGL---TSVVVTHDLDSAFAIA 209
|
250 260
....*....|....*....|....*....
gi 492309081 213 DHILHIENQELtLYTGNYSTFETTRSERL 241
Cdd:COG1127 210 DRVAVLADGKI-IAEGTPEELLASDDPWV 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-221 |
1.89e-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: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 30 IGLTGVNGAGKSTLFAALLGSLGADEGSLTRPtGWTVAHMAQEVKALDMPAIDFVLSGDeefwdIQNKLAQPDQLTdfEL 109
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKADYEGTVRDLLSSI-----TKDFYTHPYFKT--EI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 110 AKlhgrfdeihgysaPSKAAQLMaglgflENQLRlnveSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLED 189
Cdd:cd03237 100 AK-------------PLQIEQIL------DREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 492309081 190 WLKAY----EGTLILISHDRDFLDAITDHILHIENQ 221
Cdd:cd03237 157 VIRRFaennEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
340-536 |
2.12e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVGDLPLLAGE-RKASELLNIGYFA--QHQMDALDGHASPMLQLArIADKQISEATLRsfLGS 416
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKvDRNGEVSVIAISAglSGQLTGIENIEFKMLCMG-FKRKEIKAMTPK--IIE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 417 FGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGA---VVLVSHERQLIASV 493
Cdd:PRK13546 130 FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQF 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492309081 494 CDELLLVHGGKCTEFeGDLQD----YAKWLREARQQQINAQTAVAQN 536
Cdd:PRK13546 210 CTKIAWIEGGKLKDY-GELDDvlpkYEAFLNDFKKKSKAEQKEFRNK 255
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
305-514 |
2.26e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.43 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 305 TKMSSPLLTLDNASIGY----GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERKAS--------E 372
Cdd:PRK09473 6 QQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG---LLAANGRIGgsatfngrE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 373 LLNIgyfAQHQMDALDGH------ASPMLQL---ARIAD---------KQISEATlrSFLGSFGF--------SGERMDT 426
Cdd:PRK09473 83 ILNL---PEKELNKLRAEqismifQDPMTSLnpyMRVGEqlmevlmlhKGMSKAE--AFEESVRMldavkmpeARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 427 PCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRhALSMAL-----QDFEGAVVLVSHERQLIASVCDELLLVH 501
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQ-AQIMTLlnelkREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250
....*....|...
gi 492309081 502 GGKCTEFeGDLQD 514
Cdd:PRK09473 237 AGRTMEY-GNARD 248
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-223 |
2.42e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 3 QFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---TRPTG-WTVAHMAQEVKALdm 78
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldAQPLEsWSSKAFARKVAYL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 79 paidfvlsgdeefwdiQNKLAQPDQLTDFELAKLhGRFdEIHG----YSAPSKA----AQLMAGLGFLENQLrlnVESFS 150
Cdd:PRK10575 91 ----------------PQQLPAAEGMTVRELVAI-GRY-PWHGalgrFGAADREkveeAISLVGLKPLAHRL---VDSLS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIENQEL 223
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
312-504 |
2.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.95 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAE-----KIRLQITPNSRIGLLGMNGAGKSTLIK------------SLVGDLPLLAGERKASELL 374
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 N----IGY---FAQHQM--DALDGH-ASPMLQLAriADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALI 444
Cdd:PRK13645 87 RlrkeIGLvfqFPEYQLfqETIEKDiAFGPVNLG--ENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 445 VWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
307-462 |
3.11e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.94 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSL--VGDL-P--LLAGE-------------- 367
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLnPevTITGSivynghniysprtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 368 ----RKasellNIGYFAQHQmdaldgHASPM---------LQLARIADKQI-SEATLRSFLGS--FGFSGERMDTPCESF 431
Cdd:PRK14239 81 tvdlRK-----EIGMVFQQP------NPFPMsiyenvvygLRLKGIKDKQVlDEAVEKSLKGAsiWDEVKDRLHDSALGL 149
|
170 180 190
....*....|....*....|....*....|.
gi 492309081 432 SGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
150-513 |
3.14e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIENQELTl 225
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQQELNmGLLFITHNLSIVRKLADRVAVMQNGRCV- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 226 ytgnystfETTRSERLAQQQqafekqqeTRAHLQKFIDRfkakatkarqaqsrikqlERMQQLAPAHVDTPftfsfrept 305
Cdd:PRK15134 237 --------EQNRAATLFSAP--------THPYTQKLLNS------------------EPSGDPVPLPEPAS--------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 306 kmssPLLTLDNASIGY-----------GDKQIAEKIRLQITPNSRIGLLGMNGAGKST-------LIKS----LVGDLPL 363
Cdd:PRK15134 274 ----PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglallrLINSqgeiWFDGQPL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 364 LAGERKasELLNIgyfaQHQMDAL--DGHAS--PMLQLARIAD-------KQIS----EATLRSFLGSFGFSGE-RMDTP 427
Cdd:PRK15134 350 HNLNRR--QLLPV----RHRIQVVfqDPNSSlnPRLNVLQIIEeglrvhqPTLSaaqrEQQVIAVMEEVGLDPEtRHRYP 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 428 CEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQ-DFEGAVVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK15134 424 AE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAqilALLKSLQqKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
410
....*....|
gi 492309081 504 KCTEfEGDLQ 513
Cdd:PRK15134 503 EVVE-QGDCE 511
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
312-507 |
3.58e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 60.58 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYG--DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAgerKASELLN 375
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfyvpengrvlvdghDLALAD---PAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 376 IGYFAQHQM---------DALDGHASPM---LQLARIADKQisEATLRSFLGSFGFSGERmdtpCESFSGGERARLALAL 443
Cdd:cd03252 78 VGVVLQENVlfnrsirdnIALADPGMSMervIEAAKLAGAH--DFISELPEGYDTIVGEQ----GAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 444 IVWQRPNVLILDEPTNHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
311-504 |
4.05e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.68 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------RKASELLNIGY 378
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 FAQH-----QMDALDGHASpMLQLARIADKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK10895 83 LPQEasifrRLSVYDNLMA-VLQIRDDLSAEQREDRANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 454 LDEPTNHLD----LDMRHALSMaLQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK10895 161 LDEPFAGVDpisvIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGH 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
313-485 |
4.66e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.48 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 313 TLDNASIGYGDKQIAEKIRLQItPNSRI-GLLGMNGAGKSTLIkSLVGDL-PLLAGE-----------------RKAS-- 371
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTI-PKGGItALIGPNGAGKSTLL-SMISRLlPPDSGEvlvdgldvattpsrelaKRLAil 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 372 -------------ELLNIGYFAQHQmdaldGHASPmlqlariADKQISEATLRsFLGSFGFSGERMDTpcesFSGGERAR 438
Cdd:COG4604 81 rqenhinsrltvrELVAFGRFPYSK-----GRLTA-------EDREIIDEAIA-YLDLEDLADRYLDE----LSGGQRQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492309081 439 LALALIVWQRPNVLILDEPTNhlDLDMRHALSM------ALQDFEGAVVLVSH 485
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLN--NLDMKHSVQMmkllrrLADELGKTVVIVLH 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
312-457 |
5.06e-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: 60.25 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------------RKASelLNIG 377
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgqditklpmhKRAR--LGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQH-----QMDALDgHASPMLQLARIADKQISEaTLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVL 452
Cdd:cd03218 79 YLPQEasifrKLTVEE-NILAVLEIRGLSKKEREE-KLEELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKFL 155
|
....*
gi 492309081 453 ILDEP 457
Cdd:cd03218 156 LLDEP 160
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-204 |
5.94e-10 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 59.79 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALD 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAG--------LERPTSGEVLVDGEPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 mPAIDFVLSGDEEF-WD--IQNKLaqpdqltdFELaklhgrfdEIHGYSAP---SKAAQLMA--GLGFLEN----QLrln 145
Cdd:cd03293 73 -PDRGYVFQQDALLpWLtvLDNVA--------LGL--------ELQGVPKAearERAEELLElvGLSGFENayphQL--- 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 146 vesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLKAYEGTLILISHD 204
Cdd:cd03293 133 ----SGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-203 |
7.25e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 58.91 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---TRPTGWTVAHMAQEVKAL-DMPA 80
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwnGTPLAEQRDEPHENILYLgHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLSGDE--EFWdiqNKLAQPDQLTDFE-LAKlhgrfdeihgysapskaaqlmAGLGFLENqlrLNVESFSGGWRMRL 157
Cdd:TIGR01189 84 LKPELSALEnlHFW---AAIHGGAQRTIEDaLAA---------------------VGLTGFED---LPAAQLSAGQQRRL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492309081 158 NLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISH 203
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
325-500 |
7.34e-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: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 325 QIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGD-LP----------------LLAGERKASEL--LNIGYFAQH--- 382
Cdd:TIGR02324 22 PVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANyLPdsgrilvrhegawvdlAQASPREVLEVrrKTIGYVSQFlrv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 --QMDALDGHASPMLQLAriADKQISEATLRSFLGSFGFSgERM-DTPCESFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:TIGR02324 102 ipRVSALEVVAEPLLERG--VPREAARARARELLARLNIP-ERLwHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 460 HLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLV 500
Cdd:TIGR02324 179 SLDAANRQVVVELIAEAKArgaALIGIFHDEEVRELVADRVMDV 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
316-514 |
7.39e-10 |
|
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: 60.90 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIaeKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERK-ASELLN--------------IGYFA 380
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlNGRTLFdsrkgiflppekrrIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 381 QhqmDA-LDGHASPMLQL------ARIADKQISEATLRSFLGSfgfsGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:TIGR02142 82 Q---EArLFPHLSVRGNLrygmkrARPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 454 LDEPTNHLDLDMRHALSMALQ----DFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD 514
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLErlhaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA-GPIAE 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
340-500 |
9.62e-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: 59.37 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVG------------------DLpLLAGERkasELLN-----IGYFAQH-----QMDALDGHA 391
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGnylpdsgsilvrhdggwvDL-AQASPR---EILAlrrrtIGYVSQFlrvipRVSALDVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 392 SPMLQLAriADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERAR--LALALIVwqRPNVLILDEPTNHLDLDMRHAL 469
Cdd:COG4778 116 EPLLERG--VDREEARARARELLARLNLPERLWDLPPATFSGGEQQRvnIARGFIA--DPPLLLLDEPTASLDAANRAVV 191
|
170 180 190
....*....|....*....|....*....|....
gi 492309081 470 SMALQDF--EG-AVVLVSHERQLIASVCDELLLV 500
Cdd:COG4778 192 VELIEEAkaRGtAIIGIFHDEEVREAVADRVVDV 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-224 |
1.02e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 58.90 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGG-----RVLfQKASMQLHPGWKIGLTGVNGAGKSTLfaalLGSLGAdegsLTRPTGWTVAHMAQEVKA 75
Cdd:COG1136 4 LLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTL----LNILGG----LDRPTSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 76 LDmpaidfvlsgdeefwdiQNKLAQ----------------PDqLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLE 139
Cdd:COG1136 75 LS-----------------ERELARlrrrhigfvfqffnllPE-LTALENVALPLLLAGVSRKERRERARELLERVG-LG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 140 NQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAilwLEDWLKAYEGTLILISHDRDfLDAIT 212
Cdd:COG1136 136 DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTIVMVTHDPE-LAARA 211
|
250
....*....|..
gi 492309081 213 DHILHIENQELT 224
Cdd:COG1136 212 DRVIRLRDGRIV 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
315-463 |
1.07e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 315 DNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG---------ERKASELL--NIGYFAQHQ 383
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiQHYASKEVarRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 384 MDALDGHA-----------SPMLQLARIADKQISEATLRSfLGSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVL 452
Cdd:PRK10253 91 TTPGDITVqelvargryphQPLFTRWRKEDEEAVTKAMQA-TGITHLADQSVDT----LSGGQRQRAWIAMVLAQETAIM 165
|
170
....*....|.
gi 492309081 453 ILDEPTNHLDL 463
Cdd:PRK10253 166 LLDEPTTWLDI 176
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
342-462 |
1.16e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.27 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 342 LLGMNGAGKSTLIKSLVGDLPLLAGE-------------RKASELLNIGyfaqHQmDALDGHASPMLQL----ARIADKQ 404
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRvllnggpldfqrdSIARGLLYLG----HA-PGIKTTLSVLENLrfwhADHSDEQ 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 405 ISEATLRSFLGSFGfsgermDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:cd03231 106 VEEALARVGLNGFE------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
312-488 |
1.18e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 58.65 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP---------LLAGER---KASELLNIGY- 378
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsasgevLLNGRRltaLPAEQRRIGIl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 FaqhQMDALDGHASPMLQLA--------RIADKQISEATLRSfLGSFGFsGERmdTPcESFSGGERARLALALIVWQRPN 450
Cdd:COG4136 82 F---QDDLLFPHLSVGENLAfalpptigRAQRRARVEQALEE-AGLAGF-ADR--DP-ATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492309081 451 VLILDEPTNHLDLDMRHALSM----ALQDFEGAVVLVSHERQ 488
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfvfeQIRQRGIPALLVTHDEE 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
1.20e-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: 59.33 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLR----RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT------RPTGWTVAHMA 70
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 71 QEvKALdMP---AID---FVLsgdeefwdiqnklaqpdqltdfelaklhgrfdEIHGYSAPSKAAQLMA-----GLGFLE 139
Cdd:COG1116 87 QE-PAL-LPwltVLDnvaLGL--------------------------------ELRGVPKAERRERAREllelvGLAGFE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 140 N----QLrlnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAIL------WLEDWLKAYEGTLILISHDRD 206
Cdd:COG1116 133 DayphQL-------SGGMRQRVAIARALANDPEVLLMDEPFGA--LDALTrerlqdELLRLWQETGKTVLFVTHDVD 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-176 |
1.30e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.12 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT----RPTGWTVAHMAQEvkal 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVfdgkDITDWQTAKIMRE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 dmpAIDFVLSGDEEFwdiqnklaqpDQLTDFELAKLHGRFDEIHGYSapSKAAQLMAGLGFLENQLRLNVESFSGGWRMR 156
Cdd:PRK11614 81 ---AVAIVPEGRRVF----------SRMTVEENLAMGGFFAERDQFQ--ERIKWVYELFPRLHERRIQRAGTMSGGEQQM 145
|
170 180
....*....|....*....|
gi 492309081 157 LNLARTLMSRSDLLLLDEPT 176
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPS 165
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
312-485 |
1.45e-09 |
|
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: 58.14 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-RKASELLNIGYFAQHQMDALDGH 390
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEvRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 ASPMLQ----------LARI---ADKQISEAtlrsfLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILDE 456
Cdd:TIGR01189 81 LPGLKPelsalenlhfWAAIhggAQRTIEDA-----LAAVGLTG-FEDLPAAQLSAGQQRRLALArLWLSRRP-LWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 492309081 457 PTNHLD---LDMRHALSMALQDFEGAVVLVSH 485
Cdd:TIGR01189 154 PTTALDkagVALLAGLLRAHLARGGIVLLTTH 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
307-485 |
1.45e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----RKASELLNI------ 376
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhyrMRDGQLRDLyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 ----------GYFAQHQMDALDGHASpmlqlariADKQISE--------------ATLRSFLGSFGFSGERMDTPCESFS 432
Cdd:PRK11701 82 errrllrtewGFVHQHPRDGLRMQVS--------AGGNIGErlmavgarhygdirATAGDWLERVEIDAARIDDLPTTFS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 433 GGERARLALALIVWQRPNVLILDEPTNHLD-------LDMRHALsmaLQDFEGAVVLVSH 485
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGL---VRELGLAVVIVTH 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
312-504 |
1.48e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERKAS--ELL-NIGYFAQHQMDAld 388
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL-------LRLLAGLETPSagELLaGTAPLAEAREDT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 ghaSPMLQLARIA--DKQISEATL----------RSFLGSFGFSGERMDTPCeSFSGGERARLALALIVWQRPNVLILDE 456
Cdd:PRK11247 84 ---RLMFQDARLLpwKKVIDNVGLglkgqwrdaaLQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492309081 457 PTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-220 |
1.81e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 57.16 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRG-GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQevkaldmpa 80
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 idfvlsgdeefwdiqnklaqpdqltdfelaklhgrfdeiHGYSAPskaaqlmaglGFLENQLRLNVES-FSGGWRMRLNL 159
Cdd:cd03223 72 ---------------------------------------RPYLPL----------GTLREQLIYPWDDvLSGGEQQRLAF 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISHdRDFLDAITDHILHIEN 220
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.89e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.35 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGwKI-GLTGVNGAGKSTLFAALLGSLGADEGS-------LTRPTGWTVAHMAQE 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKG-EIfGLLGPNGAGKTTTIRIILGILAPDSGEvlwdgepLDPEDRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 73 vKAL--DMPAIdfvlsgdeefwdiqnklaqpDQLTDFelAKLhgrfdeiHGYS---APSKAAQLMAGLGfLENQLRLNVE 147
Cdd:COG4152 80 -RGLypKMKVG--------------------EQLVYL--ARL-------KGLSkaeAKRRADEWLERLG-LGDRANKKVE 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILIS-HDRDFLDAITDHIL 216
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaaKGTTVIFSsHQMELVEELCDRIV 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
330-491 |
1.90e-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: 58.19 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE------------RKASELL--NIGYFAQ-----HQMDALDGH 390
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngqdvsdlrGRAIPYLrrKIGVVFQdfrllPDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 ASPMlqlaRIADKQISEATLR--SFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:cd03292 100 AFAL----EVTGVPPREIRKRvpAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180
....*....|....*....|....*.
gi 492309081 469 LSMALQDFE--GAVVLVS-HERQLIA 491
Cdd:cd03292 175 IMNLLKKINkaGTTVVVAtHAKELVD 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-216 |
2.24e-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: 60.18 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 23 QLHPGWKIGLTGVNGAGKSTlFAALL-GSLGADEGSLtrPTGWTVAHMAQEVKA-LDMPAIDFVLSGDEEFWD---IQNK 97
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTT-FAKILaGVLKPDEGEV--DEDLKISYKPQYISPdYDGTVEEFLRSANTDDFGssyYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 98 LAQPdqltdfelaklhgrfdeihgysapskaaqlmagLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTN 177
Cdd:COG1245 439 IIKP---------------------------------LG-LEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492309081 178 HLDldailwLEDWLKA----------YEGTLILISHDRDFLDAITDHIL 216
Cdd:COG1245 485 HLD------VEQRLAVakairrfaenRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
312-504 |
2.41e-09 |
|
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: 58.02 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGD---------------LPLLAGERkasellNI 376
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFetptsgeilldgkdiTNLPPHKR------PV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GYFAQH-----QMDALDGHASPmLQLARIaDKQISEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNV 451
Cdd:cd03300 75 NTVFQNyalfpHLTVFENIAFG-LRLKKL-PKAEIKERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 452 LILDEPTNHLDLDMRHALS---MALQDFEG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
305-504 |
2.53e-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: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 305 TKMSSPLLTLDNASIGYGDK----QIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAGE------- 367
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPtsgtvRLAGQdlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 368 ------RKAsellNIGYFAQH-----QMDALDGHASPmLQLARIADkqiSEATLRSFLGSFGFsGERMD-TPCEsFSGGE 435
Cdd:COG4181 82 dararlRAR----HVGFVFQSfqllpTLTALENVMLP-LELAGRRD---ARARARALLERVGL-GHRLDhYPAQ-LSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQDFEGA-VVLVSHERQLiASVCDELLLVHGGK 504
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQiidLLFELNRERGTtLVLVTHDPAL-AARCDRVLRLRAGR 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
306-507 |
2.56e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.80 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 306 KMSSPLLTLDNasIGY--GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIK---SLV----GDLpLLAGERKASelLN- 375
Cdd:PRK10247 2 QENSPLLQLQN--VGYlaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKivaSLIsptsGTL-LFEGEDIST--LKp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 376 ------IGYFAQHQMDALDGHASPMLQLARIADKQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRP 449
Cdd:PRK10247 77 eiyrqqVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 450 NVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASvCDEL--LLVHGGKCTE 507
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIhryvREQNIAVLWVTHDKDEINH-ADKVitLQPHAGEMQE 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
310-508 |
3.12e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.12 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 310 PLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLvGDLPLLAGERKASEllNIGYFAQH------- 382
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG--RVEFFNQNiyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 ------------------QMDALDGHA--------SPMLQLARIADKQISEATLRSFLGSfgfsgeRMDTPCESFSGGER 436
Cdd:PRK14258 83 lnrlrrqvsmvhpkpnlfPMSVYDNVAygvkivgwRPKLEIDDIVESALKDADLWDEIKH------KIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 437 ARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHG-----GKCTE 507
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVE 236
|
.
gi 492309081 508 F 508
Cdd:PRK14258 237 F 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-203 |
3.26e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.12 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPTGWTVAHMAQEVKAL-DMPA 80
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIARGLLYLgHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLSGDE--EFWdiqnklaqpdqltdfelAKLHGRfdeihgysAPSKAAQLMAGLGFLENqlrLNVESFSGGWRMRLN 158
Cdd:cd03231 84 IKTTLSVLEnlRFW-----------------HADHSD--------EQVEEALARVGLNGFED---RPVAQLSAGQQRRVA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISH 203
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-224 |
3.74e-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: 57.44 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLR---RGGRV-LFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKAL 76
Cdd:COG4181 8 IIELRGLTKTvgtGAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG--------LDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DMPA--------IDFVlsgDEEFWDIQNKLAQPDQLTDFELAklhGRFDeihgysAPSKAAQLMA--GLGFLE----NQL 142
Cdd:COG4181 80 DEDArarlrarhVGFV---FQSFQLLPTLTALENVMLPLELA---GRRD------ARARARALLErvGLGHRLdhypAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 143 rlnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAYEG-TLILISHDRDfLDAITDHILHI 218
Cdd:COG4181 148 -------SGGEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNRERGtTLVLVTHDPA-LAARCDRVLRL 219
|
....*.
gi 492309081 219 ENQELT 224
Cdd:COG4181 220 RAGRLV 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-213 |
3.83e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 57.12 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR--RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPTGWTVAHMAQEV--KALD 77
Cdd:cd03244 3 IEFKNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIL-IDGVDISKIGLHDlrSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 M-PAIDFVLSGdeefwDIQNKLAQPDQLTDFELaklhgrfdeihgYSApSKAAQLMAGLGFLENQLRLNVES----FSGG 152
Cdd:cd03244 82 IiPQDPVLFSG-----TIRSNLDPFGEYSDEEL------------WQA-LERVGLKEFVESLPGGLDTVVEEggenLSVG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 153 WRMRLNLARTLMSRSDLLLLDEPTNHLDL--DAILW--LEDWLKAYegTLILISHdRdfLDAITD 213
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPetDALIQktIREAFKDC--TVLTIAH-R--LDTIID 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
4.88e-09 |
|
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: 55.90 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahmaqevkaldmpai 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 dfvlsgdeefwdiqnklaqpdqltdfelakLHGRfdEIHGYSaPSKAAQlmAGLGFLeNQLrlnvesfSGGWRMRLNLAR 161
Cdd:cd03216 59 ------------------------------VDGK--EVSFAS-PRDARR--AGIAMV-YQL-------SVGERQMVEIAR 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISHRLDEVFEIADRV 152
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
307-502 |
5.95e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIA-EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASELLNIG 377
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTAlRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgqptRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQHQ--------------MDALDGHASpMLQLARIADKQISEATLrsflgsfgfsgERMDT------PCESFSGGERA 437
Cdd:PRK15056 82 YVPQSEevdwsfpvlvedvvMMGRYGHMG-WLRRAKKRDRQIVTAAL-----------ARVDMvefrhrQIGELSGGQKK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 438 RLALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQDfEGAVVLVS-HERQLIASVCDELLLVHG 502
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEAriiSLLRELRD-EGKTMLVStHNLGSVTEFCDYTVMVKG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
312-511 |
7.19e-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: 58.66 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG------------------------DLPLLAGE 367
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyvERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 368 R-------KASELLNIGYFAQHQMDALDGHASPMLQ--LARIADKQISEATLRSfLGSFGFSGE---------------- 422
Cdd:TIGR03269 81 PcpvcggtLEPEEVDFWNLSDKLRRRIRKRIAIMLQrtFALYGDDTVLDNVLEA-LEEIGYEGKeavgravdliemvqls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 423 -RMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD---LDMRH-ALSMALQDFEGAVVLVSHERQLIASVCDEL 497
Cdd:TIGR03269 160 hRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHnALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....
gi 492309081 498 LLVHGGKCTEfEGD 511
Cdd:TIGR03269 240 IWLENGEIKE-EGT 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-229 |
7.38e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.79 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSltrptgwtVAHMAQEVkaldmpaidfvLSGDEEFW-----DIQ 95
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGE--------VAWLGKDL-----------LGMKDDEWravrsDIQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 96 NKLAQPdqltdfeLAKLHGR--------------FDEIHGYSAPSKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLAR 161
Cdd:PRK15079 102 MIFQDP-------LASLNPRmtigeiiaeplrtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIAR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 162 TLMSRSDLLLLDEPTNHLDLD----AILWLEDWLKAYEGTLILISHDRDFLDAITDHIlhienqeLTLYTGN 229
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSiqaqVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV-------LVMYLGH 239
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-205 |
8.66e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.17 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 12 GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKALD-MPAIDFVLSG--- 87
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGvIPQKVFIFSGtfr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 88 ----------DEEFWDIQNKLAQ-------PDQLtDFELakLHGRFDEIHGYSapskaaQLMAglgflenqlrlnvesfs 150
Cdd:cd03289 95 knldpygkwsDEEIWKVAEEVGLksvieqfPGQL-DFVL--VDGGCVLSHGHK------QLMC----------------- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 151 ggwrmrlnLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK-AYEGTLILISHDR 205
Cdd:cd03289 149 --------LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKqAFADCTVILSEHR 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
330-503 |
8.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDALDGHASPMLQLAriaDKQISEAT 409
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFP---ESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 410 LRSFLG----SFGFSGERMD-------------------TPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMR 466
Cdd:PRK13643 102 VLKDVAfgpqNFGIPKEKAEkiaaeklemvgladefwekSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492309081 467 ---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK13643 181 iemMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
307-507 |
9.11e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGY----GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP-----------LLAGER--K 369
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvypsgdiRFHGESllH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 370 ASELL-------NIGYFAQHQMDAL------DGHASPMLQLARIADKQISEATLRSFLGSFGF--SGERMDTPCESFSGG 434
Cdd:PRK15134 81 ASEQTlrgvrgnKIAMIFQEPMVSLnplhtlEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 435 ERARLALALIVWQRPNVLILDEPTNHLDL-----------DMRHALSMALqdfegavVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVsvqaqilqllrELQQELNMGL-------LFITHNLSIVRKLADRVAVMQNG 233
|
....
gi 492309081 504 KCTE 507
Cdd:PRK15134 234 RCVE 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
288-504 |
9.50e-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: 56.33 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 288 LAPAHVDTPFTF---SFREPTKmssplltldnasigyGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLL 364
Cdd:cd03248 3 LAPDHLKGIVKFqnvTFAYPTR---------------PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 365 AGERkaseLLNIGYFAQHQMDALDGHASPMLQ----------------LARIADKQISEATLRSFLGSF------GFSGE 422
Cdd:cd03248 68 GGQV----LLDGKPISQYEHKYLHSKVSLVGQepvlfarslqdniaygLQSCSFECVKEAAQKAHAHSFiselasGYDTE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 423 rMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVcDELLLV 500
Cdd:cd03248 144 -VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVERA-DQILVL 221
|
....
gi 492309081 501 HGGK 504
Cdd:cd03248 222 DGGR 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
312-514 |
9.61e-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: 56.19 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIaEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGERKasellNIG 377
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGfikpdsgkillngkDITNLPPEKR-----DIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQHQmdALDGHASPMLQLA-----RIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALA--LIVwqRPN 450
Cdd:cd03299 75 YVPQNY--ALFPHMTVYKNIAyglkkRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIAraLVV--NPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 451 VLILDEPTNHLDL----DMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD 514
Cdd:cd03299 150 ILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV-GKPEE 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
323-514 |
9.95e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 323 DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDL-------PLLAGERKASE--LLNIGYFAQHqmDALDGHAS- 392
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgTILANNRKPTKqiLKRTGFVTQD--DILYPHLTv 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 393 -------PMLQLARIADKQISEATLRSFLGSFGFsgermdTPCE------SF----SGGERARLALALIVWQRPNVLILD 455
Cdd:PLN03211 158 retlvfcSLLRLPKSLTKQEKILVAESVISELGL------TKCEntiignSFirgiSGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 456 EPTNHLDLDMRHALSMALQDF--EGAVVLVS-HE-RQLIASVCDELLLVHGGKCTeFEGDLQD 514
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLaqKGKTIVTSmHQpSSRVYQMFDSVLVLSEGRCL-FFGKGSD 293
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-219 |
1.02e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 57.46 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT--------------RPTGWtVA 67
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlppreRRVGF-VF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 68 -------HM--AQEVKA-LDmpaidfVLSGDEEfwDIQNKLAQpdQLTDFELAKLHGRFdeihgysaPSkaaqlmaglgf 137
Cdd:COG1118 82 qhyalfpHMtvAENIAFgLR------VRPPSKA--EIRARVEE--LLELVQLEGLADRY--------PS----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 138 lenQLrlnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAIL------WLEDWLKAYEGTLILISHDRDflDA- 210
Cdd:COG1118 133 ---QL-------SGGQRQRVALARALAVEPEVLLLDEPFGA--LDAKVrkelrrWLRRLHDELGGTTVFVTHDQE--EAl 198
|
250
....*....|....*
gi 492309081 211 -ITDHIL-----HIE 219
Cdd:COG1118 199 eLADRVVvmnqgRIE 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
341-561 |
1.06e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 341 GLLGMNGAGKSTLIKSLVGDLPLLAGERK-------ASEL---LNIGYFAQ----------HQmdALDGHAspmlQLARI 400
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpvdAGDIatrRRVGYMSQafslygeltvRQ--NLELHA----RLFHL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 401 ADKQISEAtLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD---LDM--RHALSMALQD 475
Cdd:NF033858 370 PAAEIAAR-VAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvaRDMfwRLLIELSRED 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 476 feGAVVLVS-H-----ERqliasvCDELLLVHGGKCTEfegdlQDYAKWLREARqqqiNAQT-----------AVAQNNS 538
Cdd:NF033858 448 --GVTIFIStHfmneaER------CDRISLMHAGRVLA-----SDTPAALVAAR----GAATleeafiayleeAAGAAAA 510
|
250 260
....*....|....*....|...
gi 492309081 539 SSAAPAPAKVDKEAQRKEAARRR 561
Cdd:NF033858 511 PAAAAAPAAAAAAPAAPAPAPRR 533
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
431-507 |
1.08e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.28 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 431 FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQ-DFEGAVVLVSHERQLIASVCDELLLVHGGKCT 506
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnLMMDLQqELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
.
gi 492309081 507 E 507
Cdd:PRK11308 235 E 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-211 |
1.09e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsltrptgwtvahmaqevKALDMPAIDFVLS 86
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG------------------------ALKGTPVAGCVDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 87 GDEEFWDIQNKLAQPDQLTDFELAK--LHgrfdeihgysapskaaqlMAGLGflENQL-RLNVESFSGGWRMRLNLARTL 163
Cdd:COG2401 92 PDNQFGREASLIDAIGRKGDFKDAVelLN------------------AVGLS--DAVLwLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492309081 164 MSRSDLLLLDEPTNHLDLD-----AILWLEDWLKAyEGTLILISHDRDFLDAI 211
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQtakrvARNLQKLARRA-GITLVVATHHYDVIDDL 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-216 |
1.12e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 23 QLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrpTGWTVAHMAQEVKAldmpaidfvlsgdeefwdiqnklAQPD 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYIKP-----------------------DYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 103 QLTDFeLAKLHGRFDEIHGYSapskaaQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDld 182
Cdd:PRK13409 416 TVEDL-LRSITDDLGSSYYKS------EIIKPLQ-LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-- 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 183 ailwLEDWLKA----------YEGTLILISHDRDFLDAITDHIL 216
Cdd:PRK13409 486 ----VEQRLAVakairriaeeREATALVVDHDIYMIDYISDRLM 525
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-188 |
1.17e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.54 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT-----------RPTGWTVAHM 69
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 70 AQEVkaldmpAIDFVLSGDeefwdiqnklaqpdQLTDFELAKLHGRFDEiHGYSAPSKAAQLMAGLGFLENQLRlNVESF 149
Cdd:PRK09536 83 PQDT------SLSFEFDVR--------------QVVEMGRTPHRSRFDT-WTETDRAAVERAMERTGVAQFADR-PVTSL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD-AILWLE 188
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINhQVRTLE 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-220 |
1.21e-08 |
|
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: 55.55 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTgwTVAHMAQEvkALDMPA-----IDFVLSGDEEFWD-- 93
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQE--PWIQNGtirenILFGKPFDEERYEkv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 94 IQNKLAQPDqltdfeLAKL-HGRFDEIHgysapskaaqlmaglgflENQLRLnvesfSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:cd03250 101 IKACALEPD------LEILpDGDLTEIG------------------EKGINL-----SGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 173 DEP--------TNHLDLDAIlwLEDWLKayEGTLILISHDRDFLdAITDHILHIEN 220
Cdd:cd03250 152 DDPlsavdahvGRHIFENCI--LGLLLN--NKTRILVTHQLQLL-PHADQIVVLDN 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
340-542 |
1.38e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVGDLPLLAGE---------------------------RKASELLnIGYFAQHQMD--ALDGH 390
Cdd:PRK10762 281 LGVSGLMGAGRTELMKVLYGALPRTSGYvtldghevvtrspqdglangivyisedRKRDGLV-LGMSVKENMSltALRYF 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 ASPMLQLARIADKQiseaTLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALS 470
Cdd:PRK10762 360 SRAGGSLKHADEQQ----AVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 471 MALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGK-CTEFEgdlqdyakwLREARQQQINAqTAVAQNNSSSAA 542
Cdd:PRK10762 436 QLINQFkaEGlSIILVSSEMPEVLGMSDRILVMHEGRiSGEFT---------REQATQEKLMA-AAVGKLNRVNQE 501
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
307-462 |
1.39e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 56.56 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGD--KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELL---------- 374
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 -NIGYFAQH----------QMD---ALDGHASPMLQLARIADKQISEATLRSFLgsfgfsgermDTPCESFSGGERARLA 440
Cdd:PRK13635 81 rQVGMVFQNpdnqfvgatvQDDvafGLENIGVPREEMVERVDQALRQVGMEDFL----------NREPHRLSGGQKQRVA 150
|
170 180
....*....|....*....|..
gi 492309081 441 LALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLD 172
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-203 |
1.54e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTgwtvahmAQEVKALDMPa 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG--------LARPD-------AGEVLWQGEP- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 idfVLSGDEEFwdiQNKLA----QP---DQLTDFE----LAKLHGRFDEihgysapSKAAQLMAGLGfLENQLRLNVESF 149
Cdd:PRK13538 65 ---IRRQRDEY---HQDLLylghQPgikTELTALEnlrfYQRLHGPGDD-------EALWEALAQVG-LAGFEDVPVRQL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISH 203
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
1.61e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.53 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLfqKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT-------------RPtgwtVA 67
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwngqdltalppaeRP----VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 68 HMAQEvkaldmpaidfvlsgDEEFW--DIQNKLA---QPD-QLTDFELAKLHgrfdeihgysapsKAAQLMaGLGFLENQ 141
Cdd:COG3840 75 MLFQE---------------NNLFPhlTVAQNIGlglRPGlKLTAEQRAQVE-------------QALERV-GLAGLLDR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 142 LRlnvESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLKAYEGTLILISHDRDflDA--ITDHI 215
Cdd:COG3840 126 LP---GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPE--DAarIADRV 200
|
....*
gi 492309081 216 LHIEN 220
Cdd:COG3840 201 LLVAD 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-216 |
1.81e-08 |
|
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: 55.65 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRG-GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL----TRPTGWTV-------AHM 69
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgTDINKLKGkalrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 70 A---QEVKALD-MPAIDFVLSGdeefwdiqnKLAQpdqlTDFeLAKLHGRFDEIHGYsapsKAAQLMAGLGFLEnQLRLN 145
Cdd:cd03256 81 GmifQQFNLIErLSVLENVLSG---------RLGR----RST-WRSLFGLFPKEEKQ----RALAALERVGLLD-KAYQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 146 VESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILIS-HDRDFLDAITDHIL 216
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREYADRIV 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
307-485 |
1.92e-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: 55.87 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGY----GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLNI 376
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptsgevLVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GY-FAQHQ----MDALD----GhaspmLQLARIADKQIsEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALA--LIV 445
Cdd:COG1116 83 GVvFQEPAllpwLTVLDnvalG-----LELRGVPKAER-RERARELLELVGLAGFEDAYPHQ-LSGGMRQRVAIAraLAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 446 wqRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSH 485
Cdd:COG1116 156 --DPEVLLMDEPFGALDaltrERLQDELLRLWQETGKTVLFVTH 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-204 |
2.29e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.17 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 26 PGWKIGLTGVNGAGKSTLFAALLGslgADEGSL--TRPTGWTVAHMAQEVKA-LDMPAIDFVLsgdeefwdiQNKLAQP- 101
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAG---LDDGSSgeVSLVGQPLHQMDEEARAkLRAKHVGFVF---------QSFMLIPt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 102 -DQLTDFEL-AKLHGRFDEihgySAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:PRK10584 103 lNALENVELpALLRGESSR----QSRNGAKALLEQLG-LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180
....*....|....*....|....*....
gi 492309081 180 DLDAILWLEDWL----KAYEGTLILISHD 204
Cdd:PRK10584 178 DRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
321-526 |
2.39e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIK--------------------SLVGDL--PLLAGERKASELLN--I 376
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegsivvngqtiNLVRDKdgQLKVADKNQLRLLRtrL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 377 GYFAQH-----QMDALDGHASPMLQLARIADKQISEATLRsFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNV 451
Cdd:PRK10619 95 TMVFQHfnlwsHMTVLENVMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 452 LILDEPTNHLDLDMRHALSMALQDF--EG-AVVLVSHERQLIASVCDELLLVHGGKCTEfEGDLQDYAKWLREARQQQ 526
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHEMGFARHVSSHVIFLHQGKIEE-EGAPEQLFGNPQSPRLQQ 250
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-204 |
2.71e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLrrGGRVlfQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGsLGADEGSLT---RP-TGWTVAHMA------- 70
Cdd:COG4138 1 LQLNDVAV--AGRL--GPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILlngRPlSDWSAAELArhrayls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 71 -QEVKALDMPAIDFvLSgdeefwdiqnkLAQPDQLTDFELAKLhgrfdeihgysapskAAQLMAGLGfLENQLRLNVESF 149
Cdd:COG4138 76 qQQSPPFAMPVFQY-LA-----------LHQPAGASSEAVEQL---------------LAQLAEALG-LEDKLSRPLTQL 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 150 SGGWRMRLNLARTLM-------SRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISHD 204
Cdd:COG4138 128 SGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
332-502 |
2.74e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 332 LQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDALDGHASPMLQLARIADKQISEATLr 411
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLNAVGLSDAVL- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 412 sFLGSFgfsgermdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHER 487
Cdd:COG2401 130 -WLRRF-----------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarraGITLVVATHHY 197
|
170
....*....|....*
gi 492309081 488 QLIASVCDELLLVHG 502
Cdd:COG2401 198 DVIDDLQPDLLIFVG 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
340-504 |
3.12e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 54.58 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVGDLP---------LLAG-ERKASELL-NIGYFAQHQmDALDG-------HASPMLQLARI- 400
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVEgggttsgqiLFNGqPRKPDQFQkCVAYVRQDD-ILLPGltvretlTYTAILRLPRKs 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 401 ---ADKQISEATLRSFLGSFGFSGERMdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF- 476
Cdd:cd03234 115 sdaIRKKRVEDVLLRDLALTRIGGNLV----KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLa 190
|
170 180 190
....*....|....*....|....*....|.
gi 492309081 477 -EGAVVLVS-HE-RQLIASVCDELLLVHGGK 504
Cdd:cd03234 191 rRNRIVILTiHQpRSDLFRLFDRILLLSSGE 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-202 |
3.40e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSltrptgwtVAHMAQEV-KALDMP 79
Cdd:PRK15056 7 IVVNDVTVTwRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGK--------ISILGQPTrQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 AIDFVLSGDEEFWDIqnklaqPDQLTDFELAKLHGRFDEIHGYSAPSKA--AQLMAGLGFLENQLRlNVESFSGGWRMRL 157
Cdd:PRK15056 79 LVAYVPQSEEVDWSF------PVLVEDVVMMGRYGHMGWLRRAKKRDRQivTAALARVDMVEFRHR-QIGELSGGQKKRV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 158 NLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAyEGTLILIS 202
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRD-EGKTMLVS 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-507 |
4.25e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahmaqeVKALDMPA 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-------------INNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLSGDEEFWDIQNKLAQPDQLTDFE---LAKLHGR----FDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGW 153
Cdd:PRK09700 72 LDHKLAAQLGIGIIYQELSVIDELTVLEnlyIGRHLTKkvcgVNIIDWREMRVRAAMMLLRVG-LKVDLDEKVANLSISH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 154 RMRLNLARTLMSRSDLLLLDEPTNHL---DLDAILWLEDWLKAyEGTLIL-ISHDRDFLDAITDHILHIENQElTLYTGN 229
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRK-EGTAIVyISHKLAEIRRICDRYTVMKDGS-SVCSGM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 230 YSTFETTRSERLAQqqqafekqqetrahlqkfidrfkakatkARQAQSRIKQLermqQLAPAHVDTPFTFSFREPTKMss 309
Cdd:PRK09700 229 VSDVSNDDIVRLMV----------------------------GRELQNRFNAM----KENVSNLAHETVFEVRNVTSR-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 310 plltldnasigygDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RKASELL----NIG 377
Cdd:PRK09700 275 -------------DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEirlngkdiSPRSPLDavkkGMA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQHQMDALDGHASPMLQLARIAdKQISEATLRSFLGSFGFSGER---------MDTPCES-------FSGGERARLAL 441
Cdd:PRK09700 342 YITESRRDNGFFPNFSIAQNMAIS-RSLKDGGYKGAMGLFHEVDEQrtaenqrelLALKCHSvnqniteLSGGNQQKVLI 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 442 ALIVWQRPNVLILDEPTNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKaeiYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
312-565 |
4.42e-08 |
|
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: 56.46 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGY--GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLvgdLPLLAGE------------------RKAS 371
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSTEgeiqidgvswnsvtlqtwRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 372 ELL--NIGYFAQHQMDALDGHAspmlqlaRIADKQI----SEATLRSFLGSFGfsgERMDTPCES----FSGGERARLAL 441
Cdd:TIGR01271 1295 GVIpqKVFIFSGTFRKNLDPYE-------QWSDEEIwkvaEEVGLKSVIEQFP---DKLDFVLVDggyvLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 442 ALIVWQRPNVLILDEPTNHLDLDMRHALSMAL-QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFEG--DLQDYAKW 518
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSiqKLLNETSL 1444
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 492309081 519 LREARQQQINAQTAVAQNNSSSAAPAPAKVdkEAQRKEAARRREQTR 565
Cdd:TIGR01271 1445 FKQAMSAADRLKLFPLHRRNSSKRKPQPKI--TALREEAEEEVQNTR 1489
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
307-514 |
4.54e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.85 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEK-IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----------RKASELL 374
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKgININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilfdgkpidysRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 --NIGYFAQ---HQMDAL----DGHASPM-LQLAriaDKQISEaTLRSFLGSFGFSGERmDTPCESFSGGERARLALALI 444
Cdd:PRK13636 81 reSVGMVFQdpdNQLFSAsvyqDVSFGAVnLKLP---EDEVRK-RVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 445 VWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTeFEGDLQD 514
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKE 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
321-504 |
4.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.70 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEK-IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER---KASELLN----IGYFAQHQMDA 386
Cdd:PRK13639 11 YPDGTEALKgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKptsgevLIKGEPikyDKKSLLEvrktVGIVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 387 L-------DGHASPM-LQLariaDKQISEATLRSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPT 458
Cdd:PRK13639 91 LfaptveeDVAFGPLnLGL----SKEEVEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492309081 459 NHLDLDMRHALSMALQDF--EGAVVLVS-HERQLIASVCDELLLVHGGK 504
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLnkEGITIIIStHDVDLVPVYADKVYVMSDGK 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-219 |
4.69e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.61 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLG-------SLGADEGSLTRPTGWTVAHMA--- 70
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfykptggTILLRGQHIEGLPGHQIARMGvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 71 --QEVKAL-DMPAIDFVLsgdeefwdiqnkLAQPDQL-TDFelakLHGRFdEIHGY-----SAPSKAAQLMAGLGFLENQ 141
Cdd:PRK11300 85 tfQHVRLFrEMTVIENLL------------VAQHQQLkTGL----FSGLL-KTPAFrraesEALDRAATWLERVGLLEHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 142 LRlNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL------DLDAILwleDWLKAYEG-TLILISHDRDFLDAITDH 214
Cdd:PRK11300 148 NR-QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnpketkELDELI---AELRNEHNvTVLLIEHDMKLVMGISDR 223
|
....*
gi 492309081 215 ILHIE 219
Cdd:PRK11300 224 IYVVN 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
307-507 |
4.78e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGY-GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE-----RKASEL------- 373
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEirldgRPLSSLshsvlrq 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 374 -----------LNIGYFA----------QHQMDALDghaspMLQLARIAdKQISEAtLRSFLGSFGfsgermdtpcESFS 432
Cdd:PRK10790 416 gvamvqqdpvvLADTFLAnvtlgrdiseEQVWQALE-----TVQLAELA-RSLPDG-LYTPLGEQG----------NNLS 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 433 GGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVSHERQLIASVcDELLLVHGGKCTE 507
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEA-DTILVLHRGQAVE 554
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
261-491 |
4.84e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.97 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 261 FIDRFKA----KATKARQA--QSRIKQLERMQQLAPA-HVDTPFTFSFREptkmssplLTLDNASigygDKQIAEKIRLQ 333
Cdd:COG4178 318 FVDNYQSlaewRATVDRLAgfEEALEAADALPEAASRiETSEDGALALED--------LTLRTPD----GRPLLEDLSLS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 334 ITPNSRIGLLGMNGAGKSTLIKSLVG---------DLPllagerKASELLnigYFAQHqmdaldghasPMLQLARIAD-- 402
Cdd:COG4178 386 LKPGERLLITGPSGSGKSTLLRAIAGlwpygsgriARP------AGARVL---FLPQR----------PYLPLGTLREal 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 403 ------KQISEATLRSFLGSFGFSG--ERMDTPC---ESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSM 471
Cdd:COG4178 447 lypataEAFSDAELREALEAVGLGHlaERLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
250 260
....*....|....*....|..
gi 492309081 472 ALQD--FEGAVVLVSHERQLIA 491
Cdd:COG4178 527 LLREelPGTTVISVGHRSTLAA 548
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
311-503 |
5.00e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIgyfaqhqmdALDG- 389
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDV---------TLNGe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 390 --HASPMLQLAR------------------------------------IADKQISEATLrSFLGSFGFSGERMDTpcesF 431
Cdd:PRK13547 72 plAAIDAPRLARlravlpqaaqpafafsareivllgrypharragaltHRDGEIAWQAL-ALAGATALVGRDVTT----L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 432 SGGERARLALALIVWQ---------RPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELL 498
Cdd:PRK13547 147 SGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAARHADRIA 226
|
....*
gi 492309081 499 LVHGG 503
Cdd:PRK13547 227 MLADG 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-203 |
6.61e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---TRPTgwTVAHMAQEVKALD-MPAID 82
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTA--TRGDRSRFMAYLGhLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 83 FVLSGDEEFwdiqnklaqpdqltdFELAKLHGRfdeiHGYSAPSKAAQLMaGLGFLENQLrlnVESFSGGWRMRLNLART 162
Cdd:PRK13543 95 ADLSTLENL---------------HFLCGLHGR----RAKQMPGSALAIV-GLAGYEDTL---VRQLSAGQKKRLALARL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISH 203
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
330-560 |
7.29e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---RKASELLNIGYFAQHQMDALDGHASPMLQLArIADKQIS 406
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTvdiKGSAALIAISSGLNGQLTGIENIELKGLMMG-LTKEKIK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 407 EATLRSFlgSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEptnhldldmrhALSMALQDFEG-------- 478
Cdd:PRK13545 122 EIIPEII--EFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE-----------ALSVGDQTFTKkcldkmne 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 479 ------AVVLVSHERQLIASVCDELLLVHGGKCTEFeGDLQD----YAKWLREA-----------RQQQINA-QTAVAQN 536
Cdd:PRK13545 189 fkeqgkTIFFISHSLSQVKSFCTKALWLHYGQVKEY-GDIKEvvdhYDEFLKKYnqmsveerkdfREEQISQfQHGLLQE 267
|
250 260
....*....|....*....|....
gi 492309081 537 NSSSAAPAPAKVDKEAQRKEAARR 560
Cdd:PRK13545 268 DQTGRERKRKKGKKTSRKFKKKRV 291
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-232 |
7.71e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.24 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 13 GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgADEGSLTrptgwtVAhmAQEVKALDMPAIDFVLSgdeefW 92
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLK------IN--GIELRELDPESWRKHLS-----W 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 93 DIQN-KLAQPDQLTDFELAKLHGRFDEIHGYSAPSKAA----QLMAGLGFL--ENQLRLnvesfSGGWRMRLNLARTLMS 165
Cdd:PRK11174 428 VGQNpQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSeflpLLPQGLDTPigDQAAGL-----SVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 166 RSDLLLLDEPTNHLDLDA-ILWLEDWLKAYEG-TLILISHDRDFLDAItDHILHIENQELtLYTGNYST 232
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSeQLVMQALNAASRRqTTLMVTHQLEDLAQW-DQIWVMQDGQI-VQQGDYAE 569
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
149-511 |
8.68e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.08 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD--LDA-ILWLEDWLKAYEGT-LILISHD----RDFldaiTDHILHIEN 220
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqILDLLKDLQRELGMaLLLITHDlgvvRRF----ADRVAVMRQ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 221 QELTlytgnystfETTRSERLaqqqqafekqqetrahlqkfidrFKAkatkARQAQSRiKQLERMQQLAPAHVDTPftfs 300
Cdd:COG4172 233 GEIV---------EQGPTAEL-----------------------FAA----PQHPYTR-KLLAAEPRGDPRPVPPD---- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 301 freptkmSSPLLTLDNASIGY-----------GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERK 369
Cdd:COG4172 272 -------APPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPSEGE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 370 AsellnigYFAQHQMDALDGHA-------------------SPMLQLARI-----------ADKQISEATLRSFLGSFGF 419
Cdd:COG4172 342 I-------RFDGQDLDGLSRRAlrplrrrmqvvfqdpfgslSPRMTVGQIiaeglrvhgpgLSAAERRARVAEALEEVGL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 420 SGERMDT-PCEsFSGGERARLALA--LIVwqRPNVLILDEPTNHLDLDMRH---ALSMALQDFEG-AVVLVSHERQLIAS 492
Cdd:COG4172 415 DPAARHRyPHE-FSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDVSVQAqilDLLRDLQREHGlAYLFISHDLAVVRA 491
|
410
....*....|....*....
gi 492309081 493 VCDELLLVHGGKCTEfEGD 511
Cdd:COG4172 492 LAHRVMVMKDGKVVE-QGP 509
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
312-507 |
8.72e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 55.17 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIA-EKIRLQITPNSRIGLLGMNGAGKSTLIKslvgdlpLLAGERKASE---LL---NIgyfAQHQM 384
Cdd:COG1132 340 IEFENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVN-------LLLRFYDPTSgriLIdgvDI---RDLTL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 385 DALDGHASPMLQLA-----------RIADKQISEATLRS---------FLGSF--GFsgermDTPCE----SFSGGERAR 438
Cdd:COG1132 410 ESLRRQIGVVPQDTflfsgtireniRYGRPDATDEEVEEaakaaqaheFIEALpdGY-----DTVVGergvNLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 439 LALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF-EGA-VVLVSHeRqlIASV--CDELLLVHGGKCTE 507
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLmKGRtTIVIAH-R--LSTIrnADRILVLDDGRIVE 554
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-226 |
8.72e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 53.05 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEG-------SLTRPTGWTVAHMAQEVK 74
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGevlfdgkPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 75 aldmpaidfvLSGDEEFWDIQNKLAQpdqltdfelaklhgrfdeIHGYS---APSKAAQLMAGLGfLENQLRLNVESFSG 151
Cdd:cd03269 81 ----------LYPKMKVIDQLVYLAQ------------------LKGLKkeeARRRIDEWLERLE-LSEYANKRVEELSK 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDW---LKAYEGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
322-490 |
9.88e-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: 55.14 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIaEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDAL----DGHASPMLQL 397
Cdd:TIGR00954 464 GDVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgtlrDQIIYPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 398 ARIaDKQISEATLRSFL------------GSFGFSGERMDTpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:TIGR00954 543 DMK-RRGLSDKDLEQILdnvqlthilereGGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|....*
gi 492309081 466 RHALSMALQDFEGAVVLVSHERQLI 490
Cdd:TIGR00954 618 EGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-223 |
1.02e-07 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 53.66 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALDmPAIDFVLSGDEE--FWD----- 93
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLG--------LEKPAQGTVSFRGQDLYQLD-RKQRRAFRRDVQlvFQDspsav 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 94 -----IQNKLAQP-DQLTDFELAKLHGRfdeihgysapskAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTLMSRS 167
Cdd:TIGR02769 102 nprmtVRQIIGEPlRHLTSLDESEQKAR------------IAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 168 DLLLLDEPTNHLDL---DAILWLEDWLKAYEGT-LILISHDRDFLDAITDHILHIENQEL 223
Cdd:TIGR02769 170 KLIVLDEAVSNLDMvlqAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
307-489 |
1.14e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIA----EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPL-------------LAGER 368
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQtdvlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTsgdvifngqpmskLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 369 KAsELLN--IGYFAQ-HQM----DALDGHASPMLqlarIADKQISEATLRSF--LGSFGFSGERMDTPCEsFSGGERARL 439
Cdd:PRK11629 81 KA-ELRNqkLGFIYQfHHLlpdfTALENVAMPLL----IGKKKPAEINSRALemLAAVGLEHRANHRPSE-LSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492309081 440 ALALIVWQRPNVLILDEPTNHLDL---DMRHALSMALQDFEG-AVVLVSHERQL 489
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGtAFLVVTHDLQL 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-219 |
1.14e-07 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 52.68 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 30 IGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQ----EVKALDMP----AIDFVLSGDEEF--WDIQNKLA 99
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAG--------LEKPDGGTIVLNGTvlfdSRKKINLPpqqrKIGLVFQQYALFphLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 100 qpdqltdFELAKLHGRFDEIhgysapsKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:cd03297 98 -------FGLKRKRNREDRI-------SVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 180 D----LDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIE 219
Cdd:cd03297 163 DralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
322-462 |
1.16e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.57 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG----ERKASELLNIG---YFAQHQmDALDGHASPM 394
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtiklDGGDIDDPDVAeacHYLGHR-NAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 395 LQL---ARI---ADKQISEAtlrsfLGSFGFSGeRMDTPCESFSGGERARLALA-LIVWQRPnVLILDEPTNHLD 462
Cdd:PRK13539 92 ENLefwAAFlggEELDIAAA-----LEAVGLAP-LAHLPFGYLSAGQKRRVALArLLVSNRP-IWILDEPTAALD 159
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-462 |
1.19e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.55 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 342 LLGMNGAGKSTLIKSLVGDLP------LLAGErkasellNIGYFAQHQ---------MDALDGHASPM-----LQLA--- 398
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPpdsgsiLIDGK-------DVTKLPEYKrakyigrvfQDPMMGTAPSMtieenLALAyrr 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 399 ------RIADKQISEATLRSFLGSFGFSGE-RMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:COG1101 110 gkrrglRRGLTKKRRELFRELLATLGLGLEnRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
303-504 |
1.25e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.07 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 303 EPTKMSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLLAGER 368
Cdd:PRK11607 11 KTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeqptagqimldgvDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 369 KASELLNIGYfaqhqmdALDGHASPMLQLA------RIADKQISE--ATLRSFLGSFGFSGERmdtPcESFSGGERARLA 440
Cdd:PRK11607 91 RPINMMFQSY-------ALFPHMTVEQNIAfglkqdKLPKAEIASrvNEMLGLVHMQEFAKRK---P-HQLSGGQRQRVA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 441 LALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAV----VLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvtcVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
307-458 |
1.34e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSlvgdlplLAGERKASELLNIgyfaqhqmda 386
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGT-------LCGDPRATSGRIV---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 387 LDGHASPMLQLARI------------------------------ADKQISEATLRSFLGSFGFSGERMDTPCESFSGGER 436
Cdd:PRK11614 64 FDGKDITDWQTAKImreavaivpegrrvfsrmtveenlamggffAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQ 143
|
170 180
....*....|....*....|..
gi 492309081 437 ARLALALIVWQRPNVLILDEPT 458
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-205 |
1.39e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVS-LRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTG---WTVAHMAQEVKAL 76
Cdd:PRK10908 1 MIRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--------IERPSAgkiWFSGHDITRLKNR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DMPAI---------DFVLSGDEEFWDiqnKLAQPDQltdfelaklhgrfdeIHGYSAPSKAAQLMAGL---GFLENQLRL 144
Cdd:PRK10908 73 EVPFLrrqigmifqDHHLLMDRTVYD---NVAIPLI---------------IAGASGDDIRRRVSAALdkvGLLDKAKNF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 145 NVEsFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDlDAIlwLEDWLKAYEG------TLILISHDR 205
Cdd:PRK10908 135 PIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-DAL--SEGILRLFEEfnrvgvTVLMATHDI 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-211 |
1.49e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.14 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 7 VSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGadegslTRPTGWTVAHMAQEVkaLDMPaidfvls 86
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPK------YEVTEGEILFKGEDI--TDLP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 87 gdeefwdiqnklaqPDqltdfELAKLhGRF------DEIHGYSapskaaqlmaglgfLENQLR-LNvESFSGGWRMRLNL 159
Cdd:cd03217 71 --------------PE-----ERARL-GIFlafqypPEIPGVK--------------NADFLRyVN-EGFSGGEKKRNEI 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 160 ARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGT-LILISHDRDFLDAI 211
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreEGKsVLIITHYQRLLDYI 170
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-223 |
1.78e-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: 52.41 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVL-FQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtRPTGWTVAHMAQEVKALDMPA 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI-RVNGQDVSDLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDFVLsgdeefwdiQNKLAQPDqLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLA 160
Cdd:cd03292 80 IGVVF---------QDFRLLPD-RNVYENVAFALEVTGVPPREIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 161 RTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYE--GTLILIS-HDRDFLDAITDHILHIENQEL 223
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
312-512 |
1.89e-07 |
|
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: 52.65 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGD-----------------LPLLAGER------ 368
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsyevtsgtilfkgqdlLELEPDERaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 369 ------------KASELLNIGYFAQHQMDALDghASPMLQLARIADK-----QISEATLRSFLGsfgfsgermdtpcESF 431
Cdd:TIGR01978 81 lafqypeeipgvSNLEFLRSALNARRSARGEE--PLDLLDFEKLLKEklallDMDEEFLNRSVN-------------EGF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 432 SGGERAR---LALALIvwqRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLIASVC-DELLLVHGGK 504
Cdd:TIGR01978 146 SGGEKKRneiLQMALL---EPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKpDYVHVLLDGR 222
|
....*...
gi 492309081 505 CTEfEGDL 512
Cdd:TIGR01978 223 IVK-SGDV 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
322-485 |
1.96e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE--------RK-----ASELLNIGyfaqHQmDALD 388
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEvlwqgepiRRqrdeyHQDLLYLG----HQ-PGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 389 GHASPM--LQ-LARIADKQiSEATLRSFLGSFGFSGeRMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDldm 465
Cdd:PRK13538 87 TELTALenLRfYQRLHGPG-DDEALWEALAQVGLAG-FEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID--- 161
|
170 180
....*....|....*....|....*.
gi 492309081 466 RHALSMALQDFE------GAVVLVSH 485
Cdd:PRK13538 162 KQGVARLEALLAqhaeqgGMVILTTH 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-495 |
2.00e-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: 53.13 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP---------LLAGER----KASELLN-----IGYFAQHQMDALDgha 391
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgitsgeiLFDGEDllklSEKELRKirgreIQMIFQDPMTSLN--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 392 sP----------MLQLARIADKQISEATLRSFLGSFGFSG--ERMDT-PCEsFSGGERAR--LALALIVwqRPNVLILDE 456
Cdd:COG0444 101 -PvmtvgdqiaePLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRyPHE-LSGGMRQRvmIARALAL--EPKLLIADE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492309081 457 PTNHLDLDMRH---ALSMALQD-FEGAVVLVSHERQLIASVCD 495
Cdd:COG0444 177 PTTALDVTIQAqilNLLKDLQReLGLAILFITHDLGVVAEIAD 219
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-203 |
2.27e-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: 53.98 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRG-GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLG---------SLGA------DEGSLTRptgwT 65
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGffqarsgeiLLNGfslkdiDRHTLRQ----F 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 66 VAHMAQEVKALDMPAIDFVLSGDEEfwdiqnKLAQPDQLTDFELAKLHgrfDEIHGYSapskaaqlmagLGFlenQLRLN 145
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGAKE------NVSQDEIWAACEIAEIK---DDIENMP-----------LGY---QTELS 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 146 VESF--SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLdaIL---WLEDWLKAYEGTLILISH 203
Cdd:TIGR01193 607 EEGSsiSGGQKQRIALARALLTDSKVLILDESTSNLDT--ITekkIVNNLLNLQDKTIIFVAH 667
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
323-504 |
2.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.91 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 323 DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkaselLNIgyfAQHQMDALDGHAS---------- 392
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGT------ITI---AGYHITPETGNKNlkklrkkvsl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 393 ----PMLQLAR---------------IADKQISEATLRsFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLI 453
Cdd:PRK13641 90 vfqfPEAQLFEntvlkdvefgpknfgFSEDEAKEKALK-WLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492309081 454 LDEPTNHLDLDMRHALSMALQDFEGA---VVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
312-486 |
2.60e-07 |
|
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: 51.87 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-----DLPLLAGERKASEL----LNIGYFAQH 382
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGleeptSGRIYIGGRDVTDLppkdRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 -----QMDALDGHASPmLQLaRIADKQISEATLRSFLGSFGFSgERMDTPCESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:cd03301 81 yalypHMTVYDNIAFG-LKL-RKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|...
gi 492309081 458 TNHLD----LDMRHALSMALQDFEGAVVLVSHE 486
Cdd:cd03301 158 LSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-526 |
3.15e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.31 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 323 DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP----LLAGERKASEL------LNIGYFAQhqmDALDGHAS 392
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgsLKINGIELRELdpeswrKHLSWVGQ---NPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 393 PM--LQLAR--IADKQISEATLRSFLGSFGFSGER-MDTPCE----SFSGGERARLALALIVWQRPNVLILDEPTNHLDL 463
Cdd:PRK11174 439 LRdnVLLGNpdASDEQLQQALENAWVSEFLPLLPQgLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 464 DMRHALSMALQD--FEGAVVLVSHERQLIASvCDELLLVHGGKCTEfEGDLQD-------YAKWLREARQQQ 526
Cdd:PRK11174 519 HSEQLVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ-QGDYAElsqagglFATLLAHRQEEI 588
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
334-509 |
3.25e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 334 ITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------------RKASELL-------------NIGYFAQHQm 384
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRimiddcdvakfgltdlRRVLSIIpqspvlfsgtvrfNIDPFSEHN- 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 385 dalDGHASPMLQLARIADkqiseATLRSflgSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLD 464
Cdd:PLN03232 1338 ---DADLWEALERAHIKD-----VIDRN---PFGLDAEVSEGG-ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492309081 465 MRHALSMAL-QDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEFE 509
Cdd:PLN03232 1406 TDSLIQRTIrEEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-180 |
3.25e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.01 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 14 RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKALDmpaIDFVlsgdeeFwd 93
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI-DGKDVTKLPEYKRAKY---IGRV------F-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 94 iQNKLA--QPDqLTDFE---LAKLHGRF---------DEIHGYSApsKAAQLmaGLGfLENQLRLNVESFSGGWRMRLNL 159
Cdd:COG1101 87 -QDPMMgtAPS-MTIEEnlaLAYRRGKRrglrrgltkKRRELFRE--LLATL--GLG-LENRLDTKVGLLSGGQRQALSL 159
|
170 180
....*....|....*....|.
gi 492309081 160 ARTLMSRSDLLLLDEPTNHLD 180
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALD 180
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-182 |
3.29e-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: 51.26 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrptgwtvahmaqEVKALDMPAIDFVlsgdeefwDIQNKLA- 99
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-------------EIDGIDISTIPLE--------DLRSSLTi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 100 --QPDQLTDFELAKLHGRFDEihgYSapskAAQLMAGLGFLENQLRLnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTN 177
Cdd:cd03369 87 ipQDPTLFSGTIRSNLDPFDE---YS----DEEIYGALRVSEGGLNL-----SQGQRQLLCLARALLKRPRVLVLDEATA 154
|
....*
gi 492309081 178 HLDLD 182
Cdd:cd03369 155 SIDYA 159
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-216 |
3.33e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.80 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 24 LHPGWKIGLTGVNGAGKSTLFAALLGSLgADEGSltrpTGWTVAHMAQEVkaLDMPAIDFVLSGDEE----FWDIQNKLa 99
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSQTAFALMGLL-AANGR----IGGSATFNGREI--LNLPEKELNKLRAEQismiFQDPMTSL- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 100 QP-----DQLTdfELAKLHGRFDEIHGYSapsKAAQLMAGLGFLENQLRLNV--ESFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:PRK09473 111 NPymrvgEQLM--EVLMLHKGMSKAEAFE---ESVRMLDAVKMPEARKRMKMypHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 173 DEPTNHLDLDA---ILWLEDWLKAYEGT-LILISHDRDFLDAITDHIL 216
Cdd:PRK09473 186 DEPTTALDVTVqaqIMTLLNELKREFNTaIIMITHDLGVVAGICDKVL 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-180 |
3.41e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPTGWT-VAHMAQ-EVKALDMP 79
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRdLYALSEaERRRLLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 AIDFV-----------------------LSGDEEFWDIQNKLAqpDQLTDFELAKlhGRFDEihgysAPSkaaqlmaglg 136
Cdd:PRK11701 90 EWGFVhqhprdglrmqvsaggnigerlmAVGARHYGDIRATAG--DWLERVEIDA--ARIDD-----LPT---------- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 137 flenqlrlnveSFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11701 151 -----------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
298-507 |
3.81e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 298 TFSFREPTKMSSPLLTLDNASIGYGDKQIA--EKIRLQITPNSRIGLLGMNGAGKSTLIkslvgdlpllagerkasELLN 375
Cdd:PRK11160 325 TFPTTSTAAADQVSLTLNNVSFTYPDQPQPvlKGLSLQIKAGEKVALLGRTGCGKSTLL-----------------QLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 376 IGYFAQHQMDALDGHA----------SPM-----------------LQLA--RIADKQISEATLRSFLGSFGFSGERMDT 426
Cdd:PRK11160 388 RAWDPQQGEILLNGQPiadyseaalrQAIsvvsqrvhlfsatlrdnLLLAapNASDEALIEVLQQVGLEKLLEDDKGLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 427 -------PcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM-RHALSMALQDFEG-AVVLVSHERQLIASVcDEL 497
Cdd:PRK11160 468 wlgeggrQ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQF-DRI 543
|
250
....*....|
gi 492309081 498 LLVHGGKCTE 507
Cdd:PRK11160 544 CVMDNGQIIE 553
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
150-216 |
4.00e-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: 50.99 E-value: 4.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLedwlkAYEG-TLILISHDRDFLDAITDHIL 216
Cdd:cd03262 137 SGGQQQRVAIARALAMNPKVMLFDEPTSALDpelvgevLDVMKDL-----AEEGmTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
5.00e-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: 51.04 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVS----LRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKAL 76
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING--------LERPTSGSVLVDGTDLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DmpaidfvlsgDEEFWDIQNKLAQPDQltDFELAKLHGRFD------EIHGYS---APSKAAQLMAGLGfLENQLRLNVE 147
Cdd:cd03258 73 S----------GKELRKARRRIGMIFQ--HFNLLSSRTVFEnvalplEIAGVPkaeIEERVLELLELVG-LEDKADAYPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-203 |
5.66e-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: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSL---RRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLfAALLGSLgadegslTRPTGWTVAHMAQEVKALDM 78
Cdd:TIGR00958 479 IEFQDVSFsypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV-AALLQNL-------YQPTGGQVLLDGVPLVQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 79 PAI--DFVLSGDEEFW---DIQNKLAQpdQLTDFELAKLhgrfdeihgySAPSKAAQLMAGLGFLENQLRLNV----ESF 149
Cdd:TIGR00958 551 HYLhrQVALVGQEPVLfsgSVRENIAY--GLTDTPDEEI----------MAAAKAANAHDFIMEFPNGYDTEVgekgSQL 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLILISH 203
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
307-469 |
6.75e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGY-GDKQIA-EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG------------DLPL----LAGER 368
Cdd:PRK13648 3 DKNSIIVFKNVSFQYqSDASFTlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGiekvksgeifynNQAItddnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 369 KasellNIGYFAQH----------QMD---ALDGHASPMLQLARIADKQISEATLRsflgsfgfsgERMDTPCESFSGGE 435
Cdd:PRK13648 83 K-----HIGIVFQNpdnqfvgsivKYDvafGLENHAVPYDEMHRRVSEALKQVDML----------ERADYEPNALSGGQ 147
|
170 180 190
....*....|....*....|....*....|....
gi 492309081 436 RARLALALIVWQRPNVLILDEPTNHLDLDMRHAL 469
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-204 |
7.60e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.23 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 10 RRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALDMPAI-DFVLSGD 88
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG--------LESPSQGNVSWRGEPLAKLNRAQRkAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 89 EEFWD----------IQNKLAQP-DQLTDFELAKLHGRFDEIHGYS--APSKAAQLMAGLgflenqlrlnvesfSGGWRM 155
Cdd:PRK10419 93 MVFQDsisavnprktVREIIREPlRHLLSLDKAERLARASEMLRAVdlDDSVLDKRPPQL--------------SGGQLQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492309081 156 RLNLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDwLKAYEGT-LILISHD 204
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKK-LQQQFGTaCLFITHD 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
332-504 |
7.86e-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: 50.18 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 332 LQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP-----LLAG---------ERKASELL---NIgyFAQHQMDALDGHA-S 392
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGfETPqsgrvLINGvdvtaappaDRPVSMLFqenNL--FAHLTVEQNVGLGlS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 393 PMLQLARIADKQISEAtlrsfLGSFGFSGERMDTPcESFSGGERARLALA-LIVWQRPnVLILDEPTNHLDLDMRHALSM 471
Cdd:cd03298 97 PGLKLTAEDRQAIEVA-----LARVGLAGLEKRLP-GELSGGERQRVALArVLVRDKP-VLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 492309081 472 ALQDF----EGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03298 170 LVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
142-240 |
7.91e-07 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 50.41 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 142 LRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDWLKAYEGTLILISHDRDFLDAITDHILH 217
Cdd:cd03299 123 LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkeKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAI 202
|
90 100
....*....|....*....|...
gi 492309081 218 IENQELTLYTGNYSTFETTRSER 240
Cdd:cd03299 203 MLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-180 |
8.15e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.48 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPG-WKIgLTGVNGAGKSTLFAALlgslgadeGSLTRPTGWTVAHMAQEVKAL--- 76
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGeFKL-ITGPSGCGKSTLLKIV--------ASLISPTSGTLLFEGEDISTLkpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 ----------DMPAidfvLSGDEEF------WDIQNKLAQPDQLTDFelaklhgrfdeihgysapskaaqlMAGLGFLEN 140
Cdd:PRK10247 78 iyrqqvsycaQTPT----LFGDTVYdnlifpWQIRNQQPDPAIFLDD------------------------LERFALPDT 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492309081 141 QLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK10247 130 ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
332-489 |
9.02e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 50.35 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 332 LQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGE---------RKASELLNIGYFAQH----QMDALDGH-- 390
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTpasgslTLNGQdhtttppsrRPVSMLFQENNLFSHltvaQNIGLGLNpg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 391 ----ASPMLQLARIAdKQISeatLRSFLgsfgfsgERMdtPCEsFSGGERARLALA-LIVWQRPnVLILDEPTNHLDLDM 465
Cdd:PRK10771 100 lklnAAQREKLHAIA-RQMG---IEDLL-------ARL--PGQ-LSGGQRQRVALArCLVREQP-ILLLDEPFSALDPAL 164
|
170 180
....*....|....*....|....
gi 492309081 466 RHALSMALQDfegavvlVSHERQL 489
Cdd:PRK10771 165 RQEMLTLVSQ-------VCQERQL 181
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
312-504 |
9.24e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERKASELL------NIGYFAQHQMD 385
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTV-------LRLVAGLEKPTEGQifidgeDVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 386 --------ALDGHAS---------PMLQLARIADKQ-ISEATLRSFLGSFGfsgermDTPCESFSGGERARLALALIVWQ 447
Cdd:PRK11432 80 icmvfqsyALFPHMSlgenvgyglKMLGVPKEERKQrVKEALELVDLAGFE------DRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 448 RPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIrelqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
312-507 |
9.51e-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: 50.31 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGD-KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPL----LAGERKA---- 370
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvssgsilIDGQDIrevtLDSLRRAigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 371 ---SELLN--IGY-FAQHQMDALDghaSPMLQLARIAdkQISEATLRSflgSFGFS---GER--MdtpcesFSGGERARL 439
Cdd:cd03253 81 pqdTVLFNdtIGYnIRYGRPDATD---EEVIEAAKAA--QIHDKIMRF---PDGYDtivGERglK------LSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEG-AVVLVSHERQLIASvCDELLLVHGGKCTE 507
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
316-507 |
1.06e-06 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 50.30 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIAEK-IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKasellnigyfaqhqMDALDGhaspm 394
Cdd:cd03254 7 NVNFSYDEKKPVLKdINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL--------------IDGIDI----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 395 lqlariadKQISEATLRSFLG-----SFGFSGE-----RMDTPC----------------------------------ES 430
Cdd:cd03254 68 --------RDISRKSLRSMIGvvlqdTFLFSGTimeniRLGRPNatdeevieaakeagahdfimklpngydtvlgengGN 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 431 FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQD-FEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:cd03254 140 LSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKlMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-180 |
1.11e-06 |
|
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: 50.31 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPtgwtvahmAQEVKALDMPA 80
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID--------GQDIREVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 I---------DFVLSGDEEFWDIqnKLAQPDQlTDFEL------AKLHgrfDEI----HGYSApskaaqlMAGlgflENQ 141
Cdd:cd03253 73 LrraigvvpqDTVLFNDTIGYNI--RYGRPDA-TDEEVieaakaAQIH---DKImrfpDGYDT-------IVG----ERG 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 492309081 142 LRLnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03253 136 LKL-----SGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-186 |
1.13e-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: 52.32 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 24 LHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEVKAL----DMPAIDFVLSGDEEFwdiqnkla 99
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgycpQFDAIDDLLTGREHL-------- 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 100 qpdqltdFELAKLHGrfdeihgysAPSKAAQLMAGLGFLENQLRLNVE----SFSGGWRMRLNLARTLMSRSDLLLLDEP 175
Cdd:TIGR01257 2034 -------YLYARLRG---------VPAEEIEKVANWSIQSLGLSLYADrlagTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170
....*....|...
gi 492309081 176 TNHLDLDA--ILW 186
Cdd:TIGR01257 2098 TTGMDPQArrMLW 2110
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
305-490 |
1.15e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 305 TKMSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--DLPLLAG----------ERKASE 372
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGdilfkgesilDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 373 LLNIGYFAQHQ----------MDaldghaspMLQLA---RIADKQISEATLRSFlgsFGFSGERMD----TPC------- 428
Cdd:CHL00131 81 RAHLGIFLAFQypieipgvsnAD--------FLRLAynsKRKFQGLPELDPLEF---LEIINEKLKlvgmDPSflsrnvn 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 429 ESFSGGERAR---LALALIvwqRPNVLILDEPTNHLDLDMRHALSMALQDF---EGAVVLVSHERQLI 490
Cdd:CHL00131 150 EGFSGGEKKRneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
321-526 |
1.16e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.13 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 321 YGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSL------------VGDLPLLAGERKASELLNIGYFAQH-----Q 383
Cdd:PRK11264 13 FHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLIRQLRQHvgfvfQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 384 MDALDGHASPMLQL------ARIADKQISEATLRSFLGSFGFSGERMDTPcESFSGGERARLALALIVWQRPNVLILDEP 457
Cdd:PRK11264 93 NFNLFPHRTVLENIiegpviVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 458 TNHLDLDM-RHALSM--ALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTEfegdlQDYAKWLREARQQQ 526
Cdd:PRK11264 172 TSALDPELvGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE-----QGPAKALFADPQQP 238
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-216 |
1.27e-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: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGG--RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgadegsltRPTGWTV----AHMAQevka 75
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW--------PPTAGSVrldgADLSQ---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 76 ldmpaidfvlsgdeefWDiqnklaqPDQLT--------DFELakLHG-------RFDEIHgysaPSK---AAQLmAG--- 134
Cdd:COG4618 399 ----------------WD-------REELGrhigylpqDVEL--FDGtiaeniaRFGDAD----PEKvvaAAKL-AGvhe 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 135 ------------LGflENQLRLnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAIlwleDWLKAYE 195
Cdd:COG4618 449 milrlpdgydtrIG--EGGARL-----SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAI----RALKARG 517
|
250 260
....*....|....*....|.
gi 492309081 196 GTLILISHDRDFLdAITDHIL 216
Cdd:COG4618 518 ATVVVITHRPSLL-AAVDKLL 537
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
323-517 |
1.52e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 51.26 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 323 DKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLV-------GDLpLLAGERkaseLLNIGYFAQHQMDALDGHaSPML 395
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQV-LLDGVP----LVQYDHHYLHRQVALVGQ-EPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 396 -----------QLARIADKQISEATLRSFLGSFGFSGER-MDTPC----ESFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:TIGR00958 567 fsgsvreniayGLTDTPDEEIMAAAKAANAHDFIMEFPNgYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 460 HLDLDMRHALSMALQDFEGAVVLVSHERQLIASvCDELLLVHGGKCTEFEGDLQDYAK 517
Cdd:TIGR00958 647 ALDAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
405-507 |
1.65e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.16 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 405 ISEATLRSF--LGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFE----G 478
Cdd:PRK13646 118 LDEVKNYAHrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenK 197
|
90 100
....*....|....*....|....*....
gi 492309081 479 AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK13646 198 TIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
311-500 |
1.99e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.70 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGERKASELLNIGYFAQHQ- 383
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyqhgsiTLDGKPVEGPGAERGVVFQNEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 384 ----MDALDGHASPmLQLARIADKQiSEATLRSFLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:PRK11248 81 llpwRNVQDNVAFG-LQLAGVEKMQ-RLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492309081 460 HLDL----DMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLV 500
Cdd:PRK11248 158 ALDAftreQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
340-486 |
2.20e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVGDL-PLLAG------------ERKASELLNigYFAQHQMDALDGHASPML--QLARIADKQ 404
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLkPNLGKfddppdwdeildEFRGSELQN--YFTKLLEGDVKVIVKPQYvdLIPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 405 ISEATLRSF-LGSFGFSGERM------DTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRhaLSMA----- 472
Cdd:cd03236 107 VGELLKKKDeRGKLDELVDQLelrhvlDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR--LNAArlire 184
|
170
....*....|....
gi 492309081 473 LQDFEGAVVLVSHE 486
Cdd:cd03236 185 LAEDDNYVLVVEHD 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
307-504 |
2.24e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.08 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSsplLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--------------DLPLL-AGERKas 371
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsghirfhgtDVSRLhARDRK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 372 ellnIGYFAQH-----QMDALDG----------HASP--------------MLQLARIADKQISEatlrsflgsfgfsge 422
Cdd:PRK10851 76 ----VGFVFQHyalfrHMTVFDNiafgltvlprRERPnaaaikakvtqlleMVQLAHLADRYPAQ--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 423 rmdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL----QDFEGAVVLVSHERQLIASVCDELL 498
Cdd:PRK10851 137 --------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVV 208
|
....*.
gi 492309081 499 LVHGGK 504
Cdd:PRK10851 209 VMSQGN 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
308-507 |
2.25e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.71 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 308 SSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKASELLNIGYFAQHQMDAL 387
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 388 D-----------GHASPMLQLARI-----ADKQISEATLRSF-------LGSFGFSGERMDTPCESFSGGERARLALALI 444
Cdd:PRK14271 98 EfrrrvgmlfqrPNPFPMSIMDNVlagvrAHKLVPRKEFRGVaqarlteVGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 445 VWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-226 |
2.28e-06 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 49.07 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 9 LRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGwtvahmaqEVKALDMPAIDFvlsgd 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RG--------RVSSLLGLGGGF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 89 eefwdiqnklaQPDqLTDFELAKLHGRfdeIHGYSAPSKAAQLMAGLGF--LENQLRLNVESFSGGWRMRLNLARTLMSR 166
Cdd:cd03220 96 -----------NPE-LTGRENIYLNGR---LLGLSRKEIDEKIDEIIEFseLGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 167 SDLLLLDEPT----NHLDLDAILWLEDWLKAyEGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:cd03220 161 PDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
21-204 |
2.38e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.04 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALlgslgadeGSLTRPTGWTVAHMAQEVKALDMPAiDFVLSGDEEFWDIQNKLAQ 100
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLL--------GGLDTPTSGDVIFNGQPMSKLSSAA-KAELRNQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 101 PDqLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11629 100 PD-FTALENVAMPLLIGKKKPAEINSRALEMLAAVG-LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180
....*....|....*....|....*...
gi 492309081 181 L---DAILWLEDWLKAYEGTLIL-ISHD 204
Cdd:PRK11629 178 ArnaDSIFQLLGELNRLQGTAFLvVTHD 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-228 |
2.39e-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: 49.19 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 14 RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgaDEGSLTRptGwTVAHMAQEVKALDMP-AIDFVLSGD---- 88
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTS--G-QILFNGQPRKPDQFQkCVAYVRQDDillp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 89 ----EEFWDIQNKLAQPDQLTDFELAKLhgrfDEIHGYSApskaaqlmAGLGFLENQLrlnVESFSGGWRMRLNLARTLM 164
Cdd:cd03234 95 gltvRETLTYTAILRLPRKSSDAIRKKR----VEDVLLRD--------LALTRIGGNL---VKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 165 SRSDLLLLDEPTNHLD----LDAILWLEDWlkAYEGTLILIS-HD-RDFLDAITDHILHIENQELtLYTG 228
Cdd:cd03234 160 WDPKVLILDEPTSGLDsftaLNLVSTLSQL--ARRNRIVILTiHQpRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
308-496 |
3.20e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.02 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 308 SSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP------LLAGER------KASELLN 375
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQpdsgeiLLDGEPvrfrspRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 376 IGYFAQH-----QMDALD----GHasPMLQLARIADKQISEATlRSFLGSFGFSgERMDTPCESFSGGER-----ARlAL 441
Cdd:COG1129 81 IAIIHQElnlvpNLSVAEniflGR--EPRRGGLIDWRAMRRRA-RELLARLGLD-IDPDTPVGDLSVAQQqlveiAR-AL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 442 AlivwQRPNVLILDEPTNHLDLD--------MRHalsmaLQDfEG-AVVLVSH---ErqlIASVCDE 496
Cdd:COG1129 156 S----RDARVLILDEPTASLTEReverlfriIRR-----LKA-QGvAIIYISHrldE---VFEIADR 209
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-218 |
3.22e-06 |
|
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: 48.80 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgaDEGslTRPTGWTVAHMAQEVKAL------------------DMPAI- 81
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSKTIAG----HPS--YEVTSGTILFKGQDLLELepderaraglflafqypeEIPGVs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 --DFVLSGDEefwdIQNKLAQPDQLTDFELAKLhgrfdeihgysapskAAQLMAGLGFLENQLRLNV-ESFSGGWRMRLN 158
Cdd:TIGR01978 94 nlEFLRSALN----ARRSARGEEPLDLLDFEKL---------------LKEKLALLDMDEEFLNRSVnEGFSGGEKKRNE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EGTLILISHDRDFLDAITDHILHI 218
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
432-507 |
3.24e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMR----HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-204 |
3.43e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtVAHM--AQEVKAL----------------DMPAID 82
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR------VLGYvpFKRRKEFarrigvvfgqrsqlwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 83 -FVLSGdeEFWDIqnklaqPDQLTDFELAKLHGRFDeihgysapskaaqlmaglgfLENQLRLNVESFSGGWRMRLNLAR 161
Cdd:COG4586 116 sFRLLK--AIYRI------PDAEYKKRLDELVELLD--------------------LGELLDTPVRQLSLGQRMRCELAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492309081 162 TLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY---EG-TLILISHD 204
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGtTILLTSHD 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
322-492 |
3.46e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLP----LLAGERKASELLN---------IGY-FAQHQ--M 384
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPsagkIWFSGHDITRLKNrevpflrrqIGMiFQDHHllM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 385 D--ALDGHASPMLQLARIAD---KQISEAtlrsfLGSFGFSGERMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTN 459
Cdd:PRK10908 93 DrtVYDNVAIPLIIAGASGDdirRRVSAA-----LDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 492309081 460 HLDLDMRHALSMALQDFE--GAVVLV-SHERQLIAS 492
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNrvGVTVLMaTHDIGLISR 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
150-225 |
3.81e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---------LDAILWLEdwlkaYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:PRK11247 135 SGGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdLIESLWQQ-----HGFTVLLVTHDVSEAVAMADRVLLIEE 209
|
....*
gi 492309081 221 QELTL 225
Cdd:PRK11247 210 GKIGL 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-223 |
4.11e-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: 47.43 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 9 LRRGGRvlFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAhmaqevkaldmpaidfvlsgd 88
Cdd:cd03215 10 LSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--------LRPPASGEIT--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 89 eefwdiqnklaqpdqltdfelakLHGRfdEIHGYSaPSKAAQlmAGLGFL-ENQLR------LNVES-------FSGGWR 154
Cdd:cd03215 59 -----------------------LDGK--PVTRRS-PRDAIR--AGIAYVpEDRKReglvldLSVAEnialsslLSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGT-LILISHDRDFLDAITDHILHIENQEL 223
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELadAGKaVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
312-597 |
4.41e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 48.70 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGY--GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLV------GDLPL---------LAGERKASELL 374
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIdgvswnsvpLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 NIGYFA-----QHQMDALDGHASPmlQLARIADKQISEATLRSFLGSFGFSGErmDTPCeSFSGGERARLALALIVWQRP 449
Cdd:cd03289 83 PQKVFIfsgtfRKNLDPYGKWSDE--EIWKVAEEVGLKSVIEQFPGQLDFVLV--DGGC-VLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 450 NVLILDEPTNHLDLDMRHALSMAL-QDFEGAVVLVSHERQLIASVCDELLLVHGGKCtefegdlqdyakWLREARQQQIN 528
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLkQAFADCTVILSEHRIEAMLECQRFLVIEENKV------------RQYDSIQKLLN 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 529 AQTAVAQnnsssaAPAPAKVDKEAQRKEAARRREQTRPirkniekvesQIEKLQPQlakIEESLADTSL 597
Cdd:cd03289 226 EKSHFKQ------AISPSDRLKLFPRRNSSKSKRKPRP----------QIQALQEE---TEEEVQDTRL 275
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-504 |
4.43e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 24 LHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtRPTGWTVAHmAQEVKALDMpAIDFVlsgdeefwdIQNKLAQPDQ 103
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTL-EIGGNPCAR-LTPAKAHQL-GIYLV---------PQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 104 LTD----FELAKLHGrfdeihgysAPSKAAQLMAGLGfleNQLRLNVESFSggwrmrLNLA--------RTLMSRSDLLL 171
Cdd:PRK15439 102 SVKenilFGLPKRQA---------SMQKMKQLLAALG---CQLDLDSSAGS------LEVAdrqiveilRGLMRDSRILI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 172 LDEPTNHL---DLDAILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLyTGNYSTFETTrserlaqqqqaf 248
Cdd:PRK15439 164 LDEPTASLtpaETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL-SGKTADLSTD------------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 249 ekqqetrahlqKFIDRFKAKATKARQAQSRIKQLErmqqlAPAHvdtpftfsfREPTKMSSPLLTLDNASiGYGDKQIAe 328
Cdd:PRK15439 231 -----------DIIQAITPAAREKSLSASQKLWLE-----LPGN---------RRQQAAGAPVLTVEDLT-GEGFRNIS- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 329 kirLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE---------------------------RKASELL------- 374
Cdd:PRK15439 284 ---LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRimlngkeinalstaqrlarglvylpedRQSSGLYldaplaw 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 NIGYFAQHQMdaldghaSPMLQLARIAdkqiseATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLIL 454
Cdd:PRK15439 361 NVCALTHNRR-------GFWIKPAREN------AVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 455 DEPTNHLDLDMRHAL-----SMALQDFegAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK15439 428 DEPTRGVDVSARNDIyqlirSIAAQNV--AVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-204 |
4.73e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.47 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTL---FAALL----GSLGADEGSLTRPTGWTVA------ 67
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLlkcFARLLtpqsGTVFLGDKPISMLSSRQLArrlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 68 ---HMAQE---VKALdmpaidfVLSGDEEFWDIQNKLAQPDQltdfelaklhgrfdeihgysapSKAAQLMAGLGFLENQ 141
Cdd:PRK11231 82 pqhHLTPEgitVREL-------VAYGRSPWLSLWGRLSAEDN----------------------ARVNQAMEQTRINHLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 142 LRLnVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLKAYEGTLILISHD 204
Cdd:PRK11231 133 DRR-LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHD 197
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-214 |
5.06e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.35 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 13 GRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrptgwtvahMAQEVKALdMPAIDFVLSGD---E 89
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---------IDDEDISL-LPLHARARRGIgylP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 90 EFWDIQNKLAQPDQLtdfeLAKLHGRfDEIHGYSAPSKAAQLMAglGFLENQLRLNV-ESFSGGWRMRLNLARTLMSRSD 168
Cdd:PRK10895 85 QEASIFRRLSVYDNL----MAVLQIR-DDLSAEQREDRANELME--EFHIEHLRDSMgQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 169 LLLLDEPTNHLDLDAILWLEDwlkayegtliLISHDRDFLDA--ITDH 214
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKR----------IIEHLRDSGLGvlITDH 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-213 |
5.36e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRR--GGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPTGWTVAH--MAQEVKAL 76
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM-IDDCDVAKfgLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DM-PAIDFVLSGDEEFwdiqnklaQPDQLTDFELAKLHGRFDEIHGYSAPSKAAqlmagLGfLENQLRLNVESFSGGWRM 155
Cdd:PLN03232 1313 SIiPQSPVLFSGTVRF--------NIDPFSEHNDADLWEALERAHIKDVIDRNP-----FG-LDAEVSEGGENFSVGQRQ 1378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 156 RLNLARTLMSRSDLLLLDEPTNHLDL--DAILWLEDWLKAYEGTLILISHDrdfLDAITD 213
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVrtDSLIQRTIREEFKSCTMLVIAHR---LNTIID 1435
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
336-493 |
5.45e-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: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 336 PNSRIGLLGMNGAGKSTLIKSLVGdlpLLAGERKASELLNIGYFAQHQMDALDGHASPMLQLariadkqiseatlrsflg 415
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR---ELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA------------------ 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 416 sfgfsgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAVVLVSHERQLIASV 493
Cdd:smart00382 60 --------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTT 123
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-182 |
5.59e-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: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR--RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtRPTGWTVAHMAQE---VKAL 76
Cdd:TIGR00957 1285 VEFRNYCLRyrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-IIDGLNIAKIGLHdlrFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 77 DMPAIDFVLSG-------------DEEFWdiqnklaqpdqlTDFELAKLHGRFDeihgySAPSKaaqlmaglgfLENQLR 143
Cdd:TIGR00957 1364 IIPQDPVLFSGslrmnldpfsqysDEEVW------------WALELAHLKTFVS-----ALPDK----------LDHECA 1416
|
170 180 190
....*....|....*....|....*....|....*....
gi 492309081 144 LNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD 182
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
311-504 |
5.64e-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: 49.44 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP--------LLAGE----RKASELLNIGY 378
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiYWSGSplkaSNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 379 FAQHQmdaldghaspmlQLARIADKQISEATlrsFLGS-FGFSGERMDTP-----CES------------------FSGG 434
Cdd:TIGR02633 81 VIIHQ------------ELTLVPELSVAENI---FLGNeITLPGGRMAYNamylrAKNllrelqldadnvtrpvgdYGGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 435 ERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-214 |
6.45e-06 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 47.92 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL----TRPTGWTV--------AHMAQE 72
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPMhkrarlgiGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 73 VKAL-DMPAIDFVLSGDEEF----WDIQNKLAQpdQLTDFELAKLhgrfdeihgysAPSKAAQLmaglgflenqlrlnve 147
Cdd:cd03218 84 ASIFrKLTVEENILAVLEIRglskKEREEKLEE--LLEEFHITHL-----------RKSKASSL---------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 148 sfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEdwlkayegTLILISHDRDFLDAITDH 214
Cdd:cd03218 135 --SGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQ--------KIIKILKDRGIGVLITDH 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-505 |
6.56e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.28 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVGDLP---------LLAGER-KASELLNIGYFAQhQMDALDGHA--------SPMLQLARIA 401
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPkgvkgsgsvLLNGMPiDAKEMRAISAYVQ-QDDLFIPTLtvrehlmfQAHLRMPRRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 402 DKQISEATLRSFLGSFGF---------SGERMdtpcESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMA 472
Cdd:TIGR00955 133 TKKEKRERVDEVLQALGLrkcantrigVPGRV----KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 492309081 473 LQDF--EGAVVLVS-HE-RQLIASVCDELLLVHGGKC 505
Cdd:TIGR00955 209 LKGLaqKGKTIICTiHQpSSELFELFDKIILMAEGRV 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-226 |
6.96e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.77 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGwTVAHMaqevkaLDMPAIdFvlsgdeefwdiqnklaQ 100
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NG-RVSAL------LELGAG-F----------------H 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 101 PDqLTDFELAKLHGRfdeIHGYSaPSKAAQLM------AGLG-FLENQLRlnveSFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:COG1134 101 PE-LTGRENIYLNGR---LLGLS-RKEIDEKFdeivefAELGdFIDQPVK----TYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 174 EptnhldldailwledWL---------KAYE---------GTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:COG1134 172 E---------------VLavgdaafqkKCLArirelresgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-208 |
7.15e-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: 49.56 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTgwTVAHMAQEVkaldmpaidfvlsgdeefWdIQNKLAQ 100
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--SVAYVPQQA------------------W-IQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 101 PDQLTDFELAKLHgrfdeihgYSAPSKAAQLMAGLGFLENQLRLNVE----SFSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:TIGR00957 717 ENILFGKALNEKY--------YQQVLEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190
....*....|....*....|....*....|....*....
gi 492309081 177 NHLD-------LDAILWLEDWLKAyeGTLILISHDRDFL 208
Cdd:TIGR00957 789 SAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYL 825
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
331-484 |
7.58e-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: 49.63 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 331 RLQIT--PNSRIGLLGMNGAGKSTLIKSLVGDLP-----LLAGERKASELLN-----IGYFAQHQMdaLDGH---ASPML 395
Cdd:TIGR01257 948 RLNITfyENQITAFLGHNGAGKTTTLSILTGLLPptsgtVLVGGKDIETNLDavrqsLGMCPQHNI--LFHHltvAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 396 QLARIADKQISEATL--RSFLGSFGFSGERmDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHAL-SMA 472
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLemEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIwDLL 1104
|
170
....*....|..
gi 492309081 473 LQDFEGAVVLVS 484
Cdd:TIGR01257 1105 LKYRSGRTIIMS 1116
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
132-224 |
8.56e-06 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 48.18 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 132 MAGLGFLenqLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIL-WLEDWLKAYEGTLILISHDRDF 207
Cdd:TIGR02142 118 LLGIGHL---LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHSLQE 194
|
90
....*....|....*..
gi 492309081 208 LDAITDHILHIENQELT 224
Cdd:TIGR02142 195 VLRLADRVVVLEDGRVA 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
316-507 |
8.71e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPL-----------LAGERKASELLN-------IG 377
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearvegevrLFGRNIYSPDVDpievrreVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQHQMD--------------ALDGHASPMLQLARIADKQISEATLRSFLGsfgfsgERMDTPCESFSGGERARLALAL 443
Cdd:PRK14267 89 MVFQYPNPfphltiydnvaigvKLNGLVKSKKELDERVEWALKKAALWDEVK------DRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 444 IVWQRPNVLILDEPTNHLD---LDMRHALSMALQDfEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
344-492 |
9.09e-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: 46.83 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 344 GMNGAGKSTLIK----SLVGDLPllagerkasellNIGYFAQHQMDAL---DGHASPMLQLARIADKQIsEAT--LRSFL 414
Cdd:cd03240 29 GQNGAGKTTIIEalkyALTGELP------------PNSKGGAHDPKLIregEVRAQVKLAFENANGKKY-TITrsLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 415 GSFGFSGERMDTPCE----SFSGGERA------RLALALIVWQRPNVLILDEPTNHLDLD-MRHALSMALQDFEGA---- 479
Cdd:cd03240 96 NVIFCHQGESNWPLLdmrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQknfq 175
|
170
....*....|...
gi 492309081 480 VVLVSHERQLIAS 492
Cdd:cd03240 176 LIVITHDEELVDA 188
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
143-239 |
9.32e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 143 RLN--VESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAILWLEDWLKAyEGTLILISHDRDFLDAITDHILH 217
Cdd:PRK14246 146 RLNspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAF 224
|
90 100
....*....|....*....|..
gi 492309081 218 IENQELTLYTGNYSTFETTRSE 239
Cdd:PRK14246 225 LYNGELVEWGSSNEIFTSPKNE 246
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
311-507 |
9.52e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 311 LLTLDNASIGYGDKQI----AEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG--DLP--------------LLAGERKA 370
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGliDYPgrvmaeklefngqdLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 371 ------SEL----------LNIGYFAQHQ-MDALDGH-----------ASPMLQLARIADKQiseatlrsflgsfgfsgE 422
Cdd:PRK11022 83 rrnlvgAEVamifqdpmtsLNPCYTVGFQiMEAIKVHqggnkktrrqrAIDLLNQVGIPDPA-----------------S 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 423 RMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQDFEG-AVVLVSHERQLIASVCDELL 498
Cdd:PRK11022 146 RLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQiieLLLELQQKENmALVLITHDLALVAEAAHKII 225
|
....*....
gi 492309081 499 LVHGGKCTE 507
Cdd:PRK11022 226 VMYAGQVVE 234
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
340-502 |
9.83e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVGDLpLLAGERKASELLNIGYFAQHQmdaldghaspmlqlariadkqiseatlrsflgsfgf 419
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQL-IPNGDNDEWDGITPVYKPQYI------------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 420 sgermdtpceSFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF----EGAVVLVSHERQLIASVCD 495
Cdd:cd03222 71 ----------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSD 140
|
....*..
gi 492309081 496 ELLLVHG 502
Cdd:cd03222 141 RIHVFEG 147
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
310-504 |
9.95e-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: 46.66 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 310 PLLTLDNASIGYGDKqiaeKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGE----------RKASELLN--IG 377
Cdd:cd03215 3 PVLEVRGLSVKGAVR----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEitldgkpvtrRSPRDAIRagIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 378 YFAQhqmdalDGHASPMLQLARIADKqiseATLRSFLgsfgfsgermdtpcesfSGGERARLALALIVWQRPNVLILDEP 457
Cdd:cd03215 79 YVPE------DRKREGLVLDLSVAEN----IALSSLL-----------------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492309081 458 TNHLDLDMR---HALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:cd03215 132 TRGVDVGAKaeiYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-212 |
1.03e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 48.29 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKALDMPAIDFVL------SGDEEFWDI 94
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHVPPYQRPINMMFQSYALfphmtvEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 95 QNKLAQpdqltdfelAKLHGRFDEihgysapskaaqlMAGLGFLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDE 174
Cdd:PRK11607 118 QDKLPK---------AEIASRVNE-------------MLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492309081 175 PTNHLD--LDAILWLE--DWLKAYEGTLILISHDRDflDAIT 212
Cdd:PRK11607 176 PMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQE--EAMT 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-220 |
1.10e-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: 46.72 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKALDMpaidfvlsgdeeFWDIQNKLAQ 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI-NGVDVTAAPPADRPVSM------------LFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 101 PDQLTDFELAKLHG-RFDEIHGYSAPSKAAQLmaGLGFLENQLrlnVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHL 179
Cdd:cd03298 85 LTVEQNVGLGLSPGlKLTAEDRQAIEVALARV--GLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492309081 180 D---LDAILWLEDWLKAYEG-TLILISHDRDFLDAITDHILHIEN 220
Cdd:cd03298 160 DpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
307-514 |
1.21e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAG------------ERKASELL 374
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtitinninynklDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 NIGYFAQhQMDALDghaspmlQLARIADKQISEATLRSFLG----SFGFSGER-------------MDTPCESFSGGERA 437
Cdd:PRK09700 81 GIGIIYQ-ELSVID-------ELTVLENLYIGRHLTKKVCGvniiDWREMRVRaammllrvglkvdLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 438 RLALALIVWQRPNVLILDEPTNHL---DLDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGK--CTefeGDL 512
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvCS---GMV 229
|
..
gi 492309081 513 QD 514
Cdd:PRK09700 230 SD 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-204 |
1.33e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.85 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGA------DEGSLTRPTGWTVAHM----AQEVKAL-DMPAIdfvlsgde 89
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGsgsiqfAGQPLEAWSAAELARHraylSQQQTPPfAMPVF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 90 EFWDiqnkLAQPDQLtdfELAKLHGRFDEIhgysapskAAQLMaglgfLENQLRLNVESFSGG-W-RMRL-----NLART 162
Cdd:PRK03695 88 QYLT----LHQPDKT---RTEAVASALNEV--------AEALG-----LDDKLGRSVNQLSGGeWqRVRLaavvlQVWPD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492309081 163 LMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYE---GTLILISHD 204
Cdd:PRK03695 148 INPAGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
307-504 |
1.35e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 47.63 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERKASE---LLN----IGYF 379
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTV-------LRLIAGFETPDSgriMLDgqdiTHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 380 AQH-------QMDALDGHASPM------LQLARIADKQISEATLRSF----LGSFGfsgERMDTpceSFSGGERARLALA 442
Cdd:PRK09452 83 AENrhvntvfQSYALFPHMTVFenvafgLRMQKTPAAEITPRVMEALrmvqLEEFA---QRKPH---QLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 443 LIVWQRPNVLILDEPTNHLDLDMRHALSM---ALQDFEG-AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLGiTFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-203 |
1.38e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.24 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLR-RGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---------RPTGW--TVAHM 69
Cdd:COG1132 340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLESLrrQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 70 AQEVkaldmpaidFVLSG--------------DEEFWDIQnKLAQpdqLTDFeLAKLHgrfdeiHGYSAPskaaqlmagL 135
Cdd:COG1132 420 PQDT---------FLFSGtirenirygrpdatDEEVEEAA-KAAQ---AHEF-IEALP------DGYDTV---------V 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 136 GflENQLRLnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAilwLEDWLKayEGTLILISH 203
Cdd:COG1132 471 G--ERGVNL-----SGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMK--GRTTIVIAH 533
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-181 |
1.46e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSL---GADEGSltRPTGwTVAHMAQEVKALD 77
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGA--RVTG-DVTLNGEPLAAID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 MPAIDFVLSgdeefwdIQNKLAQPDQLTDFELAKLHGRFDEIHGYSAPSK-------AAQLMAGLGFLenqLRLNVESFS 150
Cdd:PRK13547 78 APRLARLRA-------VLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHrdgeiawQALALAGATAL---VGRDVTTLS 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492309081 151 GGWRMRLNLARTL---------MSRSDLLLLDEPTNHLDL 181
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
270-613 |
1.59e-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: 48.40 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 270 TKARQAQSRIKQLERMQQLAPAHVDtpftfsfREPTKMSSP-LLTLDNASIGY--GDKQIAEKIRLQITPNSRIGLLGMN 346
Cdd:TIGR00957 601 VQASVSLKRLRIFLSHEELEPDSIE-------RRTIKPGEGnSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQV 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 347 GAGKSTLIKSLVGDLPLLAGE--RKASellnIGYFAQH--------QMDALDGHA-------SPMLQLARIADKQISEAT 409
Cdd:TIGR00957 674 GCGKSSLLSALLAEMDKVEGHvhMKGS----VAYVPQQawiqndslRENILFGKAlnekyyqQVLEACALLPDLEILPSG 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 410 LRSFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEGAV-----VLVS 484
Cdd:TIGR00957 750 DRTEIGEKGVN----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVT 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 485 HERQLIASVcDELLLVHGGKCTEFeGDLQD-------YAKWLREARQQQinaQTAVAQNNSSSAAPAPakvDKEAqrkea 557
Cdd:TIGR00957 820 HGISYLPQV-DVIIVMSGGKISEM-GSYQEllqrdgaFAEFLRTYAPDE---QQGHLEDSWTALVSGE---GKEA----- 886
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 558 arrreqtRPIRKNIEKVESQIEKLQPQLAKIEESLADTS--------LYEAARKDDLLKLMNEQ 613
Cdd:TIGR00957 887 -------KLIENGMLVTDVVGKQLQRQLSASSSDSGDQSrhhgssaeLQKAEAKEETWKLMEAD 943
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
568-622 |
1.70e-05 |
|
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: 42.84 E-value: 1.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 568 RKNIEKVESQIEKLQPQLAKIEESLADTSLYeaARKDDLLKLMNEQTELKAKLEQ 622
Cdd:pfam16326 7 QRELEELEAEIEKLEEEIAELEAQLADPELY--SDYEKLQELSAELEELEAELEE 59
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-181 |
1.86e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 46.61 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGwkiGLT---GVNGAGKSTLFAALLGSLGADEGSLTRpTGWTVAHMAQEVKALD 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKG---GITaliGPNGAGKSTLLSMISRLLPPDSGEVLV-DGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 MpAIdfvlsgdeefwdiqnkLAQPDQ----LTDFELAKLhGRF----------DEIHgysaPSKAAQLMaGLGFLENQlr 143
Cdd:COG4604 77 L-AI----------------LRQENHinsrLTVRELVAF-GRFpyskgrltaeDREI----IDEAIAYL-DLEDLADR-- 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 492309081 144 lNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL 181
Cdd:COG4604 132 -YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-176 |
2.63e-05 |
|
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: 45.89 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALDMPA-----IDFVLSGDEEFwdiq 95
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMG--------LLPPRSGSIRFDGRDITGLPPHEraragIGYVPEGRRIF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 96 nklaqpDQLT---DFELAKLHGRFDEIHgySAPSKAAQLMAGLGFLENQLrlnVESFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:cd03224 88 ------PELTveeNLLLGAYARRRAKRK--ARLERVYELFPRLKERRKQL---AGTLSGGEQQMLAIARALMSRPKLLLL 156
|
....
gi 492309081 173 DEPT 176
Cdd:cd03224 157 DEPS 160
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
330-504 |
2.76e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVGDL-P----------LLAGERKASEL------LNIGY-FAQHQM------- 384
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPtsgtvtigerVITAGKKNKKLkplrkkVGIVFqFPEHQLfeetvek 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 385 DALDGhasPMLQLARIADkqiSEATLRSFLGSFGFSGERMD-TPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLD- 462
Cdd:PRK13634 106 DICFG---PMNFGVSEED---AKQKAREMIELVGLPEELLArSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDp 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 463 ------LDMRHALSmalQDFEGAVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13634 179 kgrkemMEMFYKLH---KEKGLTTVLVTHSMEDAARYADQIVVMHKGT 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
430-490 |
2.77e-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: 2.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLD-----MRHALSMALQDFEGAVVLVSHERQLI 490
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-181 |
3.03e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEG--------SLTRPTGWTVAHMAQEvkaldmpAIDFVLSGDEefw 92
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGkikhsgriSFSPQTSWIMPGTIKD-------NIIFGLSYDE--- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 93 diqnklaqpdqltdfelaklhgrfdeiHGYSAPSKAAQLMAGLGFLENQLRLNVE----SFSGGWRMRLNLARTLMSRSD 168
Cdd:TIGR01271 516 ---------------------------YRYTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLARAVYKDAD 568
|
170
....*....|...
gi 492309081 169 LLLLDEPTNHLDL 181
Cdd:TIGR01271 569 LYLLDSPFTHLDV 581
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
328-511 |
3.12e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.27 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 328 EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPLLAGERKASELLN----------IGYFAQHQMDAL-------DG 389
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNaenekwvrskVGLVFQDPDDQVfsstvwdDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 390 HASPM-LQLARIADKQISEATLRSfLGSFGFSgermDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA 468
Cdd:PRK13647 102 AFGPVnMGLDKDEVERRVEEALKA-VRMWDFR----DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492309081 469 LSMALQDF--EGAVVLVS-HERQLIASVCDELLLVHGGKcTEFEGD 511
Cdd:PRK13647 177 LMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLKEGR-VLAEGD 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
328-500 |
3.14e-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: 45.53 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 328 EKIRLQITPNSRIGLLGMNGAGKSTLIKSLVG-DLPLLAGER-KASELLNIG---------YFAQHQMDALDGHASPMLQ 396
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVIlEGKQITEPGpdrmvvfqnYSLLPWLTVRENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 397 LARIADKQISEATLRSFLGSFGFsGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMAL--- 473
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqi 160
|
170 180
....*....|....*....|....*...
gi 492309081 474 -QDFEGAVVLVSHErqliasvCDELLLV 500
Cdd:TIGR01184 161 wEEHRVTVLMVTHD-------VDEALLL 181
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-275 |
3.67e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.03 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALlgslgadeGSLTRPTGWTVAHMAQEVKALDMPAIDFVLSgdEEFWDIQNKLAQ 100
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKPTSGTYRVAGQDVATLDADALAQLRR--EHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 101 PDQLTDFELAKLHGRFDEIHGYSAPSKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK10535 98 LSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLG-LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 181 ------LDAILwleDWLKAYEGTLILISHDRDfLDAITDHILHIENQELTLYTGNYSTFETTRSErlaqqqqafEKQQET 254
Cdd:PRK10535 177 shsgeeVMAIL---HQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEKVNVAGGT---------EPVVNT 243
|
250 260
....*....|....*....|.
gi 492309081 255 RAHLQKFIDRFKAKATKARQA 275
Cdd:PRK10535 244 ASGWRQFVSGFREALTMAWRA 264
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
148-180 |
3.79e-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: 3.79e-05
10 20 30
....*....|....*....|....*....|...
gi 492309081 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:cd03213 111 GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-517 |
3.83e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 342 LLGMNGAGKSTLIKSLVGDLPLLAGERKASEllNIGYFAQHQ--MDA--------LDGHASPMLQLA-RI----ADKQIS 406
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQAwiMNAtvrgnilfFDEEDAARLADAvRVsqleADLAQL 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 407 EATLRSFLGSFGFSgermdtpcesFSGGERARLALALIVWQRPNVLILDEPTNHLDldmRHALSMALQD-FEGAV----- 480
Cdd:PTZ00243 769 GGGLETEIGEKGVN----------LSGGQKARVSLARAVYANRDVYLLDDPLSALD---AHVGERVVEEcFLGALagktr 835
|
170 180 190
....*....|....*....|....*....|....*..
gi 492309081 481 VLVSHERQLIASVcDELLLVHGGKcTEFEGDLQDYAK 517
Cdd:PTZ00243 836 VLATHQVHVVPRA-DYVVALGDGR-VEFSGSSADFMR 870
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
316-507 |
4.24e-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: 46.63 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 316 NASIGYGDKQIA--EKIRLQITPNSRIGLLGMNGAGKSTLIKSL-------VGDLpLLAGERKASELL-----NIGYFAQ 381
Cdd:TIGR02203 335 NVTFRYPGRDRPalDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGQI-LLDGHDLADYTLaslrrQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 382 HQMDALDGHASPML--QLARIADKQISEATLRSFLGSF-GFSGERMDTPCES----FSGGERARLALALIVWQRPNVLIL 454
Cdd:TIGR02203 414 DVVLFNDTIANNIAygRTEQADRAEIERALAAAYAQDFvDKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492309081 455 DEPTNHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLmQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
298-462 |
4.27e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.49 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 298 TFSFREPTKMSSP-----LLTLDNASIGY-GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSL-------------- 357
Cdd:PRK13657 316 VPDVRDPPGAIDLgrvkgAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqsgrilid 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 358 ---VGDLPLlAGERKasellNIGYFAQHQM---------------DALDghaSPMLQLARIAdkQISEATLRSFLGSFGF 419
Cdd:PRK13657 396 gtdIRTVTR-ASLRR-----NIAVVFQDAGlfnrsiednirvgrpDATD---EEMRAAAERA--QAHDFIERKPDGYDTV 464
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492309081 420 SGERmdtpCESFSGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13657 465 VGER----GRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-215 |
4.55e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.44 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 26 PGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWtvahmaQEVkaldmpaIDFvLSGDE---EFWDIQN---KLA 99
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDW------DEI-------LDE-FRGSElqnYFTKLLEgdvKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 100 QPDQLTDFELAKLHG-------RFDEIHgysapsKAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:cd03236 91 VKPQYVDLIPKAVKGkvgellkKKDERG------KLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 173 DEPTNHLDLD-----AILWLEdwLKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03236 164 DEPSSYLDIKqrlnaARLIRE--LAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
403-504 |
4.72e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.51 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 403 KQISEATLRSFLGSFGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsMALqdFEG---- 478
Cdd:PRK13649 118 QEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL-MTL--FKKlhqs 194
|
90 100
....*....|....*....|....*...
gi 492309081 479 --AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13649 195 gmTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
124-240 |
4.77e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 45.39 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 124 APSKAAQLMAglgflenQLRLN--VESF----SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILwledW 190
Cdd:COG4161 118 AREKAMKLLA-------RLRLTdkADRFplhlSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqvVEIIR----E 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 492309081 191 LKAYEGTLILISHDRDFLDAITDHILHIENQELTLYtGNYSTFETTRSER 240
Cdd:COG4161 187 LSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTEA 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
307-546 |
4.87e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSplLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERKAS----ELLNigyFAQH 382
Cdd:PRK10938 1 MSS--LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshiTRLS---FEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 383 Q-----------MDAL-DGHASPMLQLARIADKQISEATLRSFLG-SFGFSGeRMDTPCESFSGGERARLALALIVWQRP 449
Cdd:PRK10938 76 QklvsdewqrnnTDMLsPGEDDTGRTTAEIIQDEVKDPARCEQLAqQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 450 NVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLI------ASVCDELLLVHGGKCTEFEgdlqdyakwlr 520
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQsgiTLVLVLNRFDEIpdfvqfAGVLADCTLAETGEREEIL----------- 223
|
250 260
....*....|....*....|....*.
gi 492309081 521 earQQQINAQTAVAQNNSSSAAPAPA 546
Cdd:PRK10938 224 ---QQALVAQLAHSEQLEGVQLPEPD 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
429-492 |
5.59e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 5.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 429 ESFSGGERARLALAL--IVWQRPN----VLILDEPTNHLDLDMRHALS----MALQDFEG--AVVLVSHERQLIAS 492
Cdd:PRK01156 800 DSLSGGEKTAVAFALrvAVAQFLNndksLLIMDEPTAFLDEDRRTNLKdiieYSLKDSSDipQVIMISHHRELLSV 875
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-204 |
6.00e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.49 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 10 RRGGRVlfqKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALD-------- 77
Cdd:COG4608 26 RTVGVV---KAvdgvSFDIRRGETLGLVGESGCGKSTLGRLLLR--------LEEPTSGEILFDGQDITGLSgrelrplr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 -----------------MPAIDFVlsgdEEFWDIqNKLAQPDQLTDfelaklhgrfdeihgysapsKAAQLMAGLGFLEN 140
Cdd:COG4608 95 rrmqmvfqdpyaslnprMTVGDII----AEPLRI-HGLASKAERRE--------------------RVAELLELVGLRPE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 141 QLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---------LdailwLEDwLKAYEG-TLILISHD 204
Cdd:COG4608 150 HADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqaqvlnL-----LED-LQDELGlTYLFISHD 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
430-596 |
6.86e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsmalqdFEGAV--VLVSHERQLIASV------CDELLLVH 501
Cdd:TIGR01271 548 TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI------FESCLckLMSNKTRILVTSKlehlkkADKILLLH 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 502 GGKC------TEFEGDLQDYAKWL---------REARQQQINAQT----AVAQNNSSSAAPAPAKVDKEAQRKEAARRRE 562
Cdd:TIGR01271 622 EGVCyfygtfSELQAKRPDFSSLLlgleafdnfSAERRNSILTETlrrvSIDGDSTVFSGPETIKQSFKQPPPEFAEKRK 701
|
170 180 190
....*....|....*....|....*....|....*..
gi 492309081 563 QT---RPIRKNIEKVESQIEKLQPQLAKIEESLADTS 596
Cdd:TIGR01271 702 QSiilNPIASARKFSFVQMGPQKAQATTIEDAVREPS 738
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
432-504 |
7.09e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 7.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-204 |
7.48e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 44.85 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKA----SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RPT---GWTVAHMA 70
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPAlqdvSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgVPVtgpGADRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 71 QEvKALdMPaidfvlsgdeefW-DIQNKLAQPDQLTDFELAKLHGRfdeihgysapskAAQLMAGLGfLENQLRLNVESF 149
Cdd:COG4525 83 QK-DAL-LP------------WlNVLDNVAFGLRLRGVPKAERRAR------------AEELLALVG-LADFARRRIWQL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHldLDAI-------LWLEDWLKAYEGTLiLISHD 204
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGA--LDALtreqmqeLLLDVWQRTGKGVF-LITHS 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-223 |
7.87e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.82 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTL---FAALL----GSLGADEGSLTRPTGwtvahmAQEVKALdMPAIDFVLSGDEefwd 93
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLmqhFNALLkpssGTITIAGYHITPETG------NKNLKKL-RKKVSLVFQFPE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 94 iqNKLAQPDQLTDFELAKLHGRFDEihgYSAPSKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLD 173
Cdd:PRK13641 96 --AQLFENTVLKDVEFGPKNFGFSE---DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492309081 174 EPTNHLDLDAILWLEDWLKAYEG---TLILISHDRDFLDAITDHILHIENQEL 223
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-226 |
8.12e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.79 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 29 KIGLTGVNGAGKSTLFAALLGSLGADEGS-LTRPTGWTVAHMaQEVKALdmPAIDFVLSGDEEFwdiqnklaQPDQLTDF 107
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSvLIRGEPITKENI-REVRKF--VGLVFQNPDDQIF--------SPTVEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 108 ELAKLHGRFDEIHGYSAPSKAAQLMAglgfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDA 183
Cdd:PRK13652 101 AFGPINLGLDEETVAHRVSSALHMLG----LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKEL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492309081 184 ILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIENQELTLY 226
Cdd:PRK13652 177 IDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
127-204 |
8.31e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.96 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 127 KAAQLMAGLGflenqlrLNVES-------FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLK 192
Cdd:PRK11308 133 KALAMMAKVG-------LRPEHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqaqvLNLMMDLQQELG 205
|
90
....*....|...
gi 492309081 193 -AYegtlILISHD 204
Cdd:PRK11308 206 lSY----VFISHD 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-204 |
8.61e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.59 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 5 DQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEV-KALDMPAIDF 83
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 84 VLSGDEEFWDIQNKLAQPDQltdfelaKLHGRF---DEihgySAPSKAAQlMAGLGFLENQlrlNVESFSGGWRMRLNLA 160
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQ-------PLFTRWrkeDE----EAVTKAMQ-ATGITHLADQ---SVDTLSGGQRQRAWIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 161 RTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLKAYEGTLILISHD 204
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
308-497 |
1.03e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 308 SSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGErkaselLNIGYFAQH---QM 384
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGS------ILIDGQEMRfasTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 385 DALDG---------HASPMLQLAR------------IADKQISEATLRSFLGSFgfsGERMD--TPCESFSGGERARLAL 441
Cdd:PRK11288 75 AALAAgvaiiyqelHLVPEMTVAEnlylgqlphkggIVNRRLLNYEAREQLEHL---GVDIDpdTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 442 ALIVWQRPNVLILDEPTNHL---DLDMRHALSMALQDfEGAVVL-VSHERQLIASVCDEL 497
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLsarEIEQLFRVIRELRA-EGRVILyVSHRMEEIFALCDAI 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-181 |
1.06e-04 |
|
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: 44.46 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 16 LFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEG--------SLTRPTGWTVAHMAQEvkaldmpAIDFVLSG 87
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGkikhsgriSFSSQFSWIMPGTIKE-------NIIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 88 DEEFWDIQNKLAQPDQltdfELAKLhgrfdeihgysaPSKAAQLMAGLGFlenqlrlnveSFSGGWRMRLNLARTLMSRS 167
Cdd:cd03291 125 DEYRYKSVVKACQLEE----DITKF------------PEKDNTVLGEGGI----------TLSGGQRARISLARAVYKDA 178
|
170
....*....|....
gi 492309081 168 DLLLLDEPTNHLDL 181
Cdd:cd03291 179 DLYLLDSPFGYLDV 192
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
322-508 |
1.25e-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: 43.39 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 322 GDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLV---------GDLpLLAGERKASELLNIGYFAQHQmdaldghas 392
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktagvitGEI-LINGRPLDKNFQRSTGYVEQQ--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 393 pmlqlariaDKQISEATLRSFLgsfgfsgeRMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNhlDLDMRHALSMA 472
Cdd:cd03232 88 ---------DVHSPNLTVREAL--------RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTS--GLDSQAAYNIV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492309081 473 -----LQDfEGAVVLVS-HE-RQLIASVCDELLLVH-GGKCTEF 508
Cdd:cd03232 149 rflkkLAD-SGQAILCTiHQpSASIFEKFDRLLLLKrGGKTVYF 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
1.29e-04 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 43.87 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALDMP-- 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG--------LERPDSGTILFGGEDATDVPVQer 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 80 AIDFVLsgdeefwdiQNkLAQPDQLTDFELAKLHGRfdEIHGYSAPSKA---AQLMAGLGF--LENQLRLNVESFSGGWR 154
Cdd:cd03296 75 NVGFVF---------QH-YALFRHMTVFDNVAFGLR--VKPRSERPPEAeirAKVHELLKLvqLDWLADRYPAQLSGGQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 155 MRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG----TLILISHDRDFLDAITDHIL 216
Cdd:cd03296 143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVV 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
312-474 |
1.44e-04 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 43.76 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 312 LTLDNASIGYGDKQIA--EKIRLQITPNSRIGLLGMNGAGKSTLIKSL-----------------VGDLPLlagerkASE 372
Cdd:cd03251 1 VEFKNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdsgrilidghdVRDYTL------ASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 373 LLNIGYFAQhqmDALDGHASPMLQLA----RIADKQISEAT----LRSFLGSF--GFS---GERMDTpcesFSGGERARL 439
Cdd:cd03251 75 RRQIGLVSQ---DVFLFNDTVAENIAygrpGATREEVEEAAraanAHEFIMELpeGYDtviGERGVK----LSGGQRQRI 147
|
170 180 190
....*....|....*....|....*....|....*
gi 492309081 440 ALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQ 474
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALE 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
430-507 |
1.47e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.01 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG--AVVLVSHERQLIASVcDELLLVHGGKCTE 507
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKA-DEILVVEDGEIVE 558
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
124-216 |
1.49e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.80 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 124 APSKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLKAYEGTLIL 200
Cdd:PRK10619 128 ARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVV 207
|
90
....*....|....*.
gi 492309081 201 ISHDRDFLDAITDHIL 216
Cdd:PRK10619 208 VTHEMGFARHVSSHVI 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
307-504 |
1.65e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP--------LLAGER------KASE 372
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEElqasniRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 373 LLNIGYFaqHQmdaldghaspmlQLARIADKQISEATlrsFLGSFGFSGERMD----------------------TPCES 430
Cdd:PRK13549 81 RAGIAII--HQ------------ELALVKELSVLENI---FLGNEITPGGIMDydamylraqkllaqlkldinpaTPVGN 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 431 FSGGERARLALALIVWQRPNVLILDEPTNHL-DLDMRHALSMaLQDFEG---AVVLVSHERQLIASVCDELLLVHGGK 504
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLLDI-IRDLKAhgiACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
138-204 |
1.82e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.62 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 138 LENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILISHD 204
Cdd:PRK14243 141 VKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
149-204 |
2.22e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 2.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492309081 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLedwLKAYEGT----LILISHD 204
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqILAL---LKSLQQKhqlaYLFISHD 485
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
138-223 |
2.35e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.87 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 138 LENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL----KAYEGTLILISHDRDFLDAITD 213
Cdd:PRK10070 154 LENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHDLDEAMRIGD 233
|
90
....*....|
gi 492309081 214 HILHIENQEL 223
Cdd:PRK10070 234 RIAIMQNGEV 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
138-240 |
2.40e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 43.08 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 138 LENQLRLN--VESF----SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEGTLI---LISHDRDFL 208
Cdd:PRK11124 125 LLERLRLKpyADRFplhlSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqvIVTHEVEVA 204
|
90 100 110
....*....|....*....|....*....|..
gi 492309081 209 DAITDHILHIENQELtLYTGNYSTFETTRSER 240
Cdd:PRK11124 205 RKTASRVVYMENGHI-VEQGDASCFTQPQTEA 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
150-203 |
2.60e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.05 E-value: 2.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLedwLKAY--EGTLILISH 203
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqILEL---LAEHaqNKTVLMITH 532
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
427-527 |
2.62e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 427 PCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRH---ALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGG 503
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
90 100
....*....|....*....|....
gi 492309081 504 KCTefeGDLQDyakwlREARQQQI 527
Cdd:PRK13549 482 KLK---GDLIN-----HNLTQEQV 497
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
149-204 |
2.70e-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: 2.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDaiLwLEDwLKAYEG-TLILISHD 204
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqiLN--L-LKD-LQRELGlAILFITHD 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
138-213 |
2.81e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.10 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 138 LENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITD 213
Cdd:PRK14258 140 IKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLSD 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
150-220 |
2.83e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 43.55 E-value: 2.83e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDL---DAIL-WLEDWLKAYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkAEILpYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
119-233 |
2.99e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 43.30 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 119 IHGYSAPSKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-----------LDAilwl 187
Cdd:PRK13631 147 VKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgehemmqliLDA---- 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 492309081 188 edwlKAYEGTLILISHDRDFLDAITDHILHIENQELTLYTGNYSTF 233
Cdd:PRK13631 223 ----KANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
305-462 |
3.40e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 43.06 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 305 TKMSSPLLTLDNASIGYGD--KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLPLLAGERK------ASELL-- 374
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiSKENLke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 ---NIGYFAQH----------QMDALDGHASPMLQLARIADKqISEATLRSFLGSFgfsgerMDTPCESFSGGERARLAL 441
Cdd:PRK13632 81 irkKIGIIFQNpdnqfigatvEDDIAFGLENKKVPPKKMKDI-IDDLAKKVGMEDY------LDKEPQNLSGGQKQRVAI 153
|
170 180
....*....|....*....|.
gi 492309081 442 ALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLD 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
314-458 |
3.59e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 314 LDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLikslvgdLPLLAGERK----ASELL--------------- 374
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL-------LSLIAGARKiqqgRVEVLggdmadarhrravcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 375 ---------------------NIGYFAQhqmdaLDGHASPMLQlARIADkqISEAT-LRSFLgsfgfsgermDTPCESFS 432
Cdd:NF033858 77 riaympqglgknlyptlsvfeNLDFFGR-----LFGQDAAERR-RRIDE--LLRATgLAPFA----------DRPAGKLS 138
|
170 180
....*....|....*....|....*...
gi 492309081 433 GGERARLAL--ALIvwQRPNVLILDEPT 458
Cdd:NF033858 139 GGMKQKLGLccALI--HDPDLLILDEPT 164
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
307-507 |
3.65e-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: 43.52 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 307 MSSPLLTLDNASIGYGD----KQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDLP----------LLAGErkasE 372
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaahpsgsiLFDGQ----D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 373 LLN-------------IGYFAQHQMDALDghasPmlqLARIAdKQISEATLRSFlgsfGFSGE----------------- 422
Cdd:COG4172 78 LLGlserelrrirgnrIAMIFQEPMTSLN----P---LHTIG-KQIAEVLRLHR----GLSGAaararalellervgipd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 423 ---RMDT-PCEsFSGGERAR----LALALivwqRPNVLILDEPTNHLD-------LDmrhaLSMALQDFEG-AVVLVSHE 486
Cdd:COG4172 146 perRLDAyPHQ-LSGGQRQRvmiaMALAN----EPDLLIADEPTTALDvtvqaqiLD----LLKDLQRELGmALLLITHD 216
|
250 260
....*....|....*....|.
gi 492309081 487 RQLIASVCDELLLVHGGKCTE 507
Cdd:COG4172 217 LGVVRRFADRVAVMRQGEIVE 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
3.80e-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: 43.16 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT-------------RPTGwTVA 67
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgrdvtglppekRNVG-MVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 68 -------HM--AQEV----KALDMPAidfvlsgdeefwdiqnklaqpdqltdfelaklhgrfDEIHgysapSKAAQLMA- 133
Cdd:COG3842 84 qdyalfpHLtvAENVafglRMRGVPK------------------------------------AEIR-----ARVAELLEl 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 134 -GLGFLEN----QLrlnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA----ILWLEDWLKAYEGTLILISHD 204
Cdd:COG3842 123 vGLEGLADryphQL-------SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELGITFIYVTHD 195
|
250
....*....|...
gi 492309081 205 RDflDAIT--DHI 215
Cdd:COG3842 196 QE--EALAlaDRI 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-215 |
4.47e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 14 RVLfQKASMQLHPGwKI-GLTGVNGAGKSTLFAALLGSLGADEGSLT------RPTGWTVAHMA------QEvkaldmpa 80
Cdd:COG1129 18 KAL-DGVSLELRPG-EVhALLGENGAGKSTLMKILSGVYQPDSGEILldgepvRFRSPRDAQAAgiaiihQE-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 idfvlsgdeefwdiqnkLAQPDQLT-------DFELAKlHGRFD--EIHgysapSKAAQLMAGLGfLENQLRLNVESFSG 151
Cdd:COG1129 88 -----------------LNLVPNLSvaeniflGREPRR-GGLIDwrAMR-----RRARELLARLG-LDIDPDTPVGDLSV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 152 GWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWL----EDwLKAyEG-TLILISHdrdFLD---AITDHI 215
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriiRR-LKA-QGvAIIYISH---RLDevfEIADRV 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
303-462 |
4.67e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.33 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 303 EPTKMSSPLLTLDNASIGYGDKQIAEKIRLQITPNSRIGLLGMNGAGKSTLIKSL-----------------VGDLPLLA 365
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgarvegeilLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 366 GERKASEL-LNIGY-------FaqhqmdaldghasPM---------LQLARIADK----QISEATLRSflgsfgfSG--- 421
Cdd:COG1117 83 PDVDVVELrRRVGMvfqkpnpF-------------PKsiydnvaygLRLHGIKSKseldEIVEESLRK-------AAlwd 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492309081 422 ---ERMDTPCESFSGGERARL----ALALivwqRPNVLILDEPTNHLD 462
Cdd:COG1117 143 evkDRLKKSALGLSGGQQQRLciarALAV----EPEVLLMDEPTSALD 186
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-218 |
4.80e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 42.36 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 32 LTGVNGAGKSTLFAALLGslgadegsltrptgwtvaHMAQEVKA----------LDMPAidfvlsgdEE------FWDIQ 95
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMG------------------HPKYEVTSgsilldgediLELSP--------DEraragiFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 96 NKLAQPD-QLTDF-ELAKLHGRFDEIHGYSAPSKAAQLMAGLGFLENQLRLNV-ESFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:COG0396 85 YPVEIPGvSVSNFlRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492309081 173 DEPTNHLDLDAILWLEDWLKAY---EGTLILISHDRDFLDAITDHILHI 218
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILDYIKPDFVHV 213
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
431-546 |
5.20e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 431 FSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF--EGAVVLVS----HERQLIA---SVCDELLLVH 501
Cdd:NF000106 145 YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLTtqymEEAEQLAhelTVIDRGRVIA 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 492309081 502 GGKCTEFEGDLQDYAKWLREARQQQINAQT-AVAQNNSSSAAPAPA 546
Cdd:NF000106 225 DGKVDELKTKVGGRTLQIRPAHAAELDRMVgAIAQAGLDGIAGATA 270
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
300-507 |
5.32e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.71 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 300 SFREPTKMSSPLLTLDNASIGYGDKQIAekirLQITPNSRIGLLGMNGAGKSTLIKSL--------------------VG 359
Cdd:PRK10070 21 AFKYIEQGLSKEQILEKTGLSLGVKDAS----LAIEEGEIFVIMGLSGSGKSTMVRLLnrlieptrgqvlidgvdiakIS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 360 DLPLLAGERKASELLNIGYFAQHQMDALDGHASPMlQLARIADKQISEATLRSfLGSFGFSGERMDTPCEsFSGGERARL 439
Cdd:PRK10070 97 DAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGM-ELAGINAEERREKALDA-LRQVGLENYAHSYPDE-LSGGMRQRV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492309081 440 ALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK10070 174 GLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
432-504 |
5.47e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.41 E-value: 5.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 432 SGGERARLALALIVWQRPNVLILDEPTNHLD----LDMRHALSMALQDFEGAVVLVSHERQLIAsVCDELLLVHGGK 504
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
330-504 |
6.47e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.00 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 330 IRLQITPNSRIGLLGMNGAGKSTLIKSLVG------DLPLLAGERKASELL-----NIGYFAQHQMD------------- 385
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGlfeefeGKVKIDGELLTAENVwnlrrKIGMVFQNPDNqfvgatveddvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 386 ALDGHASPMLQLARIADKQISEATLRSFlgsfgfsgeRMDTPCEsFSGGERARLALALIVWQRPNVLILDEPTNHLDLDM 465
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDF---------KTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492309081 466 RHALSMALQDFEG----AVVLVSHERQLIASvCDELLLVHGGK 504
Cdd:PRK13642 176 RQEIMRVIHEIKEkyqlTVLSITHDLDEAAS-SDRILVMKAGE 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-180 |
6.51e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 34 GVNGAGKSTLFAALLGSLGADEGSLtrptgW---TVAHMAQEVKALDMPAIDFVLSGDEEfwdiqnklaqpdqltdfELA 110
Cdd:PTZ00243 693 GATGSGKSTLLQSLLSQFEISEGRV-----WaerSIAYVPQQAWIMNATVRGNILFFDEE-----------------DAA 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 111 KLHgrfDEIHGYSAPSKAAQLMAGLgflENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PTZ00243 751 RLA---DAVRVSQLEADLAQLGGGL---ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-180 |
6.80e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.49 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSL---------TRPTGWTVAHMAQEVKALDMPAIDfvlsgdeef 91
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhttTPPSRRPVSMLFQENNLFSHLTVA--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 92 wdiQN---------KL--AQPDQLTDfelaklhgrfdeihgysapskaaqlMAGLGFLENQL-RLNVEsFSGGWRMRLNL 159
Cdd:PRK10771 90 ---QNiglglnpglKLnaAQREKLHA-------------------------IARQMGIEDLLaRLPGQ-LSGGQRQRVAL 140
|
170 180
....*....|....*....|.
gi 492309081 160 ARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALD 161
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-204 |
6.88e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.99 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 14 RVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLgadegsltrPTGwtVAHMAQEVKALDMPAIDFVLSGDEEFWD 93
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL---------PAG--VRQTAGRVLLDGKPVAPCALRGRKIATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 94 IQNKLAQPDQLTDFelaKLHGRfDEIHGYSAPSKAAQLMA-----GLGFLENQLRLNVESFSGGWRMRLNLARTLMSRSD 168
Cdd:PRK10418 85 MQNPRSAFNPLHTM---HTHAR-ETCLALGKPADDATLTAaleavGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492309081 169 LLLLDEPTNHLDLDA---ILWLEDWLKAYEGT-LILISHD 204
Cdd:PRK10418 161 FIIADEPTTDLDVVAqarILDLLESIVQKRALgMLLVTHD 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
138-203 |
7.29e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 7.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 138 LENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY--EGTLILISH 203
Cdd:PRK14267 139 VKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
143-241 |
7.29e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 143 RLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAYEGTLILISHDRDFLDAITDHILHIE 219
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAkfeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMS 465
|
90 100
....*....|....*....|..
gi 492309081 220 NQELtlyTGNYSTFETTRSERL 241
Cdd:PRK10982 466 NGLV---AGIVDTKTTTQNEIL 484
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-185 |
7.58e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRV--LFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTrPTGWTVAHM--AQEVKALD 77
Cdd:PLN03130 1238 IKFEDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-IDGCDISKFglMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 78 M-PAIDFVLSGDEEF-WDIQNKLAQPDQLTDFELAKLHgrfDEIHGYSAPSKAAQLMAGlgflenqlrlnvESFSGGWRM 155
Cdd:PLN03130 1317 IiPQAPVLFSGTVRFnLDPFNEHNDADLWESLERAHLK---DVIRRNSLGLDAEVSEAG------------ENFSVGQRQ 1381
|
170 180 190
....*....|....*....|....*....|..
gi 492309081 156 RLNLARTLMSRSDLLLLDEPTNHLDL--DAIL 185
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVrtDALI 1413
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
340-507 |
8.34e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 340 IGLLGMNGAGKSTLIKSLVGDLPLLAGE----RKASELLNIGYFAQH-QMDALDGHAS--PMLQLARIAD---------- 402
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGEllidDHPLHFGDYSYRSQRiRMIFQDPSTSlnPRQRISQILDfplrlntdle 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 403 -----KQISEaTLRSFlgsfGFSGERMDTPCESFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHA---LSMALQ 474
Cdd:PRK15112 122 peqreKQIIE-TLRQV----GLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQlinLMLELQ 196
|
170 180 190
....*....|....*....|....*....|....
gi 492309081 475 DFEG-AVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:PRK15112 197 EKQGiSYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
124-206 |
9.44e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.61 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 124 APSKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLKAYEGTLIL 200
Cdd:PRK13651 141 AKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIIL 220
|
....*.
gi 492309081 201 ISHDRD 206
Cdd:PRK13651 221 VTHDLD 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-176 |
1.08e-03 |
|
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: 41.12 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGG-RVLFQkASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLT---RP-TGWTVAHMAQ---- 71
Cdd:COG0410 3 MLEVENLHAGYGGiHVLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgEDiTGLPPHRIARlgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 72 ------EVKA-------LDMPAidFVLSGDEEF-WDIQnklaqpDQLTDF-ELAKLHGRfdeihgysapsKAAQLmaglg 136
Cdd:COG0410 82 yvpegrRIFPsltveenLLLGA--YARRDRAEVrADLE------RVYELFpRLKERRRQ-----------RAGTL----- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492309081 137 flenqlrlnvesfSGGWRMRLNLARTLMSRSDLLLLDEPT 176
Cdd:COG0410 138 -------------SGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
127-206 |
1.14e-03 |
|
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: 41.09 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 127 KAAQLMAGLGfLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD-------LDAILWLEDWLKAyegTLI 199
Cdd:cd03294 140 RAAEALELVG-LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAELQK---TIV 215
|
....*..
gi 492309081 200 LISHDRD 206
Cdd:cd03294 216 FITHDLD 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
114-180 |
1.17e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 114 GRFDEIHGYSAPSKAAQLMAGLGFLENQLRLNVEsFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:NF000106 111 GR*LDLSRKDARARADELLERFSLTEAAGRAAAK-YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-204 |
1.28e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 30 IGLTGVNGAGKSTLFAALLGSLGADEGSLTRPTGWTVAHMAQEvkaldmPAIDFVLSGDEEFWDI--------QNKLAQP 101
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEE------ASVELEFEHGGKRYRIerrqgefaEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 102 DQLTDF--------ELAKLHGRFDEIHGySAPSKAAQLMAGLGFLENQLRL-----NVESFSGGWRMRLNLARTLMsrsd 168
Cdd:COG0419 100 SERKEAlkrllgleIYEELKERLKELEE-ALESALEELAELQKLKQEILAQlsgldPIETLSGGERLRLALADLLS---- 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 492309081 169 lLLLDepTNHLDLDAILWLEDWLKAyegtLILISHD 204
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
150-220 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWL----KAYEGTLILISHDRDFLDAITDHILHIEN 220
Cdd:TIGR01184 116 SGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDVDEALLLSDRVVMLTN 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-215 |
1.67e-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: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 2 IQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLtrptgwtvahMAQEVKALDMPA- 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI----------LLDGKDITNLPPh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 ---IDFVLsgdeefwdiQNKLAQPdQLTDFE-------LAKLHGrfDEIHgysapSKAAQLMAGLGfLENQLRLNVESFS 150
Cdd:cd03300 71 krpVNTVF---------QNYALFP-HLTVFEniafglrLKKLPK--AEIK-----ERVAEALDLVQ-LEGYANRKPSQLS 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492309081 151 GGWRMRLNLARTLMSRSDLLLLDEPTNHLDL----DAILWLEDWLKAYEGTLILISHDRDFLDAITDHI 215
Cdd:cd03300 133 GGQQQRVAIARALVNEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHDQEEALTMSDRI 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-203 |
1.69e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 1.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492309081 138 LENQLRLNV----ESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLE----DWLKAYEGTLILISH 203
Cdd:PTZ00265 1344 LPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH 1417
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
362-498 |
1.70e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 362 PLLAGERKASELLNIGYFAQHQMDALDGHA----SPMLQLARIADKqiSEAtlrsfLGSFGFSGERMDTPCESFSGGERA 437
Cdd:PRK00635 744 PSCLGKRFLPQVLEVRYKGKNIADILEMTAyeaeKFFLDEPSIHEK--IHA-----LCSLGLDYLPLGRPLSSLSGGEIQ 816
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492309081 438 RLALA---LIVWQRPNVLILDEPTNHLDLDMRHALSMALQD--FEGAVVLVSHERQLIASVCDELL 498
Cdd:PRK00635 817 RLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSltHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
150-216 |
1.71e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 40.80 E-value: 1.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWL-EDWLKAYEGTLILISHDRDFLDAITDHIL 216
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgRDEILNKiKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-180 |
1.86e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 40.45 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 1 MIQFDQVSLRRGGRVLFQKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTRptgwtvahmaqEVKALDMPA 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL-----------DGKPVEGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 81 IDF-VLSGDEEFWDIQNklAQPDQLTDFELAKLhGRFDEIHgysapsKAAQLMAGLGFLENQLRLnVESFSGGWRMRLNL 159
Cdd:PRK11248 70 AERgVVFQNEGLLPWRN--VQDNVAFGLQLAGV-EKMQRLE------IAHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGI 139
|
170 180
....*....|....*....|.
gi 492309081 160 ARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALD 160
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
149-204 |
1.87e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.85 E-value: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 149 FSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG--TLILISHD 204
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
430-505 |
1.98e-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: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 430 SFSGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALsmalqdFEGAV--VLVSHERQLIAS------VCDELLLVH 501
Cdd:cd03291 159 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI------FESCVckLMANKTRILVTSkmehlkKADKILILH 232
|
....
gi 492309081 502 GGKC 505
Cdd:cd03291 233 EGSS 236
|
|
| 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 492309081 519 LREARQQQINAQTAVAQNNSSSAApapAKVDKEAQRKEAARRREQTRPIRKNIEKVESQIEKLQPQLAKIEESLADTSLY 598
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQLQA---AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144
|
90 100
....*....|....*....|....
gi 492309081 599 EAARKDDLLKLMNEQTELKAKLEQ 622
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAA 168
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
432-462 |
2.38e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.45 E-value: 2.38e-03
10 20 30
....*....|....*....|....*....|.
gi 492309081 432 SGGERARLALALIVWQRPNVLILDEPTNHLD 462
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-60 |
2.44e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 2.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 492309081 18 QKASMQLHPGWKIGLTGVNGAGKSTLFAALLGSLGADEGSLTR 60
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDR 83
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
138-203 |
2.51e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 2.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 138 LENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAI-----LWLEdwLKAyEGTLILISH 203
Cdd:PRK14247 136 VKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTakiesLFLE--LKK-DMTIVLVTH 203
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-216 |
2.59e-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: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 134 GLGFLenQLRLNVESFSGGWRMRLNLARTLMSRSD---LLLLDEPTNHLDLDAILWLED---WLKAYEGTLILISHDrdf 207
Cdd:TIGR00630 817 GLGYI--RLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEvlqRLVDKGNTVVVIEHN--- 891
|
90
....*....|.
gi 492309081 208 LDAI--TDHIL 216
Cdd:TIGR00630 892 LDVIktADYII 902
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
148-240 |
2.94e-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: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 148 SFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAY----EGTLILISHDRDFLDAITDHILHIENQel 223
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDRIHVFEGE-- 148
|
90
....*....|....*..
gi 492309081 224 tlyTGNYSTFETTRSER 240
Cdd:cd03222 149 ---PGVYGIASQPKGTR 162
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-241 |
2.97e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 40.00 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 22 MQLHPGWKIGLTGVNGAGKSTLFAALLGSLGAD----------------EGSLTRPTGWTVAHMA---QEVKALD-MPAI 81
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshiellgrtvqrEGRLARDIRKSRANTGyifQQFNLVNrLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 82 DFVLSG---DEEFWDIQNKLAQPDQltdfelaklhgrfdEIHGYSAPSKAaqlmaGLGFLENQlrlNVESFSGGWRMRLN 158
Cdd:PRK09984 105 ENVLIGalgSTPFWRTCFSWFTREQ--------------KQRALQALTRV-----GMVHFAHQ---RVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 159 LARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLKAYEG----TLILISHDRDFLDAITDHILHIEnQELTLYTGNYSTFE 234
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALR-QGHVFYDGSSQQFD 241
|
....*..
gi 492309081 235 TTRSERL 241
Cdd:PRK09984 242 NERFDHL 248
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
127-223 |
3.17e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.39 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 127 KAAQLMAGLGF---LENQLRL----NVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLD---AILWLEDWLKAyEG 196
Cdd:PRK11176 452 EAARMAYAMDFinkMDNGLDTvigeNGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTEserAIQAALDELQK-NR 530
|
90 100
....*....|....*....|....*....
gi 492309081 197 TLILISHDrdfLDAI--TDHILHIENQEL 223
Cdd:PRK11176 531 TSLVIAHR---LSTIekADEILVVEDGEI 556
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-209 |
3.33e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.84 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 134 GLGFLenQLRLNVESFSGGWRMRLNLARTLMSRSD--LLLLDEPTNHLDLDAILWLEDWLKAY--EG-TLILISHDRDFL 208
Cdd:cd03238 75 GLGYL--TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidLGnTVILIEHNLDVL 152
|
.
gi 492309081 209 D 209
Cdd:cd03238 153 S 153
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
329-492 |
3.39e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.84 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 329 KIRLQITPNSRIGLLGMNGAGKSTLIKSLVGDlpllAGERKASELLNIgyFAQHQMDALDghaspmlQLARIADKQISEA 408
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPK--FSRNKLIFID-------QLQFLIDVGLGYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 409 TLrsflgsfgfsGERMDTpcesFSGGERARLALA--LIVWQRPNVLILDEPTNHLDL-DMRHALSM--ALQDFEGAVVLV 483
Cdd:cd03238 80 TL----------GQKLST----LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQqDINQLLEVikGLIDLGNTVILI 145
|
....*....
gi 492309081 484 SHERQLIAS 492
Cdd:cd03238 146 EHNLDVLSS 154
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
126-206 |
3.42e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 39.76 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 126 SKAAQLMAGLGFLENQLRLNVESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLD---LDAILWLEDWLKAYEG-TLILI 201
Cdd:PRK13646 123 NYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqsKRQVMRLLKSLQTDENkTIILV 202
|
....*
gi 492309081 202 SHDRD 206
Cdd:PRK13646 203 SHDMN 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
150-220 |
4.78e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 39.33 E-value: 4.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD----LDAILWLEDWLKAYEGTLILISHDRDFLdAITDHILHIEN 220
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKN 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
150-180 |
4.98e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 39.63 E-value: 4.98e-03
10 20 30
....*....|....*....|....*....|.
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLD 180
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
126-206 |
5.65e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 39.30 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 126 SKAAQL--MAGLGFLEN----QLrlnvesfSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDWLK----AYE 195
Cdd:PRK10851 115 AKVTQLleMVQLAHLADrypaQL-------SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlheELK 187
|
90
....*....|.
gi 492309081 196 GTLILISHDRD 206
Cdd:PRK10851 188 FTSVFVTHDQE 198
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
142-229 |
5.83e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 142 LRLNV-ESFSGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDAILWLE---DWLKAYEGTLILISHDRDFLDAITDHILH 217
Cdd:CHL00131 144 LSRNVnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYIKPDYVH 223
|
90
....*....|..
gi 492309081 218 IENQELTLYTGN 229
Cdd:CHL00131 224 VMQNGKIIKTGD 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
150-216 |
5.93e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 5.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 150 SGGWRMRLNLARTLMSRSDLLLLDEPTNHLDLDA---ILWLEDWLKAyEG-TLILISHDRDFLDAITDHIL 216
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAkkeIYQLINQFKA-EGlSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
432-485 |
6.06e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 38.92 E-value: 6.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 492309081 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDFEG----AVVLVSH 485
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH 203
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
146-210 |
6.25e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 146 VESFSGGWRM------RLNLARTLMSRSDLLLLDEPTNHLDLDAILWLEDW----LKAYEG--TLILISHDRDFLDA 210
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIieysLKDSSDipQVIMISHHRELLSV 875
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
432-507 |
7.76e-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: 7.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492309081 432 SGGERARLALALIVWQRPNVLILDEPTNHLDLDMRHALSMALQDF-EGAVVLVSHERQLIASVCDELLLVHGGKCTE 507
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAmKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-228 |
9.47e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.18 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 21 SMQLHPGWKIGLTGVNGAGKSTLFAALLGslgadegsLTRPTGWTVAHMAQEVKALDMPAIDFVLSGdeefwdiqnklaq 100
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTG--------LYQPQSGEILLDGKPVTAEQPEDYRKLFSA------------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 101 pdQLTDFELaklhgrFDEIHGYSA-PSKAAQLMAGLGFLENQLRLNVE-------SFSGGWRMRLNLARTLMSRSDLLLL 172
Cdd:PRK10522 402 --VFTDFHL------FDQLLGPEGkPANPALVEKWLERLKMAHKLELEdgrisnlKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492309081 173 DEptnhldldailWLED---------------WLKAYEGTLILISHDRDFLDAiTDHILHIENQELTLYTG 228
Cdd:PRK10522 474 DE-----------WAADqdphfrrefyqvllpLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSELTG 532
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
524-622 |
9.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.84 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492309081 524 QQQINAQtavaQNNSSSAapapakvdKEAQRKEAARRREQTRPIRKNIEKVESQIEKLQPQLAKIEESLADTSlyeaark 603
Cdd:PHA02562 194 QQQIKTY----NKNIEEQ--------RKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS------- 254
|
90
....*....|....*....
gi 492309081 604 DDLLKLMNEQTELKAKLEQ 622
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQ 273
|
|
| |
