|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-574 |
6.15e-129 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 387.50 E-value: 6.15e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 19 VSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPLRVGLLYQEPPFAPHDT 98
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS---IPKGLRIGYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 VAQAVESAVRTVRDAasaVDRTADALARAPEDEGAATAYAAALDTAERIGAWDVDTRIDVTLDGLGLGGVDRDRSTGALS 178
Cdd:COG0488 78 VLDTVLDGDAELRAL---EAELEELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDpaprphavtsd 258
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD----------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 259 lvgDGTgtgigVTRFGGTYSQYVLARMDTRERWERTYRDEQAQLKKLRAAVREQqtvghsgrspKTEGRAAKKfyadrna 338
Cdd:COG0488 224 ---RGK-----LTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRF----------RAKARKAKQ------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 339 tvvsrrvngARARLATVED-EQIRKPPRELYFQgltagLSGSEAAlhRTG-PVLTASAAEVA--GRM--APVSLTVSAGE 412
Cdd:COG0488 279 ---------AQSRIKALEKlEREEPPRRDKTVE-----IRFPPPE--RLGkKVLELEGLSKSygDKTllDDLSLRIDRGD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 413 SWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQD-ATLpgaDPEHTaahIYHEL--VGEDRAETVP---L 486
Cdd:COG0488 343 RIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHqEEL---DPDKT---VLDELrdGAPGGTEQEVrgyL 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 487 GTFgLLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPGTVLVASHDRWLRRNW 566
Cdd:COG0488 417 GRF-LFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
|
....*...
gi 1586061923 567 TGRDLALE 574
Cdd:COG0488 496 ATRILEFE 503
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-561 |
7.81e-73 |
|
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: 242.92 E-value: 7.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 21 GISASYGSHR-VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvglGDPLRVGLLYQEPPFAPHDTV 99
Cdd:TIGR03719 9 RVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP---QPGIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 100 AQAVESAVRTVRDAASAVDRTADALARapEDEGAATAYAAALDTAERI---GAWDVDTRIDVTLDGLGLGGVDRDRSTga 176
Cdd:TIGR03719 86 RENVEEGVAEIKDALDRFNEISAKYAE--PDADFDKLAAEQAELQEIIdaaDAWDLDSQLEIAMDALRCPPWDADVTK-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDpaprphavt 256
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELD--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 257 sdlvgdgTGTGIGvtrFGGTYSQYVLARmdtRERWERTYRDEQAQLKKLRaavREQQTVghsGRSPKteGRAAKkfyadr 336
Cdd:TIGR03719 233 -------RGRGIP---WEGNYSSWLEQK---QKRLEQEEKEESARQKTLK---RELEWV---RQSPK--GRQAK------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 337 natvvsrrvngARARLATVE-----DEQIRKPPRELYFQgltaglsgseaalhrTGPVLTASAAEVAG-------RM--A 402
Cdd:TIGR03719 286 -----------SKARLARYEellsqEFQKRNETAEIYIP---------------PGPRLGDKVIEAENltkafgdKLliD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQdaTLPGADPEHTaahIYHELV-GEDRA 481
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ--SRDALDPNKT---VWEEISgGLDII 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 482 E----TVP----LGTFGlLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPGTV 553
Cdd:TIGR03719 415 KlgkrEIPsrayVGRFN-FKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCA 493
|
....*...
gi 1586061923 554 LVASHDRW 561
Cdd:TIGR03719 494 VVISHDRW 501
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-561 |
1.41e-65 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 223.46 E-value: 1.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 21 GISASYGSHR-VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPLRVGLLYQEPPFAPHDTV 99
Cdd:PRK11819 11 RVSKVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR---PAPGIKVGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 100 AQAVESAVRTVRDAASAVDRTADALARAPEDegAATAYAAALDTAERI---GAWDVDTRIDVTLDGLGLGgvDRDRSTGA 176
Cdd:PRK11819 88 RENVEEGVAEVKAALDRFNEIYAAYAEPDAD--FDALAAEQGELQEIIdaaDAWDLDSQLEIAMDALRCP--PWDAKVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDpapRphavt 256
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELD---R----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 257 sdlvgdgtGTGIGvtrFGGTYSQYVLARmdtRERWERTYRDEQAQLKKLRaavREQQTVghsgR-SPKteGRAAKkfyad 335
Cdd:PRK11819 236 --------GRGIP---WEGNYSSWLEQK---AKRLAQEEKQEAARQKALK---RELEWV----RqSPK--ARQAK----- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 336 rnatvvsrrvngARARLATVE-----DEQIRKPPRELYFQgltaglsgseaalhrTGPVLTASAAEVAGrmapvsLTVSA 410
Cdd:PRK11819 288 ------------SKARLARYEellseEYQKRNETNEIFIP---------------PGPRLGDKVIEAEN------LSKSF 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 411 GESWLIT---------------GSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQD-ATLpgaDPEHTaahIYHE 474
Cdd:PRK11819 335 GDRLLIDdlsfslppggivgiiGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSrDAL---DPNKT---VWEE 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 475 LV-GEDRAE----TVP----LGTFGlLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAA 545
Cdd:PRK11819 409 ISgGLDIIKvgnrEIPsrayVGRFN-FKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEA 487
|
570
....*....|....*.
gi 1586061923 546 VPDYPGTVLVASHDRW 561
Cdd:PRK11819 488 LLEFPGCAVVISHDRW 503
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-560 |
4.82e-53 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 191.32 E-value: 4.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPLRVGLLYQEPPFAPH 96
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII---YEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVAQAVESAVRTVRDAASAVDRTADALARAPEDEgAATAYAAALDTAERIGAWDVDTRIDVTLDGLGLggvDRDRSTGA 176
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEK-NLNELAKLQEQLDHHNLWQLENRINEVLAQLGL---DPDAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDpapRPHAVT 256
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLD---RGKLVS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 257 sdlvgdgtgtgigvtrFGGTYSQYvlarMDTRERWERTYRDEQAQL-KKLraavrEQQTV----GHSGRSPKTEG--RAA 329
Cdd:PRK11147 234 ----------------YPGNYDQY----LLEKEEALRVEELQNAEFdRKL-----AQEEVwirqGIKARRTRNEGrvRAL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 330 KKFYADRnatvvsrrvngaRARlatvedeqirkppRELyfQGlTAGLSGSEAAlhRTGP-VLTASAA--EVAGR--MAPV 404
Cdd:PRK11147 289 KALRRER------------SER-------------REV--MG-TAKMQVEEAS--RSGKiVFEMENVnyQIDGKqlVKDF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQ-DATLpgaDPEHTAAhiyhELVGEDRAET 483
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQhRAEL---DPEKTVM----DNLAEGKQEV 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 484 vplgtfgLLAGRDEN------------RR----VGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVP 547
Cdd:PRK11147 412 -------MVNGRPRHvlgylqdflfhpKRamtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
570
....*....|...
gi 1586061923 548 DYPGTVLVASHDR 560
Cdd:PRK11147 485 SYQGTVLLVSHDR 497
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-280 |
5.02e-43 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 161.39 E-value: 5.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPLRVGLLYQEP-PFAP 95
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---LGETVKIGYFDQHQeELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 HDTVAQavesavrTVRDAASAVDRTAdalARApedegaatayaaaldtaerigawdvdtridvTLDGLGLGGVDRDRSTG 175
Cdd:COG0488 393 DKTVLD-------ELRDGAPGGTEQE---VRG-------------------------------YLGRFLFSGDDAFKPVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 176 ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVdldpaprphav 255
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRIL----------- 500
|
250 260
....*....|....*....|....*
gi 1586061923 256 tsdLVGDGtgtgiGVTRFGGTYSQY 280
Cdd:COG0488 501 ---EFEDG-----GVREYPGGYDDY 517
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-562 |
8.53e-40 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 154.63 E-value: 8.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAgLRAPDagevravglGDPLRVGLLYQEPPFAPH 96
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAID---------GIPKNCQILHVEQEVVGD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVA------------QAVESAVRTVRDAASAVDRTADALARAPEDEGAATAYAAALDTA-----ERIGAWDVDTRIDVT 159
Cdd:PLN03073 248 DTTAlqcvlntdiertQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEiykrlELIDAYTAEARAASI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 160 LDGLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTA 239
Cdd:PLN03073 328 LAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 240 VTSLVDLDpaprphavtsdlvgdgtgtGIGVTRFGGTYsqyvlarmDTrerWERTyRDEQaqlkklraaVREQQTVGHSG 319
Cdd:PLN03073 408 VTDILHLH-------------------GQKLVTYKGDY--------DT---FERT-REEQ---------LKNQQKAFESN 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 320 RSPKTEGRA-AKKF-YADRNATVVSRRVNgARARLATVeDEQIRKPPRELYF-----QGLTAGLSGSEAAL-HRTGPVLT 391
Cdd:PLN03073 448 ERSRSHMQAfIDKFrYNAKRASLVQSRIK-ALDRLGHV-DAVVNDPDYKFEFptpddRPGPPIISFSDASFgYPGGPLLF 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 392 AS---AAEVAGRMAPVsltvsageswlitGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQ---DATLPGADPE 465
Cdd:PLN03073 526 KNlnfGIDLDSRIAMV-------------GPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQhhvDGLDLSSNPL 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 466 HTAAHIYHElVGEDRAETvPLGTFGlLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAA 545
Cdd:PLN03073 593 LYMMRCFPG-VPEQKLRA-HLGSFG-VTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669
|
570
....*....|....*..
gi 1586061923 546 VPDYPGTVLVASHDRWL 562
Cdd:PLN03073 670 LVLFQGGVLMVSHDEHL 686
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-560 |
5.59e-39 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 150.04 E-value: 5.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvglgDP-LRVGLLYQEPpFAP 95
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL----DPnERLGKLRQDQ-FAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 H-----DTVAQAVES--AVRTVRDAASAvdrtadaLARAPEDEGaatayaaaldtaerIGAWDVDTRIdVTLDG------ 162
Cdd:PRK15064 77 EeftvlDTVIMGHTElwEVKQERDRIYA-------LPEMSEEDG--------------MKVADLEVKF-AEMDGytaear 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 163 -----LGLGgVDRDRSTGALSG---GQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRA 234
Cdd:PRK15064 135 agellLGVG-IPEEQHYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 235 FLDTAVTSLVDLDpaprphavtsdlvgdgTGTgigVTRFGGTYSQYVLARMDTRERWERTYRDEQAQLKKLRAAVReqqt 314
Cdd:PRK15064 214 FLNSVCTHMADLD----------------YGE---LRVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVS---- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 315 vghsgrspktegraakKFYAdrnatvvsrrvNGARARLATVEDEQIRKPPRE-----------LYFQGltaglsgsEAAL 383
Cdd:PRK15064 271 ----------------RFSA-----------NASKAKQATSRAKQIDKIKLEevkpssrqnpfIRFEQ--------DKKL 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 384 HRTGPVLTASAAEVAGRM--APVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQDATLPG 461
Cdd:PRK15064 316 HRNALEVENLTKGFDNGPlfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDF 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 462 ADPEhTAAHIYHELVGEDRAETVPLGTFG-LLAGRDE-NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLA 539
Cdd:PRK15064 396 ENDL-TLFDWMSQWRQEGDDEQAVRGTLGrLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI 474
|
570 580
....*....|....*....|.
gi 1586061923 540 TQLEAAVPDYPGTVLVASHDR 560
Cdd:PRK15064 475 ESLNMALEKYEGTLIFVSHDR 495
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
17-248 |
5.29e-38 |
|
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: 136.81 E-value: 5.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPLRVGLLYQeppfaph 96
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---WGSTVKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 dtvaqavesavrtvrdaasavdrtadalarapedegaatayaaaldtaerigawdvdtridvtldglglggvdrdrstga 176
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDP 248
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELED 142
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-573 |
5.53e-37 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 145.70 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTD-ISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlgdPLRVGLLYQEPPFAPhdtvaqavESAVR 108
Cdd:PRK10636 14 RVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---NWQLAWVNQETPALP--------QPALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 109 TVRDAASAVDRTADALARAPEdEGAATAYAAALDTAERIGAWDVDTRIDVTLDGLGLGGVDRDRSTGALSGGQRSRLSLA 188
Cdd:PRK10636 83 YVIDGDREYRQLEAQLHDANE-RNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 189 WLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDPAPrphavtsdlvgdgtgtgi 268
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQS------------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 269 gVTRFGGTYSQYVLARMDTRERWERTYRDEQAQLKKLRAAVreqqtvghsgrsPKTEGRAAKKFYADRNATVVSRRVNGA 348
Cdd:PRK10636 224 -LFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYI------------DRFRAKATKAKQAQSRIKMLERMELIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 349 RARLATVEDEQIRKP---PRELY-FQGLTAGLsGSEAALHRtgpvltasaaevagrmapVSLTVSAGESWLITGSNGVGK 424
Cdd:PRK10636 291 PAHVDNPFHFSFRAPeslPNPLLkMEKVSAGY-GDRIILDS------------------IKLNLVPGSRIGLLGRNGAGK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 425 STLLSLFARRLEPTRGSVHAAPGVRVGLLDQ-DATLPGADP---EHTAAHIYHELVGEDRAEtvpLGTFGlLAGRDENRR 500
Cdd:PRK10636 352 STLIKLLAGELAPVSGEIGLAKGIKLGYFAQhQLEFLRADEsplQHLARLAPQELEQKLRDY---LGGFG-FQGDKVTEE 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 501 VGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPGTVLVASHDRWLRRNwTGRDLAL 573
Cdd:PRK10636 428 TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRS-TTDDLYL 499
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
17-232 |
1.83e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.96 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgDPL--------RVGLLY 88
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE-DVArdpaevrrRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 QEPPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGV 168
Cdd:COG1131 80 QEPALYPDLTVRENLRFFAR---------------LYGLPRKE--------------------ARERIDELLELFGLTDA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 169 dRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP---VLLASHD 232
Cdd:COG1131 125 -ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgktVLLSTHY 190
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-232 |
7.26e-36 |
|
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: 134.60 E-value: 7.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG---DPL----RVGLLYQ 89
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkEPRearrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 90 EPPFAPHdtvaqavesavRTVRDaasAVDRTAdALARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGvD 169
Cdd:COG4555 82 ERGLYDR-----------LTVRE---NIRYFA-ELYGLFDEE--------------------LKKRIEELIELLGLEE-F 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 170 RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP---VLLASHD 232
Cdd:COG4555 126 LDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgktVLFSSHI 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-231 |
6.82e-35 |
|
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: 130.80 E-value: 6.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG-----LGDPL-RVGLLYQE 90
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkNIEALrRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHdtvaqavesavRTVRDAAsavdRTADALARAPedegaatayaaaldtaerigawdvDTRIDVTLDGLGLGGVDR 170
Cdd:cd03268 81 PGFYPN-----------LTARENL----RLLARLLGIR------------------------KKRIDEVLDVVGLKDSAK 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 171 DRsTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH---GPVLLASH 231
Cdd:cd03268 122 KK-VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSH 184
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
15-239 |
6.18e-33 |
|
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: 125.28 E-value: 6.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPL-------RVGLL 87
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDaredyrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPPFAPHDTVAQAVESAVRtvrdaASAVDRTADALARApedegaatayaaaldtaerigawdvdtridvtLDGLGLGG 167
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAA-----LYGLRADREAIDEA--------------------------------LEAVGLAG 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 168 VdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH---GPVLLASHDRAFLDTA 239
Cdd:COG4133 124 L-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-208 |
1.52e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 122.84 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgL-GDPL----------RVG 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL---LdGRDLaslsrrelarRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAVesavrtvrdaasavdrtadALARAPedegaatayaaaldtaeRIGAWDVDTRIDVT-----L 160
Cdd:COG1120 79 YVPQEPPAPFGLTVRELV-------------------ALGRYP-----------------HLGLFGRPSAEDREaveeaL 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586061923 161 DGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG1120 123 ERTGLEHL-ADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-232 |
2.35e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrvglLYQEPPFAPH 96
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVR------------LFGKPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVA---QAVESAVR---TVRDAAsavdrtadALARAPEdegaatayaaaLDTAERIGAWDVDtRIDVTLDGLGLGGVdR 170
Cdd:COG1121 75 RRIGyvpQRAEVDWDfpiTVRDVV--------LMGRYGR-----------RGLFRRPSRADRE-AVDEALERVGLEDL-A 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 171 DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG---PVLLASHD 232
Cdd:COG1121 134 DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-236 |
3.86e-31 |
|
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: 120.26 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHR--VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL---GDPL-----RVGLL 87
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltKLSLkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPpfaphDTvaQAVESAVRtvrdaasavdrtaDALARAPEDEGAATAyaaaldtaerigawDVDTRIDVTLDGLGLGG 167
Cdd:cd03225 81 FQNP-----DD--QFFGPTVE-------------EEVAFGLENLGLPEE--------------EIEERVEEALELVGLEG 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 168 VdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG---PVLLASHDRAFL 236
Cdd:cd03225 127 L-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLL 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
403-574 |
9.43e-31 |
|
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: 116.78 E-value: 9.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQdatlpgadpehtaahiyhelvgedrae 482
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 483 tvplgtfgllagrdenrrvgeLSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPGTVLVASHDRWL 562
Cdd:cd03221 71 ---------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYF 129
|
170
....*....|..
gi 1586061923 563 RRNWTGRDLALE 574
Cdd:cd03221 130 LDQVATKIIELE 141
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-236 |
1.32e-30 |
|
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: 119.36 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL----------RVG 85
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV--DGKDItkknlrelrrKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPpfaphDTvaQAVESavrTVRDaasavDrtadaLARAPEDEGAATAyaaaldtaerigawDVDTRIDVTLDGLGL 165
Cdd:COG1122 79 LVFQNP-----DD--QLFAP---TVEE-----D-----VAFGPENLGLPRE--------------EIRERVEEALELVGL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 166 GGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP---VLLASHDRAFL 236
Cdd:COG1122 125 EHL-ADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLV 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-232 |
2.15e-30 |
|
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: 118.40 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL---GDPLRVGLLYQEPPFA 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKpleKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PhdTVAQAVESAVRTVRDAASAVDRTADALARApedegaatayaaaldtaerigawdvdtRIDVTLDGLGLGGVdRDRST 174
Cdd:cd03235 81 R--DFPISVRDVVLMGLYGHKGLFRRLSKADKA---------------------------KVDEALERVGLSEL-ADRQI 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 175 GALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG---PVLLASHD 232
Cdd:cd03235 131 GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
17-232 |
2.84e-30 |
|
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: 116.73 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL---------RVGLL 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--LGKDIkkepeevkrRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPPFAPHDTVAQAVEsavrtvrdaasavdrtadalarapedegaatayaaaldtaerigawdvdtridvtldglglgg 167
Cdd:cd03230 79 PEEPSLYENLTVRENLK--------------------------------------------------------------- 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 168 vdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD-DAATDFLRA--TLRSWHGPVLLASHD 232
Cdd:cd03230 96 ---------LSGGMKQRLALAQALLHDPELLILDEPTSGLDpESRREFWELlrELKKEGKTILLSSHI 154
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-233 |
4.73e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.02 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD-------PLR---VGL 86
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV---LNGrdlftnlPPRerrVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADALARApedegaatayaaaldtaerigawdvdtridVTLDGLGlg 166
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLEL------------------------------VQLEGLA-- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 167 gvdrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDdaatDFLRATLRSW--------HGPVLLASHDR 233
Cdd:COG1118 128 ----DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD----AKVRKELRRWlrrlhdelGGTTVFVTHDQ 194
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
17-234 |
6.06e-29 |
|
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: 114.15 E-value: 6.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDPLR--VGLLYQE 90
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVPPERrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGVdR 170
Cdd:cd03259 81 YALFPHLTVAENIAFGLK---------------LRGVPKAE--------------------IRARVRELLELVGLEGL-L 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 171 DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG----PVLLASHDRA 234
Cdd:cd03259 125 NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQE 192
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-237 |
2.19e-28 |
|
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: 113.74 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS----HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL---------- 82
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF--DGRPVtrrrrkafrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 RVGLLYQEPP--FAPHDTVAQAVESAVRTvrdaasavdrtadalarapedegaatayaaaldtaerIGAWDVDTRIDVTL 160
Cdd:COG1124 80 RVQMVFQDPYasLHPRHTVDRILAEPLRI-------------------------------------HGLPDREERIAELL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 161 DGLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD----DAATDFLRAtLRSWHG-PVLLASHDRAF 235
Cdd:COG1124 123 EQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKD-LREERGlTYLFVSHDLAV 201
|
..
gi 1586061923 236 LD 237
Cdd:COG1124 202 VA 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
17-248 |
2.29e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.60 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDPL----RVGLLY 88
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgKPLSAMPPPewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 QEPPFaPHDTVAQAVEsAVRTVRDAASAVDRTADALARapedegaatayaaaldtaerigawdvdtridvtldgLGLGGV 168
Cdd:COG4619 81 QEPAL-WGGTVRDNLP-FPFQLRERKFDRERALELLER------------------------------------LGLPPD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 169 DRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHDRAFLDTAVTSLV 244
Cdd:COG4619 123 ILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTrrveELLREYLAEEGRAVLWVSHDPEQIERVADRVL 202
|
....
gi 1586061923 245 DLDP 248
Cdd:COG4619 203 TLEA 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-208 |
9.88e-28 |
|
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: 110.75 E-value: 9.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGdPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR-----AVGLGDPLR--VGLLYQ 89
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdVLKQPQKLRrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 90 EPPFAPHDTVAQAVesavrtvrdaasavdrtaDALARApedegaatayaaaldtaERIGAWDVDTRIDVTLDGLGLGGVd 169
Cdd:cd03264 80 EFGVYPNFTVREFL------------------DYIAWL-----------------KGIPSKEVKARVDEVLELVNLGDR- 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586061923 170 RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03264 124 AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-531 |
4.51e-27 |
|
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: 115.00 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDA---GEVR-----AVGLGDPLR--- 83
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLldgrdLLELSEALRgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 VGLLYQEPP--FAPHDTVAQAVESAVRTVRDAASAVDRTADALARapedegaatayaaaldtaerigawdvdtridVTLD 161
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEA-------------------------------VGLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 162 GLglggvdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHDRAfld 237
Cdd:COG1123 134 RR------LDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQaeilDLLRELQRERGTTVLLITHDLG--- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 238 tavtslVDLDPAPRphavtsdlvgdgtgtgIGVTRFGgtysqyvlarmdtRERWERTYRDEQAQLKKLRAAVREQQTVGH 317
Cdd:COG1123 205 ------VVAEIADR----------------VVVMDDG-------------RIVEDGPPEEILAAPQALAAVPRLGAARGR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 318 SGRSPKT-----EGRAAKKFYAdrnatvvSRRVNGARArlatVEDeqirkpprelyfqgltaglsgseaalhrtgpvlta 392
Cdd:COG1123 250 AAPAAAAaepllEVRNLSKRYP-------VRGKGGVRA----VDD----------------------------------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 393 saaevagrmapVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH--------------AAPGVRVGLLDQDat 458
Cdd:COG1123 284 -----------VSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltklsrrslRELRRRVQMVFQD-- 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 459 lPGA--DPEHT-------AAHIYHELVGEDRAETVP--LGTFGLLAgRDENRRVGELSVGQRRRLALAVLLADPPHVLLL 527
Cdd:COG1123 351 -PYSslNPRMTvgdiiaePLRLHGLLSRAERRERVAelLERVGLPP-DLADRYPHELSGGQRQRVAIARALALEPKLLIL 428
|
....
gi 1586061923 528 DEPT 531
Cdd:COG1123 429 DEPT 432
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
403-532 |
9.66e-27 |
|
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: 105.81 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDATLpgaDPEHTAA-H 470
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQDPQL---FPRLTVReN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 471 IYHELVG--------EDRAETVpLGTFGLLAGRDE--NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:pfam00005 80 LRLGLLLkglskrekDARAEEA-LEKLGLGDLADRpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-232 |
2.36e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.25 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASY----GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---LGDPLRVG 85
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADALarapedegaatayaaaldtaerigawdvdtridvtLDGLGL 165
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERAREL-----------------------------------LELVGL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 166 GGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAATdflRATLRSW-------HGP-VLLASHD 232
Cdd:COG1116 129 AGF-EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGAL-DALT---RERLQDEllrlwqeTGKtVLFVTHD 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
34-232 |
2.77e-26 |
|
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: 106.61 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFsVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPL---------------RVGLLYQEPPFAPHDT 98
Cdd:cd03297 16 KIDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV---LNGTVlfdsrkkinlppqqrKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 VAQAVESAVRTVRDAasaVDRTadalarapedegaatayaaaldtaerigawdvdtRIDVTLDGLGLGGVdRDRSTGALS 178
Cdd:cd03297 92 VRENLAFGLKRKRNR---EDRI----------------------------------SVDELLDLLGLDHL-LNRYPAQLS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD----FLRATLRSWHGPVLLASHD 232
Cdd:cd03297 134 GGEKQRVALARALAAQPELLLLDEPFSALDRALRLqllpELKQIKKNLNIPVIFVTHD 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-232 |
4.71e-26 |
|
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: 104.82 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPLRVgllyqeppfAPHD 97
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL--DGKDLAS---------LSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 98 TVAQAVesAVrtVRDAASAVDrtADALArapedegaatayaaaldtaerigawdvdtridvtldglglggvdrDRSTGAL 177
Cdd:cd03214 70 ELARKI--AY--VPQALELLG--LAHLA---------------------------------------------DRPFNEL 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 178 SGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD----DAATDFLRATLRSWHGPVLLASHD 232
Cdd:cd03214 99 SGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHD 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-240 |
9.15e-26 |
|
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: 105.25 E-value: 9.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS----HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL-----RVGLL 87
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV--DGEPVtgpgpDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADALarapedegaatayaaaldtaerigawdvdtridvtLDGLGLGG 167
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEEL-----------------------------------LELVGLSG 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 168 VdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAAT-----DFLRATLRSWHGPVLLASHDrafLDTAV 240
Cdd:cd03293 124 F-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSAL-DALTreqlqEELLDIWRETGKTVLLVTHD---IDEAV 196
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-245 |
9.46e-26 |
|
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: 105.98 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---LGDP------LRVGLL 87
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGediTGLPpheiarLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEP-PFaPHDTVAQAVESAVRTVRDAASAVDRTADALARAPEdegaatayaaaldtaerigawdvdtRIDVTLDGLGLG 166
Cdd:cd03219 81 FQIPrLF-PELTVLENVMVAAQARTGSGLLLARARREEREARE-------------------------RAEELLERVGLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 167 GVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP---VLLASHDRAFldtaVTSL 243
Cdd:cd03219 135 DL-ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgitVLLVEHDMDV----VMSL 209
|
..
gi 1586061923 244 VD 245
Cdd:cd03219 210 AD 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-205 |
1.27e-25 |
|
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: 102.73 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL----------RVGLLYQEPPFAPHDTVAQ 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL--DGQDLtdderkslrkEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 AVESAVRTVRDAASAVDRTADALArapedegaatayaaaldtaERIGAWDV-DTRIdvtldglglggvdrDRSTGALSGG 180
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEAL-------------------EKLGLGDLaDRPV--------------GERPGTLSGG 125
|
170 180
....*....|....*....|....*
gi 1586061923 181 QRSRLSLAWLLLSTPDVLLLDEPTN 205
Cdd:pfam00005 126 QRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-280 |
1.57e-25 |
|
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: 110.80 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPLRVGLLYQE-PPFAP 95
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE---IGETVKLAYVDQSrDALDP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 HDTVAQAVESAvrtvrdaasavdrtADALarapedegaatayaaaldtaeRIGAWDVDTRIDVTldGLGLGGVDRDRSTG 175
Cdd:TIGR03719 400 NKTVWEEISGG--------------LDII---------------------KLGKREIPSRAYVG--RFNFKGSDQQKKVG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 176 ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDdaaTDFLRA---TLRSWHGPVLLASHDRAFLDTAVTSLVDLDpaprp 252
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD---VETLRAleeALLNFAGCAVVISHDRWFLDRIATHILAFE----- 514
|
250 260
....*....|....*....|....*...
gi 1586061923 253 havtsdlvGDGTgtgigVTRFGGTYSQY 280
Cdd:TIGR03719 515 --------GDSH-----VEWFEGNFSEY 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-239 |
9.31e-25 |
|
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: 109.15 E-value: 9.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 1 MAHPP------HSPATPNTAAHIRVSGISASYGSHR--VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGE 72
Cdd:COG2274 452 LDLPPereegrSKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 73 V-------RAVGLGDpLR--VGLLYQEP-PFAphdtvaqavesavRTVRD--AASAVDRTADALARApedegaatayaaa 140
Cdd:COG2274 532 IlidgidlRQIDPAS-LRrqIGVVLQDVfLFS-------------GTIREniTLGDPDATDEEIIEA------------- 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 141 ldtAERIGAWDV--------DTRIdvtldglGLGGvdrdrstGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:COG2274 585 ---ARLAGLHDFiealpmgyDTVV-------GEGG-------SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
250 260
....*....|....*....|....*....
gi 1586061923 213 DFLRATLRSWHGP--VLLASHDRAFLDTA 239
Cdd:COG2274 648 AIILENLRRLLKGrtVIIIAHRLSTIRLA 676
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
17-212 |
1.09e-24 |
|
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: 102.64 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLR-----APDAGEVRAVGLG------DPL--- 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiydldvDVLelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 -RVGLLYQEP-PFapHDTVAQAVESAVR--TVRDAASAVDRTADALARApedegaatayaaaldtaeriGAWD-VDTRid 157
Cdd:cd03260 81 rRVGMVFQKPnPF--PGSIYDNVAYGLRlhGIKLKEELDERVEEALRKA--------------------ALWDeVKDR-- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 158 vtLDGLGlggvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:cd03260 137 --LHALG------------LSGGQQQRLCLARALANEPEVLLLDEPTSALDPIST 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-232 |
1.96e-24 |
|
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: 102.03 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV-----RAVGLGDPLR-VGLLYQE 90
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggeDATDVPVQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVESAVRtVRDAASavdrtadalaRAPEDEgaatayaaaldtaerigawdVDTRID-----VTLDGLGl 165
Cdd:cd03296 83 YALFRHMTVFDNVAFGLR-VKPRSE----------RPPEAE--------------------IRAKVHellklVQLDWLA- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 166 ggvdrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPV----LLASHD 232
Cdd:cd03296 131 -----DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHD 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-208 |
2.04e-24 |
|
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: 106.91 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 1 MAHPPHSPATPNTAAHIRVSGISASYGSH-----RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRA 75
Cdd:COG1123 245 AARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 76 vgLGDPL-------------RVGLLYQEpPFA---PHDTVAQAVESAVR--TVRDAASAVDRTADALARapedegaatay 137
Cdd:COG1123 325 --DGKDLtklsrrslrelrrRVQMVFQD-PYSslnPRMTVGDIIAEPLRlhGLLSRAERRERVAELLER----------- 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 138 aaaldtaerigawdvdtridvtldgLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG1123 391 -------------------------VGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-239 |
2.48e-24 |
|
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: 107.15 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 2 AHPPHSPATPNTAAHIRVSGISASYGSHR-VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGD 80
Cdd:COG4988 322 APAGTAPLPAAGPPSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL-IN-GV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 81 PLR----------VGLLYQEPPFaPHDTVAQavesavrTVRDAASAVDRTA--DALARApedegaatayaaaldtaeriG 148
Cdd:COG4988 400 DLSdldpaswrrqIAWVPQNPYL-FAGTIRE-------NLRLGRPDASDEEleAALEAA--------------------G 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 149 AWDV--------DTRIdvtldglGLGGVdrdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD-DAATDFLRATL 219
Cdd:COG4988 452 LDEFvaalpdglDTPL-------GEGGR-------GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDaETEAEILQALR 517
|
250 260
....*....|....*....|.
gi 1586061923 220 RSWHG-PVLLASHDRAFLDTA 239
Cdd:COG4988 518 RLAKGrTVILITHRLALLAQA 538
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-208 |
3.17e-24 |
|
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: 101.04 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY----GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR-----AVGLGDPLR---- 83
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 --VGLLYQEPPFA--PHDTVAQAVESAVRTVRDAasavDRTADALARAPEDegaatayaaaldtaerigawdvdtridvt 159
Cdd:cd03257 82 keIQMVFQDPMSSlnPRMTIGEQIAEPLRIHGKL----SKKEARKEAVLLL----------------------------- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 160 LDGLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03257 129 LVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-239 |
6.31e-24 |
|
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: 100.26 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS----HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR-----AVGLGD----PLR 83
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 ---VGLLYQEPPFAPHDTVAQAVESAVRTVRdaasavDRTADALARAPEdegaatayaaaldtaerigawdvdtridvTL 160
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAG------VPKKERRERAEE-----------------------------LL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 161 DGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG----PVLLASHDRAFL 236
Cdd:cd03255 126 ERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDPELA 204
|
...
gi 1586061923 237 DTA 239
Cdd:cd03255 205 EYA 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
17-238 |
7.11e-24 |
|
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: 98.80 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG-----LGDPL-----RVGL 86
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdLEDELpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPPFAPHDTVaqavesavrtvrdaasavdrtadalarapedegaatayaaaldtaerigawdvdtridvtLDGLGLG 166
Cdd:cd03229 81 VFQDFALFPHLTV------------------------------------------------------------LENIALG 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 167 gvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG----PVLLASHDRAFLDT 238
Cdd:cd03229 101 ----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDLDEAAR 166
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
402-559 |
1.21e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 99.09 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 402 APVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH----------AAPGVRVGLLDQDatlPGADPEHTA--- 468
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepirdarEDYRRRLAYLGHA---DGLKPELTVren 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 ----AHIYHELVGEDRAETVpLGTFGLlAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHF----SLVLAT 540
Cdd:COG4133 96 lrfwAALYGLRADREAIDEA-LEAVGL-AGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALdaagVALLAE 172
|
170
....*....|....*....
gi 1586061923 541 QLEAAVpDYPGTVLVASHD 559
Cdd:COG4133 173 LIAAHL-ARGGAVLLTTHQ 190
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-234 |
1.34e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDA---GEV----RAVGLGDPL--RVGLLY 88
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVllngRRLTALPAEqrRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 QEPPFAPHDTVAQAVesavrtvrdaasavdrtADALARAPedegaatayaaalDTAERigawdvDTRIDVTLDGLGLGGV 168
Cdd:COG4136 83 QDDLLFPHLSVGENL-----------------AFALPPTI-------------GRAQR------RARVEQALEEAGLAGF 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 169 -DRDRSTgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAatdfLRATLRSW--------HGPVLLASHDRA 234
Cdd:COG4136 127 aDRDPAT--LSGGQRARVALLRALLAEPRALLLDEPFSKLDAA----LRAQFREFvfeqirqrGIPALLVTHDEE 195
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-247 |
1.71e-23 |
|
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: 98.48 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYG-SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDPLR-VGLLYQEP 91
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngKPIKAKERRKsIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 92 PFaphdtvaQAVESAVRtvrdaaSAVDRTADALARAPEdegaatayaaaldtaerigawdvdtRIDVTLDGLGLGGVdRD 171
Cdd:cd03226 81 DY-------QLFTDSVR------EELLLGLKELDAGNE-------------------------QAETVLKDLDLYAL-KE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 172 RSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD----DAATDFLRaTLRSWHGPVLLASHDRAFLDTAVTSLVDLD 247
Cdd:cd03226 122 RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknmERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-220 |
2.04e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 101.71 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGDPL--------RV 84
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIL-LD-GRDVtglppekrNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEppFA--PHDTVAQAVESAVRTVRDAASAVD-RTADALARapedegaatayaaaldtaerigawdvdtridVTLD 161
Cdd:COG3842 80 GMVFQD--YAlfPHLTVAENVAFGLRMRGVPKAEIRaRVAELLEL-------------------------------VGLE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 162 GLGlggvdrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDdaatDFLRATLR 220
Cdd:COG3842 127 GLA------DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD----AKLREEMR 175
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-239 |
4.33e-23 |
|
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: 103.31 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 5 PHSPATPNTAAHIRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD-P 81
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT---LGGvD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 82 LR----------VGLLYQEPP-FapHDTVAQAVesavRTVRDAASAvDRTADALARApedegaatayaaaldtaeRIGAW 150
Cdd:COG4987 399 LRdldeddlrrrIAVVPQRPHlF--DTTLRENL----RLARPDATD-EELWAALERV------------------GLGDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 151 dvdtrIDVTLDGL----GLGGVdrdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP- 225
Cdd:COG4987 454 -----LAALPDGLdtwlGEGGR-------RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGr 521
|
250
....*....|....*
gi 1586061923 226 -VLLASHDRAFLDTA 239
Cdd:COG4987 522 tVLLITHRLAGLERM 536
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-247 |
6.28e-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: 95.39 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvglgdplrvgllyqeppfaphd 97
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 98 tvaqavesavrtvrdaasavdrtadalarapedEGAATAYAAALDTAERIGAwdvdtridvtldglglggvdrdrsTGAL 177
Cdd:cd00267 59 ---------------------------------DGKDIAKLPLEELRRRIGY------------------------VPQL 81
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 178 SGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP---VLLASHDRAFLDTAVTSLVDLD 247
Cdd:cd00267 82 SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgrtVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-208 |
1.05e-22 |
|
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: 96.44 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG--LGDPL--------RVGL 86
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPPFAPHDTVAQAVESAVRTVR--DAASAVDRTADALARapedegaatayaaaldtaerigawdvdtridVTLDglg 164
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKgmSKAEAEERALELLEK-------------------------------VGLA--- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586061923 165 lggvDR-DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03262 127 ----DKaDAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-234 |
1.32e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 25 SYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgdpLRVGLLYQEPpfAPHDTVAQAVE 104
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---ARVAYVPQRS--EVPDSLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 105 SAVRTVRDAASAVDRTADALARApedegaatayaaaldtaerigawdvdtRIDVTLDGLGLGGVDRdRSTGALSGGQRSR 184
Cdd:NF040873 76 DLVAMGRWARRGLWRRLTRDDRA---------------------------AVDDALERVGLADLAG-RQLGELSGGQRQR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 185 LSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG---PVLLASHDRA 234
Cdd:NF040873 128 ALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLE 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
15-221 |
2.58e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.61 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD-------PLR--VG 85
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL---IGGrdvtdlpPKDrnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGL 165
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLK---------------LRKVPKAE--------------------IDRRVREAAELLGL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 166 GGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAAtdfLRATLRS 221
Cdd:COG3839 124 EDL-LDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNL-DAK---LRVEMRA 174
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-237 |
3.07e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 100.58 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGsHRVL-TDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDplrvgllyqeppfap 95
Cdd:PRK11819 325 IEAENLSKSFG-DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK---IGE--------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 hdtvaqavesavrTVRdaASAVDRTADALAraPED-------EGAATAyaaaldtaeRIGAWDVDTRIDVTldGLGLGGV 168
Cdd:PRK11819 386 -------------TVK--LAYVDQSRDALD--PNKtvweeisGGLDII---------KVGNREIPSRAYVG--RFNFKGG 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 169 DRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDdaaTDFLRA---TLRSWHGPVLLASHDRAFLD 237
Cdd:PRK11819 438 DQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD---VETLRAleeALLEFPGCAVVISHDRWFLD 506
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
403-574 |
3.74e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 94.88 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH---------AAPGVR--VGLLDQDATLPGADPEH---TA 468
Cdd:COG4619 18 PVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPEWRrqVAYVPQEPALWGGTVRDnlpFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 AHIYHELVGEDRAETVpLGTFGLlAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNhfSL--VLATQLEAAV 546
Cdd:COG4619 98 FQLRERKFDRERALEL-LERLGL-PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS--ALdpENTRRVEELL 173
|
170 180 190
....*....|....*....|....*....|..
gi 1586061923 547 PDYP----GTVLVASHDRWLRRNWTGRDLALE 574
Cdd:COG4619 174 REYLaeegRAVLWVSHDPEQIERVADRVLTLE 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
17-241 |
4.90e-22 |
|
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: 95.26 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG-----------LGDPLRVG 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAVESAVRTVRdaasavdrtadalaRAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGL 165
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHT--------------RLSEEE--------------------IREIVLEKLEAVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 166 GGvDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP----VLLASHDrafLDTAVT 241
Cdd:cd03261 127 RG-AEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVTHD---LDTAFA 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
403-559 |
1.15e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 91.92 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvglldqdaTLPGADPEHTAAHIYHELVGedrae 482
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI---------------LIDGKDIAKLPLEELRRRIG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 483 tvplgtfgllagrdenrRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPG---TVLVASHD 559
Cdd:cd00267 77 -----------------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHD 139
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-245 |
1.39e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 93.42 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHR--VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG----DP--LRVGLLY 88
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqlDPadLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 qeppfaphdtVAQAVESAVRTVRD--AASAVDRTADALARAPEDEGaatayaaaldtaerigawdVDTRIDVTLDGLGLG 166
Cdd:cd03245 83 ----------VPQDVTLFYGTLRDniTLGAPLADDERILRAAELAG-------------------VTDFVNKHPNGLDLQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 167 GVDRDRStgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP--VLLASHDRAFLDtavtsLV 244
Cdd:cd03245 134 IGERGRG---LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLD-----LV 205
|
.
gi 1586061923 245 D 245
Cdd:cd03245 206 D 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
17-208 |
1.94e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------GDPL--RVGLLY 88
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 QEPPFAPHDTVAQAVesavrtvrdaasavdrtadALARAPEDEGaatayaaaldtaeRIGAWDVDtRIDVTLDGLGLGGV 168
Cdd:COG4604 82 QENHINSRLTVRELV-------------------AFGRFPYSKG-------------RLTAEDRE-IIDEAIAYLDLEDL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586061923 169 dRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG4604 129 -ADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-234 |
3.63e-21 |
|
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: 96.97 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 4 PPHSPATPNTAAH---IRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG-- 77
Cdd:TIGR02857 306 RPLAGKAPVTAAPassLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvp 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 78 ----LGDPLRVGLLY-QEPPFAPHDTVAQAVESAVRtvrdaasavDRTADALARApedegaatayaaaldtAERIGAWDV 152
Cdd:TIGR02857 386 ladaDADSWRDQIAWvPQHPFLFAGTIAENIRLARP---------DASDAEIREA----------------LERAGLDEF 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 153 DTRIdvtldGLGLGGVDRDRSTGaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG--PVLLAS 230
Cdd:TIGR02857 441 VAAL-----PQGLDTPIGEGGAG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVT 514
|
....
gi 1586061923 231 HDRA 234
Cdd:TIGR02857 515 HRLA 518
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-208 |
4.38e-21 |
|
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: 92.30 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV-----RAVGLGDPLR-VGLLYQE 90
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkDITNLPPHKRpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGVdR 170
Cdd:cd03300 81 YALFPHLTVFENIAFGLR---------------LKKLPKAE--------------------IKERVAEALDLVQLEGY-A 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586061923 171 DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03300 125 NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
17-208 |
4.48e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 92.81 E-value: 4.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------GDPLR-----V 84
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalrGRALRrlrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPPFAPHDTVAQAV-------ESAVRTVRDAASAVDRTA--DALARapedegaatayaaaldtaerigawdvdtr 155
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVlagrlgrTSTWRSLLGLFPPEDRERalEALER----------------------------- 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 156 idvtldgLGLGGVDRDRsTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG3638 134 -------VGLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-280 |
6.39e-21 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 96.50 E-value: 6.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 19 VSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPLRVGLLYQeppfaphdt 98
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK---WSENANIGYYAQ--------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 vaqavesavrtvrdaasavDRTADAlaraPEDEgaatayaaalDTAERIGAW----DVDTRIDVTLDGLGLGGVDRDRST 174
Cdd:PRK15064 390 -------------------DHAYDF----ENDL----------TLFDWMSQWrqegDDEQAVRGTLGRLLFSQDDIKKSV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 175 GALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDPAprpha 254
Cdd:PRK15064 437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPD----- 511
|
250 260
....*....|....*....|....*.
gi 1586061923 255 vtsdlvgdgtgtgiGVTRFGGTYSQY 280
Cdd:PRK15064 512 --------------GVVDFSGTYEEY 523
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
404-559 |
6.63e-21 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 91.37 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGV------------RVGLLDQdatlpgaDPEH--TAA 469
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKdltklslkelrrKVGLVFQ-------NPDDqfFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 HIYHELV------GEDRAETVP-----LGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVL 538
Cdd:cd03225 92 TVEEEVAfglenlGLPEEEIEErveeaLELVGLEGLRD--RSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180
....*....|....*....|....
gi 1586061923 539 ATQLEAAV---PDYPGTVLVASHD 559
Cdd:cd03225 170 RRELLELLkklKAEGKTIIIVTHD 193
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
17-232 |
1.17e-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: 91.80 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlGD---------PLRVGLL 87
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAG-VDlhglsrrarARRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPPFAPHDTVAQAVesavrtvrdaasavdrtadALARAPEdegaatayaaaldtaerIGAWDVDTRIDVTLDGLGLGG 167
Cdd:TIGR03873 81 EQDSDTAVPLTVRDVV-------------------ALGRIPH-----------------RSLWAGDSPHDAAVVDRALAR 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 168 VD----RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP---VLLASHD 232
Cdd:TIGR03873 125 TElshlADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAATgvtVVAALHD 196
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-245 |
1.34e-20 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 96.09 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG----DP--LR--VG 85
Cdd:TIGR03375 463 EIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDirqiDPadLRrnIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPP-FapHDTVAQAVESAVRTVRDAAsavdrtadaLARAPEDEGaatayaaaldtaerigawdVDTRIDVTLDGLG 164
Cdd:TIGR03375 543 YVPQDPRlF--YGTLRDNIALGAPYADDEE---------ILRAAELAG-------------------VTEFVRRHPDGLD 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 165 LGGVDRDRStgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP--VLLASHDRAFLDtavts 242
Cdd:TIGR03375 593 MQIGERGRS---LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTHRTSLLD----- 664
|
...
gi 1586061923 243 LVD 245
Cdd:TIGR03375 665 LVD 667
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
13-245 |
1.43e-20 |
|
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: 91.25 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR-----AVGLGDPLRV--G 85
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrdITGLPPHRIArlG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LL--YQEP-PFaPHDTVAQAVESAVRTVRDAASAVDRTADALARAPEDEgaatayaaaldTAERIGAWdvdtridvtLDG 162
Cdd:COG0411 81 IArtFQNPrLF-PELTVLENVLVAAHARLGRGLLAALLRLPRARREERE-----------ARERAEEL---------LER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 163 LGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPT---NHLD-DAATDFLRAtLRSWHG-PVLLASHDRAFld 237
Cdd:COG0411 140 VGLADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEEtEELAELIRR-LRDERGiTILLIEHDMDL-- 215
|
....*...
gi 1586061923 238 taVTSLVD 245
Cdd:COG0411 216 --VMGLAD 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-232 |
1.61e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDPLRVGLLYQEpp 92
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgEPLDPEDRRRIGYLPEE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 93 faphdtvaqavesavR------TVRDAASavdrtadALAR---APEDEGaatayaaaldtAERIGAWdvdtridvtLDGL 163
Cdd:COG4152 80 ---------------RglypkmKVGEQLV-------YLARlkgLSKAEA-----------KRRADEW---------LERL 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 164 GLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH--G-PVLLASHD 232
Cdd:COG4152 118 GLGDR-ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGtTVIFSSHQ 188
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
17-239 |
2.77e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 89.72 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS----HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR-----AVGLGDP----LR 83
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdISSLSERelarLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 ---VGLLYQEPPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldTAERIGAWdvdtridvtL 160
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLL---------------LAGVSRKE-----------RRERAREL---------L 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 161 DGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHDRAFL 236
Cdd:COG1136 130 ERVGLGDR-LDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNRELGTTIVMVTHDPELA 208
|
...
gi 1586061923 237 DTA 239
Cdd:COG1136 209 ARA 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-220 |
6.64e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR----AVGLGDP-----LR 83
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgePVRFRSPrdaqaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 VGLLYQEPPFAPHDTVAQAV----ESAVRTVRDAASAVDRTADALARapedegaatayaaaldtaerigawdVDTRIDVt 159
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIflgrEPRRGGLIDWRAMRRRARELLAR-------------------------LGLDIDP- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 160 ldglglggvdrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:COG1129 135 -----------DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIR 184
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-221 |
7.60e-20 |
|
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: 88.08 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDPLR--VGLLYQE 90
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLPPKDrdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGVdR 170
Cdd:cd03301 81 YALYPHMTVYDNIAFGLK---------------LRKVPKDE--------------------IDERVREVAELLQIEHL-L 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 171 DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAatdfLRATLRS 221
Cdd:cd03301 125 DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK----LRVQMRA 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-234 |
7.92e-20 |
|
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: 87.05 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS--HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGDPLR----------V 84
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL-ID-GVDLRdldleslrknI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEpPFAPHDTVAqavesavrtvrdaasavdrtadalarapedegaatayaaaldtaERIgawdvdtridvtldglg 164
Cdd:cd03228 79 AYVPQD-PFLFSGTIR--------------------------------------------ENI----------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 165 lggvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP--VLLASHDRA 234
Cdd:cd03228 97 ------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLS 156
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
13-208 |
8.60e-20 |
|
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: 88.88 E-value: 8.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR-----AVGLGD------P 81
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqdITGLSEkelyelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 82 LRVGLLYQEPpfAPHD--TVAQAVESAVRtvrdaasavdrtadALARAPEDEgaatayaaaldtaerigawdVDTRIDVT 159
Cdd:COG1127 82 RRIGMLFQGG--ALFDslTVFENVAFPLR--------------EHTDLSEAE--------------------IRELVLEK 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 160 LDGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG1127 126 LELVGLPGA-ADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLD 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-212 |
8.65e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG------------LGDPLR- 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpsekAIRLLRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 -VGLLYQEPPFAPHDTVAQ-AVESAVRTVRDA-ASAVDRTADALARapedegaatayaaaldtaerigawdvdtridvtl 160
Cdd:COG4161 83 kVGMVFQQYNLWPHLTVMEnLIEAPCKVLGLSkEQAREKAMKLLAR---------------------------------- 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 161 dgLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:COG4161 129 --LRLTDK-ADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
403-559 |
9.65e-20 |
|
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: 88.76 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR--VGLLDQDATLPgadPEHTA---A 469
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrKEPREARrqIGVLPDERGLY---DRLTVrenI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 HIY---HELVGEDRAETVP--LGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLE- 543
Cdd:COG4555 96 RYFaelYGLFDEELKKRIEelIELLGLEEFLD--RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLRe 173
|
170
....*....|....*...
gi 1586061923 544 --AAVPDYPGTVLVASHD 559
Cdd:COG4555 174 ilRALKKEGKTVLFSSHI 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
416-580 |
9.79e-20 |
|
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: 92.69 E-value: 9.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 416 ITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQDatlPGADPEHTAAHIYHELVGE-----DRAETV------ 484
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQE---PQLDPTKTVRENVEEGVAEikdalDRFNEIsakyae 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 485 PLGTFGLLA--------------GRDENRR----------------VGELSVGQRRRLALAVLLADPPHVLLLDEPTNHF 534
Cdd:TIGR03719 113 PDADFDKLAaeqaelqeiidaadAWDLDSQleiamdalrcppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 535 SLVLATQLEAAVPDYPGTVLVASHDRWLRRNWTGRDLALEVPAGTP 580
Cdd:TIGR03719 193 DAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIP 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-231 |
1.10e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.60 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVgLGDPL----------RVGL 86
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRL-FGERRggedvwelrkRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQE--PPFAPHDTVAQAVESAvrtvrdAASAVDrtadaLARAPEDEgaatayaaaldTAERIGAWdvdtridvtLDGLG 164
Cdd:COG1119 83 VSPAlqLRFPRDETVLDVVLSG------FFDSIG-----LYREPTDE-----------QRERAREL---------LELLG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 165 LGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP----VLLASH 231
Cdd:COG1119 132 LAHL-ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-232 |
1.69e-19 |
|
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: 87.43 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlgdplrvgllyqeppfapH 96
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG------------------H 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVAQAvesavRTVRDAASAV--DRTADalarapeDEGAATAYAAALDTAERIGAWDVDTRIDVTLDGLGLGGVdRDRST 174
Cdd:cd03265 63 DVVREP-----REVRRRIGIVfqDLSVD-------DELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 175 GALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHD 232
Cdd:cd03265 130 KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHY 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
17-212 |
1.98e-19 |
|
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: 87.62 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS-HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------GDPLR-----V 84
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkGKALRqlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPPFAPHDTVAQAVESA----VRTVRDAASAVDRTADALARApedegaatayaaaldtaerigawdvdtridvTL 160
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrRSTWRSLFGLFPKEEKQRALA-------------------------------AL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 161 DGLGLGGVDRDRsTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:cd03256 130 ERVGLLDKAYQR-ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASS 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-208 |
2.24e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------------GDPLR- 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkaIRELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 -VGLLYQEPPFAPHDTVAQ-AVESAVRTvrdaaSAVDRTAdALARAPEdegaatayaaaldtaerigawdvdtridvTLD 161
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQnLIEAPCRV-----LGLSKDQ-ALARAEK-----------------------------LLE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586061923 162 GLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11124 128 RLRLKPY-ADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-213 |
2.88e-19 |
|
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: 86.87 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHR----VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------GDPLR--- 83
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsGKELRkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 --VGLLYQEPPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLD 161
Cdd:cd03258 82 rrIGMIFQHFNLLSSRTVFENVALPLE---------------IAGVPKAE--------------------IEERVLELLE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 162 GLGLGGvDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD 213
Cdd:cd03258 127 LVGLED-KADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQ 177
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-231 |
2.94e-19 |
|
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: 86.57 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL------RVGLLYQE 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF--DGKPLdiaarnRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVA-QAVESA-VRTV--RDAASAVDRtadalarapedegaatayaaaldtaerigaWdvdtridvtLDGLGLG 166
Cdd:cd03269 79 RGLYPKMKVIdQLVYLAqLKGLkkEEARRRIDE------------------------------W---------LERLELS 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 167 GVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRA---TLRSWHGPVLLASH 231
Cdd:cd03269 120 EY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDvirELARAGKTVILSTH 186
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-232 |
3.57e-19 |
|
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: 86.40 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS--HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLRVGLLYQEPPFA 94
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PHD-------TVAQAVE--SAVRTVRDaasavdrtadalarapedegaatayaaaldtaerigaWDVDTRIDVTLDGLGL 165
Cdd:cd03263 81 PQFdalfdelTVREHLRfyARLKGLPK-------------------------------------SEIKEEVELLLRVLGL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 166 GGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFL-RATLRSWHG-PVLLASHD 232
Cdd:cd03263 124 TDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIwDLILEVRKGrSIILTTHS 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-208 |
4.25e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.99 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 1 MAHPPHSPATPNTAAHIRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV------ 73
Cdd:COG1132 324 IPDPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 74 -RAVGLGDpLR--VGLLYQEPP-FAphdtvaqavesavRTVRD--AASAVDRTADALARApedegaatayaaaldtAERI 147
Cdd:COG1132 404 iRDLTLES-LRrqIGVVPQDTFlFS-------------GTIREniRYGRPDATDEEVEEA----------------AKAA 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 148 GAWDV--------DTRIdvtldglGLGGVDrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG1132 454 QAHEFiealpdgyDTVV-------GERGVN-------LSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-220 |
5.07e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 84.40 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlgdplrvgllyQEPPFAph 96
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------KEVSFA-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 dTVAQAVESAVRTVRDaasavdrtadalarapedegaatayaaaldtaerigawdvdtridvtldglglggvdrdrstga 176
Cdd:cd03216 68 -SPRDARRAGIAMVYQ---------------------------------------------------------------- 82
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-232 |
6.40e-19 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 87.12 E-value: 6.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYG-----SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL---------GDPL 82
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditakkkkkLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 R--VGLLYQEPP---FAphDTVAQAV-----------ESAVRTVRDAASAVdrtadalarapedegaatayaaaldtaer 146
Cdd:TIGR04521 81 RkkVGLVFQFPEhqlFE--ETVYKDIafgpknlglseEEAEERVKEALELV----------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 147 igawdvdtridvtldglglgGVDR---DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH 223
Cdd:TIGR04521 130 --------------------GLDEeylERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLH 189
|
250
....*....|...
gi 1586061923 224 G----PVLLASHD 232
Cdd:TIGR04521 190 KekglTVILVTHS 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
369-565 |
8.43e-19 |
|
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: 89.65 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 369 FQGLTAGLSGSEAALHRTGPVLTASAAEV---------AGRM---APVSLTVSAGESWLITGSNGVGKSTLLSLFARRLE 436
Cdd:TIGR02857 294 AEALFAVLDAAPRPLAGKAPVTAAPASSLefsgvsvayPGRRpalRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 437 PTRGSV-----------HAAPGVRVGLLDQDATLPG---------ADPEHTAAHIyhelvgEDRAETVPLGTFGLLAGRD 496
Cdd:TIGR02857 374 PTEGSIavngvpladadADSWRDQIAWVPQHPFLFAgtiaenirlARPDASDAEI------REALERAGLDEFVAALPQG 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 497 ENRRVGE----LSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPG--TVLVASHDRWLRRN 565
Cdd:TIGR02857 448 LDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAAL 522
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
17-223 |
8.58e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.22 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------GDPLRVGLLYQE 90
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAqavesavrtvrdaasavDRTADALARAPEdegaatayaaaldtAERIGAWDVDTRIDVTLDGLGLGGVdR 170
Cdd:PRK10851 83 YALFRHMTVF-----------------DNIAFGLTVLPR--------------RERPNAAAIKAKVTQLLEMVQLAHL-A 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 171 DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH 223
Cdd:PRK10851 131 DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLH 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-203 |
1.37e-18 |
|
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: 84.90 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD------PL----RVGL 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL---LDGqditklPMhkraRLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LY--QEPpfaphdtvaqaveSAVR--TVRDAASAVdrtadaLARAPEDEgaatayaaaldtAERIgawdvdTRIDVTLDG 162
Cdd:cd03218 78 GYlpQEA-------------SIFRklTVEENILAV------LEIRGLSK------------KERE------EKLEELLEE 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1586061923 163 LGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEP 203
Cdd:cd03218 121 FHITHL-RKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
404-559 |
2.72e-18 |
|
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: 83.92 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGV------------RVGLLDQDatlpgadPEHtaaHI 471
Cdd:COG1122 20 VSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKditkknlrelrrKVGLVFQN-------PDD---QL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 472 YHELVGED-----------------RAETVpLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNhf 534
Cdd:COG1122 89 FAPTVEEDvafgpenlglpreeireRVEEA-LELVGLEHLAD--RPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA-- 163
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 535 SLVLATQLE-----AAVPDYPGTVLVASHD 559
Cdd:COG1122 164 GLDPRGRREllellKRLNKEGKTVIIVTHD 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-242 |
3.15e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 88.47 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 22 ISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvglGDPLRVGLLYQEppfaphdtvaq 101
Cdd:PRK11147 325 VNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC---GTKLEVAYFDQH----------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 avesavRTVRDAasavDRTA-DALArapedegaatayaaaldtaerigawdvDTRIDVTLDG-----LG-----LGGVDR 170
Cdd:PRK11147 391 ------RAELDP----EKTVmDNLA---------------------------EGKQEVMVNGrprhvLGylqdfLFHPKR 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 171 DRS-TGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTS 242
Cdd:PRK11147 434 AMTpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTE 506
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-236 |
3.50e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 88.30 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVravGLGDPLRVGLlyqeppFAPH 96
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGIKLGY------FAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 D-TVAQAVESAVRtvrdaasavdrtadALARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGVDRDRSTG 175
Cdd:PRK10636 384 QlEFLRADESPLQ--------------HLARLAPQE--------------------LEQKLRDYLGGFGFQGDKVTEETR 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 176 ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFL 236
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLL 490
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-208 |
5.37e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 84.02 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgDPL----------RV 84
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL-DTLdeenlweirkKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPpfaphDTvaQAVESavrTVRDaasavDrtadaLARAPEDEGAATAyaaaldtaerigawDVDTRIDVTLDGLG 164
Cdd:TIGR04520 80 GMVFQNP-----DN--QFVGA---TVED-----D-----VAFGLENLGVPRE--------------EMRKRVDEALKLVG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586061923 165 LGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:TIGR04520 126 MEDF-RDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-231 |
6.82e-18 |
|
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: 82.16 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 19 VSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLRVGLLYQEPPFAPHDT 98
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 VAQAVESAVRTVR--DAASAVDRTADALARApedegaatayaaaldtaerigawdvdtridvtldglGLGGVDrDRSTGA 176
Cdd:cd03231 83 GIKTTLSVLENLRfwHADHSDEQVEEALARV------------------------------------GLNGFE-DRPVAQ 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSwH----GPVLLASH 231
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-HcargGMVVLTTH 183
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-237 |
8.57e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.41 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG--LGD------PL---RV 84
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdLSRlkrreiPYlrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLG 164
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLR---------------VTGKSRKE--------------------IRRRVREVLDLVG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 165 LGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD-DAATDFLR---------ATlrswhgpVLLASHDRA 234
Cdd:COG2884 127 LSDK-AKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDpETSWEIMElleeinrrgTT-------VLIATHDLE 198
|
...
gi 1586061923 235 FLD 237
Cdd:COG2884 199 LVD 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
390-559 |
1.13e-17 |
|
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: 86.35 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 390 LTASAAEVAGRMAPVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDAT 458
Cdd:COG4988 342 VSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldPASWRRQIAWVPQNPY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 459 LPG---------ADPEHTAAHIyhelvgEDRAETVPLGTF--GLLAGRDEnrRVGE----LSVGQRRRLALAVLLADPPH 523
Cdd:COG4988 422 LFAgtirenlrlGRPDASDEEL------EAALEAAGLDEFvaALPDGLDT--PLGEggrgLSGGQAQRLALARALLRDAP 493
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1586061923 524 VLLLDEPTNHF-----SLVLATqLEAAVPDYpgTVLVASHD 559
Cdd:COG4988 494 LLLLDEPTAHLdaeteAEILQA-LRRLAKGR--TVILITHR 531
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-231 |
1.51e-17 |
|
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: 81.25 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 19 VSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLRVGLLYQEPPFAPHdt 98
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 vaqavESAVRTVRDAASAVDRTADALArapedegaatayaaaldtAERIGAWDvdtridvTLDGLGLGGVDrDRSTGALS 178
Cdd:TIGR01189 81 -----LPGLKPELSALENLHFWAAIHG------------------GAQRTIED-------ALAAVGLTGFE-DLPAAQLS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSwH----GPVLLASH 231
Cdd:TIGR01189 130 AGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA-HlargGIVLLTTH 185
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-203 |
1.89e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD------PL----RV 84
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF---LDGedithlPMhkraRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLY--QEPpfaphdtvaqaveSAVR--TVRDAASAVDRTADaLARApedegaatayaaaldtaERigawdvDTRIDVTL 160
Cdd:COG1137 79 GIGYlpQEA-------------SIFRklTVEDNILAVLELRK-LSKK-----------------ER------EERLEELL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586061923 161 DGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEP 203
Cdd:COG1137 122 EEFGITHL-RKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
1.91e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 2 AHPPHSPATPNTAahIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDP 81
Cdd:PRK13536 29 AKASIPGSMSTVA--IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 82 -------LRVGLLYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADALARAPEDEGaatayaaaldtaerigawDVDT 154
Cdd:PRK13536 107 ararlarARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLES------------------KADA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 155 RIdvtldglglggvdrdrstGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRS 221
Cdd:PRK13536 169 RV------------------SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRS 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-238 |
1.91e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 11 PNTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDP-------LR 83
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPsrarharQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 VGLLYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADALARAPEDEGAAtayaaaldtaerigawdvdtridvtldgl 163
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKA----------------------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 164 glggvdrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSwhgpvLLASHDRAFLDT 238
Cdd:PRK13537 133 -------DAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRS-----LLARGKTILLTT 195
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
404-559 |
1.93e-17 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 86.04 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGV---RVGLLDQDATL-PG--------AD 463
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGVVLQDVFLfSGtirenitlGD 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 464 PEHTAAHIYH--ELVG-EDRAETVPLGtfgllagrdENRRVGE----LSVGQRRRLALA-VLLADPPhVLLLDEPTNHfs 535
Cdd:COG2274 574 PDATDEEIIEaaRLAGlHDFIEALPMG---------YDTVVGEggsnLSGGQRQRLAIArALLRNPR-ILILDEATSA-- 641
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 536 lvLATQLEAAV------PDYPGTVLVASHD 559
Cdd:COG2274 642 --LDAETEAIIlenlrrLLKGRTVIIIAHR 669
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
404-559 |
2.00e-17 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 80.17 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgvrvgLLDQD-ATLPGADpehtaahiyhelvgedRAE 482
Cdd:cd03214 18 LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL--------LDGKDlASLSPKE----------------LAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 483 T---VP--LGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHfsLVLATQLE------AAVPDYPG 551
Cdd:cd03214 74 KiayVPqaLELLGLAHLAD--RPFNELSGGERQRVLLARALAQEPPILLLDEPTSH--LDIAHQIEllellrRLARERGK 149
|
....*...
gi 1586061923 552 TVLVASHD 559
Cdd:cd03214 150 TVVMVLHD 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
404-532 |
2.07e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 81.65 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGEswlIT---GSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR--VGLLDQDATLpgaDPEHTA-- 468
Cdd:COG1131 19 VSLTVEPGE---IFgllGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvaRDPAEVRrrIGYVPQEPAL---YPDLTVre 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 469 -----AHIYH--ELVGEDRAETVpLGTFGLLAGRDenRRVGELSVGQRRRLALAV-LLADPPhVLLLDEPTN 532
Cdd:COG1131 93 nlrffARLYGlpRKEARERIDEL-LELFGLTDAAD--RKVGTLSGGMKQRLGLALaLLHDPE-LLILDEPTS 160
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-212 |
2.34e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.01 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 7 SPATPNTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLR-------IVAGLRApdAGEVRavgLG 79
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEIL---LD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 80 ---------DPL----RVGLLYQEP-PFaPH---DTVAQAVEsaVRTVRDAASAVDRTADALARApedegaatayaaald 142
Cdd:COG1117 77 gediydpdvDVVelrrRVGMVFQKPnPF-PKsiyDNVAYGLR--LHGIKSKSELDEIVEESLRKA--------------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 143 taeriGAWD-VDTRidvtLDGLGLGgvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:COG1117 139 -----ALWDeVKDR----LKKSALG----------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIST 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
404-559 |
3.56e-17 |
|
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: 81.24 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-------HAAPGV----RVGLLDQDATLPGAdpeHTAAhiy 472
Cdd:COG1120 20 VSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlASLSRRelarRIAYVPQEPPAPFG---LTVR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 473 hELVGEDRAetvP-LGTFGLLAGRDE----------------NRRVGELSVGQRRRLALAVLLA-DPPhVLLLDEPTNHf 534
Cdd:COG1120 94 -ELVALGRY---PhLGLFGRPSAEDReaveealertglehlaDRPVDELSGGERQRVLIARALAqEPP-LLLLDEPTSH- 167
|
170 180 190
....*....|....*....|....*....|.
gi 1586061923 535 sLVLATQLE------AAVPDYPGTVLVASHD 559
Cdd:COG1120 168 -LDLAHQLEvlellrRLARERGRTVVMVLHD 197
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
343-559 |
4.41e-17 |
|
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: 84.43 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 343 RRVN---GARARLATVEDEQIRKPPRELYFQGLTAGLSGSEAalhrtgPVLTasaaevagrmaPVSLTVSAGESWLITGS 419
Cdd:COG4987 307 RRLNellDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR------PVLD-----------GLSLTLPPGERVAIVGP 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 420 NGVGKSTLLSLFARRLEPTRGSVHAApGV------------RVGLLDQDATL-------------PGADPEhtaahiyhE 474
Cdd:COG4987 370 SGSGKSTLLALLLRFLDPQSGSITLG-GVdlrdldeddlrrRIAVVPQRPHLfdttlrenlrlarPDATDE--------E 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 475 LVgeDRAETVPLGTFglLAGRDE--NRRVGE----LSVGQRRRLALA-VLLADPPhVLLLDEPTNHFSLVLATQLEAAVP 547
Cdd:COG4987 441 LW--AALERVGLGDW--LAALPDglDTWLGEggrrLSGGERRRLALArALLRDAP-ILLLDEPTEGLDAATEQALLADLL 515
|
250
....*....|....
gi 1586061923 548 DYPG--TVLVASHD 559
Cdd:COG4987 516 EALAgrTVLLITHR 529
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
10-208 |
5.27e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 81.00 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 10 TPNTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGDPL------- 82
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIR-VG-GEEIrlkpdrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 ----------------RVGLLYQEPPFAPHDTVAQAVESAVRTV--RDAASAVDRtADALarapedegaatayaaaldtA 144
Cdd:COG4598 80 gelvpadrrqlqrirtRLGMVFQSFNLWSHMTVLENVIEAPVHVlgRPKAEAIER-AEAL-------------------L 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 145 ERIGAWDVdtridvtldglglggvdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG4598 140 AKVGLADK-----------------RDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-231 |
5.76e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrvgllyqeppFAP 95
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK------------------LDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 HDTVAQAVESAVRTV--RDAASavdrtaDALARApedegaatayaaaldtaERIGAW-----DVDTRIDVTLDGLGLGGV 168
Cdd:PRK13539 64 GDIDDPDVAEACHYLghRNAMK------PALTVA-----------------ENLEFWaaflgGEELDIAAALEAVGLAPL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 169 DrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAATDFLRATLRSWH----GPVLLASH 231
Cdd:PRK13539 121 A-HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL-DAAAVALFAELIRAHlaqgGIVIAATH 185
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-232 |
7.02e-17 |
|
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: 80.07 E-value: 7.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHrVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG------DPLRVGLLYQE 90
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDitnlppEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVESAVRTVRDAASAVDRTADALARapedegaatayaaaldtaerigawdvDTRIDVTLDglglggvdr 170
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAE--------------------------MLGIDHLLN--------- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 171 dRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG----PVLLASHD 232
Cdd:cd03299 125 -RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefgvTVLHVTHD 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
17-210 |
1.20e-16 |
|
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: 79.07 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVltDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRA----VGLGDPLR--VGLLYQE 90
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdVTAAPPADrpVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVesavrtvrdaasavdrtadALARAPedegaatayaaaldtAERIGAWDvDTRIDVTLDGLGLGGVDR 170
Cdd:cd03298 79 NNLFAHLTVEQNV-------------------GLGLSP---------------GLKLTAED-RQAIEVALARVGLAGLEK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586061923 171 dRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDA 210
Cdd:cd03298 124 -RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-232 |
1.35e-16 |
|
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: 81.69 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGDPL--------------RVGLLYQEPPFAPHDTV 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIR-LG-GEVLqdsargiflpphrrRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 100 AQAVESAVRtvrdaasavdrtadalaRAPEDEGAAtayaaaldtaerigawDVDTRIDVtldgLGLGGVdRDRSTGALSG 179
Cdd:COG4148 95 RGNLLYGRK-----------------RAPRAERRI----------------SFDEVVEL----LGIGHL-LDRRPATLSG 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 180 GQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAA----TDFLRATLRSWHGPVLLASHD 232
Cdd:COG4148 137 GERQRVAIGRALLSSPRLLLMDEPLAALDLARkaeiLPYLERLRDELDIPILYVSHS 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-248 |
1.38e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.69 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrvgllYQEPPfap 95
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL-------------WQGEP--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 hdtvaqavesaVRTVRDA----------ASAVDR--TAD-------ALARAPEDEgaatayaaaldtaeriGAWDVdtri 156
Cdd:PRK13538 65 -----------IRRQRDEyhqdllylghQPGIKTelTALenlrfyqRLHGPGDDE----------------ALWEA---- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 157 dvtLDGLGLGGVDrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSwH----GPVLLASHD 232
Cdd:PRK13538 114 ---LAQVGLAGFE-DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ-HaeqgGMVILTTHQ 188
|
250
....*....|....*.
gi 1586061923 233 RAFLDTAVTSLVDLDP 248
Cdd:PRK13538 189 DLPVASDKVRKLRLGQ 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
17-208 |
1.53e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.82 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL----------RVGL 86
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL--NGRPLadwspaelarRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEP----PFAPHDTVAQAVESAVRTVRDAASAVDRtadALARapedegaatayaaaldtaerigawdvdtridVTLDG 162
Cdd:PRK13548 81 LPQHSslsfPFTVEEVVAMGRAPHGLSRAEDDALVAA---ALAQ-------------------------------VDLAH 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 163 LglggvdRDRSTGALSGGQRSRLSLA------WLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13548 127 L------AGRDYPQLSGGEQQRVQLArvlaqlWEPDGPPRWLLLDEPTSALD 172
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-220 |
1.58e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDP-----LRVGLL 87
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidgKPVRIRSPrdaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPPFAPHDTVAQ----AVESAVRTVRDAASAVDRTADALARapedegaatayaaaldtaerigawdvdtridvtldgL 163
Cdd:COG3845 86 HQHFMLVPNLTVAEnivlGLEPTKGGRLDRKAARARIRELSER------------------------------------Y 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 164 GLgGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:COG3845 130 GL-DVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILR 185
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-208 |
1.88e-16 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 78.88 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG----DPL----RVGLL 87
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireqDPVelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPPFAPHDTVAQAVEsavrtvrdaasavdrTADALARAPEdegaatayaaaldtaERIgawdvDTRIDVTLDGLGLGG 167
Cdd:cd03295 81 IQQIGLFPHMTVEENIA---------------LVPKLLKWPK---------------EKI-----RERADELLALVGLDP 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586061923 168 VD-RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03295 126 AEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-208 |
2.18e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgdPL----------RV 84
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--VLseetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPpfaphDTvaQAVESAVRtvrdaasavdrtaDALARAPEDEGaatayaaaldtaerIGAWDVDTRIDVTLDGLG 164
Cdd:PRK13635 84 GMVFQNP-----DN--QFVGATVQ-------------DDVAFGLENIG--------------VPREEMVERVDQALRQVG 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1586061923 165 LGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13635 130 MEDF-LNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
17-232 |
3.46e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVltDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---LGDP--LR-VGLLYQE 90
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPpaERpVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVesavrtvrdaasavdrtadALARAPedegaatayAAALDTAERigawdvdTRIDVTLDGLGLGGVDr 170
Cdd:COG3840 80 NNLFPHLTVAQNI-------------------GLGLRP---------GLKLTAEQR-------AQVEQALERVGLAGLL- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 171 DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAatdfLRA-------TLRSWHG-PVLLASHD 232
Cdd:COG3840 124 DRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA----LRQemldlvdELCRERGlTVLMVTHD 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-231 |
3.83e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 77.79 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHR----VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG---DPL----RVG 85
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvvkEPAearrRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAVESAVR---TVRDAASAvdrtadalarapedegaatayaaaldtaerigawdvdtRIDVTLDG 162
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGlygLKGDELTA--------------------------------------RLEELADR 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 163 LGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRAtLRSWHGPVLLASH 231
Cdd:cd03266 124 LGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATralrEFIRQ-LRALGKCILFSTH 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
404-558 |
7.29e-16 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 75.50 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLDqdatlpGADPEHTAAHIYHELVGedraeT 483
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI---------LID------GVDLRDLDLESLRKNIA-----Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 484 VPLGTFgLLAG--RdENRrvgeLSVGQRRRLALA-VLLADPPhVLLLDEPTNHFSLVLATQLEAAVPDYPG--TVLVASH 558
Cdd:cd03228 81 VPQDPF-LFSGtiR-ENI----LSGGQRQRIAIArALLRDPP-ILILDEATSALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-204 |
7.55e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 76.70 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDP---LRVGLLY- 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgRDITGLPPherARAGIGYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 -QEPPFAPHDTVAQAVESAVRTVRDAASAvDRTADALARAPEdegaatayaaaldTAERigawdvdtridvtldglglgg 167
Cdd:cd03224 81 pEGRRIFPELTVEENLLLGAYARRRAKRK-ARLERVYELFPR-------------LKER--------------------- 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586061923 168 vdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPT 204
Cdd:cd03224 126 --RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
404-559 |
8.20e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 77.05 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------AAPGVRVGLLDQ----DATLP---------GADP 464
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQraevDWDFPitvrdvvlmGRYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 465 EHTAAHIY----HELVgeDRAetvpLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTN-------- 532
Cdd:COG1121 105 RRGLFRRPsradREAV--DEA----LERVGLEDLAD--RPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAgvdaatee 176
|
170 180
....*....|....*....|....*..
gi 1586061923 533 HFSLVLATQLEAAVpdypgTVLVASHD 559
Cdd:COG1121 177 ALYELLRELRREGK-----TILVVTHD 198
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-232 |
9.05e-16 |
|
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: 79.00 E-value: 9.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV---------RAVGLGDPL---RVGLLYQEPPFAPHDTVAQ 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdSRKGIFLPPekrRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 AVESAVRTVRDAasavdrtadalarapedegaatayaaaldtaERIGAWDVDTRIdvtldgLGLGGVdRDRSTGALSGGQ 181
Cdd:TIGR02142 95 NLRYGMKRARPS-------------------------------ERRISFERVIEL------LGIGHL-LGRLPGRLSGGE 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 182 RSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD----FLRATLRSWHGPVLLASHD 232
Cdd:TIGR02142 137 KQRVAIGRALLSSPRLLLMDEPLAALDDPRKYeilpYLERLHAEFGIPILYVSHS 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
404-558 |
9.72e-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: 76.47 E-value: 9.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDATL---------PGAD 463
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldPADLRRNIGYVPQDVTLfygtlrdniTLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 464 PEHTAAHIyhelvgEDRAETVPLGTFGLLAGRDENRRVGE----LSVGQRRRLALA-VLLADPPhVLLLDEPTNHFSLVL 538
Cdd:cd03245 103 PLADDERI------LRAAELAGVTDFVNKHPNGLDLQIGErgrgLSGGQRQAVALArALLNDPP-ILLLDEPTSAMDMNS 175
|
170 180
....*....|....*....|..
gi 1586061923 539 ATQLEAAVPDYPG--TVLVASH 558
Cdd:cd03245 176 EERLKERLRQLLGdkTLIIITH 197
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
394-558 |
1.27e-15 |
|
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: 75.47 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 394 AAEVAGRM--APVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQDAT-------LPGADP 464
Cdd:TIGR01189 7 ACSRGERMlfEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEnilylghLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 465 EHTAA---HIYHELVG-EDRAETVPLGTFGLLAGrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLAT 540
Cdd:TIGR01189 87 ELSALenlHFWAAIHGgAQRTIEDALAAVGLTGF--EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 1586061923 541 QLEAAVPDY---PGTVLVASH 558
Cdd:TIGR01189 165 LLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
404-531 |
1.37e-15 |
|
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: 76.00 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH----------AAPGVRVGLLDQDATLpgaDPEHTAA---H 470
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQFDAL---FDELTVRehlR 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 471 IYHELVG---EDRAETVP--LGTFGLLAgrDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03263 98 FYARLKGlpkSEIKEEVEllLRVLGLTD--KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-250 |
1.86e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.44 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASYGSHR----VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---LGDPLRVGLL 87
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 88 YQEPPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldTAERIGAWdvdtridvtLDGLGLGG 167
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLR---------------LRGVPKAE-----------RRARAEEL---------LALVGLAD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 168 VDRdRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAATdflRAT-----LRSW---HGPVLLASHDrafLDTA 239
Cdd:COG4525 127 FAR-RRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGAL-DALT---REQmqellLDVWqrtGKGVFLITHS---VEEA 198
|
250
....*....|....
gi 1586061923 240 V---TSLVDLDPAP 250
Cdd:COG4525 199 LflaTRLVVMSPGP 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-234 |
2.19e-15 |
|
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: 75.55 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 10 TPNTAAHIRVSGISASYGSHR----VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV------------ 73
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVrlagqdlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 74 --RAVGLGDplRVGLLYQEPPFAPHDT----VAQAVEsaVRTVRDAAsavDRTADALARapedegaatayaaaldtaeri 147
Cdd:COG4181 82 daRARLRAR--HVGFVFQSFQLLPTLTalenVMLPLE--LAGRRDAR---ARARALLER--------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 148 gawdvdtridvtldgLGLGgvdrDRST---GALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAAT-----DFLRAtL 219
Cdd:COG4181 134 ---------------VGLG----HRLDhypAQLSGGEQQRVALARAFATEPAILFADEPTGNL-DAATgeqiiDLLFE-L 192
|
250
....*....|....*.
gi 1586061923 220 RSWHGPVL-LASHDRA 234
Cdd:COG4181 193 NRERGTTLvLVTHDPA 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-232 |
2.25e-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: 75.83 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 26 YGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgDPLRvgllyQEPPFAPHDTVAQAVES 105
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWK-----RRKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 106 AVR---TVRDAASAVDRtadaLARAPEDEGAatayaaaldtaerigawdvdTRIDVTLDGLGLGGVdRDRSTGALSGGQR 182
Cdd:cd03267 105 QLWwdlPVIDSFYLLAA----IYDLPPARFK--------------------KRLDELSELLDLEEL-LDTPVRQLSLGQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 183 SRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSW---HGP-VLLASHD 232
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnreRGTtVLLTSHY 213
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
11-245 |
3.60e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 78.54 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 11 PNTAAHIRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGdplrvglLY 88
Cdd:TIGR01842 311 PEPEGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD-------LK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 QEPP--FAPH-DTVAQAVESAVRTVRDAASAVDRTAD-----ALARAPedegaatayaaaldtaeriGAWDVDTRIDVTL 160
Cdd:TIGR01842 384 QWDRetFGKHiGYLPQDVELFPGTVAENIARFGENADpekiiEAAKLA-------------------GVHELILRLPDGY 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 161 DG-LGLGGvdrdrstGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRAT---LRSWHGPVLLASHdRAfl 236
Cdd:TIGR01842 445 DTvIGPGG-------ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAikaLKARGITVVVITH-RP-- 514
|
....*....
gi 1586061923 237 dtAVTSLVD 245
Cdd:TIGR01842 515 --SLLGCVD 521
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-208 |
4.01e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVglGDPLrvgllyqeppfapH 96
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVA--GDDV-------------E 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVAQAVESAVRTV-RDAASAVD---RTADALARAPEdegaatayaaaldtAERIGAWDVDTRIDVTlDGLGLGGVDR-- 170
Cdd:PRK09536 69 ALSARAASRRVASVpQDTSLSFEfdvRQVVEMGRTPH--------------RSRFDTWTETDRAAVE-RAMERTGVAQfa 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586061923 171 DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
32-238 |
4.41e-15 |
|
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: 74.37 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG--LGD------PL---RVGLLYQEPPFAPHDTVA 100
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdVSDlrgraiPYlrrKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 101 QAVESAVRTVrdaasavdrtadalarapedegaatayaaaldtaeRIGAWDVDTRIDVTLDGLGLGGVDRDRSTGaLSGG 180
Cdd:cd03292 97 ENVAFALEVT-----------------------------------GVPPREIRKRVPAALELVGLSHKHRALPAE-LSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 181 QRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH---GPVLLASHDRAFLDT 238
Cdd:cd03292 141 EQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDT 201
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-204 |
5.44e-15 |
|
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: 74.63 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR-------------AVGLGdplrV 84
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglpphrIARLG----I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADALARAPEdegaatayaaaldTAERigawdvdtridvtldglg 164
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELFPR-------------LKER------------------ 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586061923 165 lggvdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPT 204
Cdd:COG0410 130 -----RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
17-212 |
5.85e-15 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 74.64 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS-HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAG-------EVRAVGlGDPLR----- 83
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGsillegtDITKLR-GKKLRklrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 VGLLYQEPPFAPHDTVAQAVESAvrtvRDAASAVDRTAdaLARAPEdegaatayaaaldtAERIGAWDVDTRidVTLDGL 163
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHG----RLGYKPTWRSL--LGRFSE--------------EDKERALSALER--VGLADK 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 164 GLGGVDrdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:TIGR02315 139 AYQRAD------QLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTS 181
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
404-559 |
6.04e-15 |
|
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: 74.11 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------AAPGVRVGLLDQ----DATLP---------GADP 464
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQrrsiDRDFPisvrdvvlmGLYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 465 EHTAAHIYHElvgEDRAE-TVPLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNhfSLVLATQ-- 541
Cdd:cd03235 98 HKGLFRRLSK---ADKAKvDEALERVGLSELAD--RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA--GVDPKTQed 170
|
170 180
....*....|....*....|.
gi 1586061923 542 ---LEAAVPDYPGTVLVASHD 559
Cdd:cd03235 171 iyeLLRELRREGMTILVVTHD 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
404-559 |
6.76e-15 |
|
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: 72.82 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV----------HAAPGVRVGLLDQDATLpgadpehtaahiYH 473
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkdikkePEEVKRRIGYLPEEPSL------------YE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 474 ELVGEDraetvplgtfgLLagrdenrrvgELSVGQRRRLALAV-LLADPPhVLLLDEPTNHFSLVLATQLEAAVPDY--- 549
Cdd:cd03230 87 NLTVRE-----------NL----------KLSGGMKQRLALAQaLLHDPE-LLILDEPTSGLDPESRREFWELLRELkke 144
|
170
....*....|
gi 1586061923 550 PGTVLVASHD 559
Cdd:cd03230 145 GKTILLSSHI 154
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-208 |
6.90e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.02 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV--RAVGLGDPLR-------VGL 86
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvSGIDTGDFSKlqgirklVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPpfaphdtvaqAVESAVRTVRdaasavdrtaDALARAPEDEGaatayaaaldtaerIGAWDVDTRIDVTLDGLGLG 166
Cdd:PRK13644 82 VFQNP----------ETQFVGRTVE----------EDLAFGPENLC--------------LPPIEIRKRVDRALAEIGLE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586061923 167 GVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13644 128 KY-RHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-208 |
7.12e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVglGDPL----------RVGL 86
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG--DKPIsmlssrqlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPPfAPHD-TVAQAVesavrtvrdaasavdrtadALARAP----------EDEgaatayaaaldtaERIGAWDVDTR 155
Cdd:PRK11231 81 LPQHHL-TPEGiTVRELV-------------------AYGRSPwlslwgrlsaEDN-------------ARVNQAMEQTR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 156 IDvTLdglglggvdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11231 128 IN-HL---------ADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-208 |
9.04e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.97 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG--DP--------LRVGL 86
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPkvderlirQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPPFAPHDTVAQAVESAVRTVRDAASAvdrTADALARApedegaatayaaaldtaerigawdvdtridvTLDGLGLG 166
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRGASKE---EAEKQARE-------------------------------LLAKVGLA 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586061923 167 gvDR-DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK09493 128 --ERaHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
404-558 |
9.75e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGvrvgllDQDATLPGAD-----------PEHTA---- 468
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVAEAchylghrnamkPALTVaenl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 ---AHIYHelvGEDRAETVPLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNH--------FSLV 537
Cdd:PRK13539 95 efwAAFLG---GEELDIAAALEAVGL--APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAldaaavalFAEL 169
|
170 180
....*....|....*....|.
gi 1586061923 538 LATQLEAAvpdypGTVLVASH 558
Cdd:PRK13539 170 IRAHLAQG-----GIVIAATH 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
404-564 |
9.79e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.65 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQDATLPGADPEHTA--------AHI--YH 473
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRdlvamgrwARRglWR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 474 ELVGEDRAETV-PLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPG- 551
Cdd:NF040873 91 RLTRDDRAAVDdALERVGL--ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAr 168
|
170
....*....|....*
gi 1586061923 552 --TVLVASHDRWLRR 564
Cdd:NF040873 169 gaTVVVVTHDLELVR 183
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-231 |
1.47e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.31 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY--GS---HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV---------RAVGLGD-P 81
Cdd:PRK13637 3 IKIENLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdKKVKLSDiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 82 LRVGLLYQEPPFaphdtvaQAVESAVRtvRDaasavdrtadaLARAPEDEGaatayaaaldtaerIGAWDVDTRIDVTLD 161
Cdd:PRK13637 83 KKVGLVFQYPEY-------QLFEETIE--KD-----------IAFGPINLG--------------LSEEEIENRVKRAMN 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 162 GLGLGGVD-RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG----PVLLASH 231
Cdd:PRK13637 129 IVGLDYEDyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeynmTIILVSH 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-232 |
1.48e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvglGDPLRVGLLYQEPPFAPh 96
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR---NGKLRIGYVPQKLYLDT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 dTVAQAVESAVRT---VR--DAASAVDRT-ADALARAPEDEgaatayaaaldtaerigawdvdtridvtldglglggvdr 170
Cdd:PRK09544 81 -TLPLTVNRFLRLrpgTKkeDILPALKRVqAGHLIDAPMQK--------------------------------------- 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 171 drstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDD----AATDFLRATLRSWHGPVLLASHD 232
Cdd:PRK09544 121 ------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvALYDLIDQLRRELDCAVLMVSHD 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-208 |
1.67e-14 |
|
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: 73.69 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGdplrvglLYQEPPfap 95
Cdd:TIGR02769 11 TYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQD-------LYQLDR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 hdTVAQAVESAVRTV-RDAASAVD--RTADALARAPedegaatayaaaLDTAERIGAWDVDTRIDVTLDGLGLGGVDRDR 172
Cdd:TIGR02769 81 --KQRRAFRRDVQLVfQDSPSAVNprMTVRQIIGEP------------LRHLTSLDESEQKARIAELLDMVGLRSEDADK 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586061923 173 STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:TIGR02769 147 LPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
25-77 |
1.72e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.19 E-value: 1.72e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 25 SYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG 77
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-208 |
1.96e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.98 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------GDPLRVGLLYQE 90
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVESAVRTVRDAASAVD-RTADALARapedegaatayaaaldtaerigawdvdtridVTLDGLGlggvd 169
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITpRVMEALRM-------------------------------VQLEEFA----- 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586061923 170 rDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK09452 139 -QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-250 |
2.03e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL---GDPLRVGLLYQEPPF 93
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpveGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 94 APHDTVAQAVESAVRTvrdaaSAVDRtADALARAPEdegaatayaaaldtaerigawdvdtridvTLDGLGLGGVDRdRS 173
Cdd:PRK11248 82 LPWRNVQDNVAFGLQL-----AGVEK-MQRLEIAHQ-----------------------------MLKKVGLEGAEK-RY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 174 TGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRA-TLRSWHG---PVLLASHDrafLDTAV---TSLVDL 246
Cdd:PRK11248 126 IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTlLLKLWQEtgkQVLLITHD---IEEAVfmaTELVLL 202
|
....
gi 1586061923 247 DPAP 250
Cdd:PRK11248 203 SPGP 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-232 |
2.11e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.17 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 5 PHSPATPNTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRA-----VGLG 79
Cdd:PRK11247 1 MMNTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtaplAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 80 DPLRvgLLYQEPPFAPHDTVAQAVESAVRtvrdaasavdrtadalarapedegaatayaaaldtaeriGAWDVDTRidVT 159
Cdd:PRK11247 81 EDTR--LMFQDARLLPWKKVIDNVGLGLK---------------------------------------GQWRDAAL--QA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 160 LDGLGLGgvdrDRST---GALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAATDF----LRATLRSWHG-PVLLASH 231
Cdd:PRK11247 118 LAAVGLA----DRANewpAALSGGQKQRVALARALIHRPGLLLLDEPLGAL-DALTRIemqdLIESLWQQHGfTVLLVTH 192
|
.
gi 1586061923 232 D 232
Cdd:PRK11247 193 D 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-207 |
2.39e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGDPLR--------- 83
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL-ID-GQEMRfasttaala 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 --VGLLYQEPPFAPHDTVAQAVesavrtvrdaasavdrtadALARAPEDEGAATAYAAALDTAERigawdvdtridvtLD 161
Cdd:PRK11288 79 agVAIIYQELHLVPEMTVAENL-------------------YLGQLPHKGGIVNRRLLNYEAREQ-------------LE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 162 GLGLgGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHL 207
Cdd:PRK11288 127 HLGV-DIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
404-530 |
2.64e-14 |
|
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: 72.12 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------AAPGVRVGLLDQDATL------------------ 459
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQQDALlpwltvldnvalglelqg 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 460 -PGADPEHTAAHiYHELVGedraetvplgtfglLAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03293 103 vPKAEARERAEE-LLELVG--------------LSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
404-532 |
2.88e-14 |
|
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: 72.81 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSvhaapgvRVGLLDQdaTLPGAD-------------------- 463
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN-------DVRLFGE--RRGGEDvwelrkriglvspalqlrfp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 464 PEHTAAHI-----------YHELVGED--RAETVpLGTFGLlaGRDENRRVGELSVGQRRRLALA-VLLADPPhVLLLDE 529
Cdd:COG1119 93 RDETVLDVvlsgffdsiglYREPTDEQreRAREL-LELLGL--AHLADRPFGTLSQGEQRRVLIArALVKDPE-LLILDE 168
|
...
gi 1586061923 530 PTN 532
Cdd:COG1119 169 PTA 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
404-531 |
2.95e-14 |
|
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: 72.47 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH--------------AAPG-------------------VRV 450
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglppheiARLGigrtfqiprlfpeltvlenVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 451 GLLdqdATLPGADPEHTAAHIYHELvgEDRAETVpLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03219 99 AAQ---ARTGSGLLLARARREEREA--RERAEEL-LERVGLADLAD--RPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
.
gi 1586061923 531 T 531
Cdd:cd03219 171 A 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-239 |
3.09e-14 |
|
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: 75.55 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 2 AHPPHSPAT--PNTAAHIRVSGISASY-GSHR-VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR--- 74
Cdd:COG4618 314 AVPAEPERMplPRPKGRLSVENLTVVPpGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldg 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 75 -AVGLGDPLR----VGLLYQEPPFAPhDTVAQAV----ESAVRTVRDAASAVDrTADALARAPEdegaatayaaaldtae 145
Cdd:COG4618 394 aDLSQWDREElgrhIGYLPQDVELFD-GTIAENIarfgDADPEKVVAAAKLAG-VHEMILRLPD---------------- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 146 riGawdVDTRIdvtldglGLGGvdrdrstGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH-- 223
Cdd:COG4618 456 --G---YDTRI-------GEGG-------ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKar 516
|
250
....*....|....*..
gi 1586061923 224 -GPVLLASHDRAFLDTA 239
Cdd:COG4618 517 gATVVVITHRPSLLAAV 533
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-208 |
3.82e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.69 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAG-------EVRAVGLGD--------- 80
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqTINLVRDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 81 -----PLRVGLLYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRtadalarapedegaatayaaaldtaerigawdvdTR 155
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEAR----------------------------------ER 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 156 IDVTLDGLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK10619 132 AVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
404-559 |
4.16e-14 |
|
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: 72.14 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGV---RVGLLDQDATLpGADPEHT----- 467
Cdd:COG1124 24 VSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtRRRRKAfrrRVQMVFQDPYA-SLHPRHTvdril 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 468 --AAHIYHELVGEDRAETVpLGTFGLLAG-RDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNhfSLVLATQ--- 541
Cdd:COG1124 103 aePLRIHGLPDREERIAEL-LEQVGLPPSfLD--RYPHQLSGGQRQRVAIARALILEPELLLLDEPTS--ALDVSVQaei 177
|
170 180
....*....|....*....|.
gi 1586061923 542 ---LEAAVPDYPGTVLVASHD 559
Cdd:COG1124 178 lnlLKDLREERGLTYLFVSHD 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-531 |
4.93e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.84 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRA--PDAGEV--------RAVGLGDPLRVG- 85
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalceKCGYVERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 --------LLYQEPPF-APHDTVAQAVESAV-----RTVrdAASAVDRTADALARAPEDEGAAtayaaaldtaeriGAWD 151
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFwNLSDKLRRRIRKRIaimlqRTF--ALYGDDTVLDNVLEALEEIGYE-------------GKEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 152 VDTRIDVtLDGLGLG----GVDRDrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD----DAATDFLRATLRSWH 223
Cdd:TIGR03269 146 VGRAVDL-IEMVQLShritHIARD-----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtaKLVHNALEEAVKASG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 224 GPVLLASHDRAFLDTAVTSLVDLDPaprphavtsdlvgdgtgtgiGVTRFGGTYSQYVLARMDTRERWErtyRDEQAQLK 303
Cdd:TIGR03269 220 ISMVLTSHWPEVIEDLSDKAIWLEN--------------------GEIKEEGTPDEVVAVFMEGVSEVE---KECEVEVG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 304 KlraavreqqtvghsgrsPKTEGRAAKKFYADRNATVVsRRVNGararlatvedeqirkpprelyfqgltaglsgseaal 383
Cdd:TIGR03269 277 E-----------------PIIKVRNVSKRYISVDRGVV-KAVDN------------------------------------ 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 384 hrtgpvltasaaevagrmapVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgVRVGLLDQDATLPGAD 463
Cdd:TIGR03269 303 --------------------VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN----VRVGDEWVDMTKPGPD 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 464 PE----------HTAAHIY-HELVGEDRAETVPL---GTFGLL--------AGRDE-------NRRVGELSVGQRRRLAL 514
Cdd:TIGR03269 359 GRgrakryigilHQEYDLYpHRTVLDNLTEAIGLelpDELARMkavitlkmVGFDEekaeeilDKYPDELSEGERHRVAL 438
|
570
....*....|....*..
gi 1586061923 515 AVLLADPPHVLLLDEPT 531
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPT 455
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-208 |
5.65e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrvgllYQEPPFAP 95
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVS-------------WRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 HDTVAQ-AVESAVRTV-RDAASAVD--RTADALARAPedegaaTAYAAALDTAERIgawdvdTRIDVTLDGLGLGGVDRD 171
Cdd:PRK10419 79 LNRAQRkAFRRDIQMVfQDSISAVNprKTVREIIREP------LRHLLSLDKAERL------ARASEMLRAVDLDDSVLD 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586061923 172 RSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK10419 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-208 |
6.01e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.04 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 29 HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV--------------RAVGLGdplRVgllYQEPPF- 93
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklpeykRAKYIG---RV---FQDPMMg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 94 -APHDTVAQ--AVESAVRTVRDAASAVDRTADALARApedegaatayaaaldtaerigawdvdtridvTLDGLGLGGVDR 170
Cdd:COG1101 93 tAPSMTIEEnlALAYRRGKRRGLRRGLTKKRRELFRE-------------------------------LLATLGLGLENR 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586061923 171 -DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG1101 142 lDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
30-208 |
6.66e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.36 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD-------------PLR--VGLLYQeppFA 94
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT---IGErvitagkknkklkPLRkkVGIVFQ---FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PHDTVAQAVEsavrtvRDAA-----SAVDRtADALARAPEdegaatayaaaldtaerigawdvdtridvTLDGLGLGGVD 169
Cdd:PRK13634 95 EHQLFEETVE------KDICfgpmnFGVSE-EDAKQKARE-----------------------------MIELVGLPEEL 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586061923 170 RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13634 139 LARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
404-531 |
7.93e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.86 E-value: 7.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAA--------PGVR--VGLLDQDATLpgaDPEHTA----- 468
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvrepREVRrrIGIVFQDLSV---DDELTGwenly 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 469 --AHIYHeLVGEDRAETVP--LGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03265 96 ihARLYG-VPGAERRERIDelLDFVGLLEAAD--RLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-233 |
8.98e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 69.55 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYG--SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgdPLRvglLYQEPPFA 94
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA--DIS---QWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PH-DTVAQAVESAVRTVRDAasavdrtadalarapedegaatayaaaldtaerigawdvdtridvtldglglggvdrdrs 173
Cdd:cd03246 76 DHvGYLPQDDELFSGSIAEN------------------------------------------------------------ 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 174 tgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSW-----------HGPVLLASHDR 233
Cdd:cd03246 96 --ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALkaagatriviaHRPETLASADR 164
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-208 |
9.19e-14 |
|
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: 71.11 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHR--VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAG-------EVRAVGLGDpLR--VG 85
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGrilidghDVRDYTLAS-LRrqIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEpPFAPHDTVAQAVESAvrtVRDAASAVDRTADALARAPE-----DEGaatayaaaldtaerigawdVDTRIdvtl 160
Cdd:cd03251 80 LVSQD-VFLFNDTVAENIAYG---RPGATREEVEEAARAANAHEfimelPEG-------------------YDTVI---- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586061923 161 dglGLGGVDrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03251 133 ---GERGVK-------LSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
404-536 |
9.22e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------AAPGVRVgLLDQDATLPGA--DPEHTAAHiyhEL 475
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpiSMLSSRQ-LARRLALLPQHhlTPEGITVR---EL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 476 VGEDRAETVPLgtFGLLAGRDE----------------NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSL 536
Cdd:PRK11231 97 VAYGRSPWLSL--WGRLSAEDNarvnqameqtrinhlaDRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
404-531 |
9.56e-14 |
|
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: 71.22 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH--------------AAPG-------------------VRV 450
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriARLGiartfqnprlfpeltvlenVLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 451 GLLDQDATLPGADPEHTAAHIYHELVGEDRAETVpLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:COG0411 103 AAHARLGRGLLAALLRLPRARREEREARERAEEL-LERVGL--ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEP 179
|
.
gi 1586061923 531 T 531
Cdd:COG0411 180 A 180
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-73 |
1.67e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.87 E-value: 1.67e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1586061923 24 ASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV 73
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
404-531 |
1.73e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 70.07 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgvrvgLLDQD-ATLPGAD------------------- 463
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVL--------IDGQDiSSLSERElarlrrrhigfvfqffnll 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 464 PEHTA------AHIYHEL---VGEDRAETVpLGTFGLlAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:COG1136 99 PELTAlenvalPLLLAGVsrkERRERAREL-LERVGL-GDR-LDHRPSQLSGGQQQRVAIARALVNRPKLILADEPT 172
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-221 |
1.91e-13 |
|
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: 72.78 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 5 PHSPATPNTAAHIRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV-------RAV 76
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 77 GLGDPLRVGLLYQEPPFAPHDTVAQAVESAVRTVRDAAsavdrTADALARApedegaatayaaaldtaeRIGAWdvdtrI 156
Cdd:TIGR02868 403 DQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEE-----LWAALERV------------------GLADW-----L 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 157 DVTLDGLG--LGGVDRdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRS 221
Cdd:TIGR02868 455 RALPDGLDtvLGEGGA-----RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA 516
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-231 |
2.26e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.92 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 28 SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD-------------PLR--VGLLYQEPP 92
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT---VGDivvsstskqkeikPVRkkVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 93 faphdtvAQAVESAVrtVRDaasavdrtadaLARAPEDEGaatayaAALDTAERIGAwdvdtridVTLDGLGLGGVDRDR 172
Cdd:PRK13643 95 -------SQLFEETV--LKD-----------VAFGPQNFG------IPKEKAEKIAA--------EKLEMVGLADEFWEK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 173 STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWH---GPVLLASH 231
Cdd:PRK13643 141 SPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTH 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-232 |
2.31e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 14 AAHIRVSGISASY----GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL------GDPL- 82
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 -----RVGLLYQEPPFAPHDTVAQAVESAvrtvrdAASAVDRTADALARAPEdegaatayaaaldtaerigawdvdtrid 157
Cdd:PRK10535 82 qlrreHFGFIFQRYHLLSHLTAAQNVEVP------AVYAGLERKQRLLRAQE---------------------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 158 vTLDGLGLGgvDR-DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRAT---LRSWHGPVLLASHD 232
Cdd:PRK10535 128 -LLQRLGLE--DRvEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIlhqLRDRGHTVIIVTHD 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-208 |
2.41e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 22 ISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV---------RAVGLGDplrVGLLYQEPP 92
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthRSIQQRD---ICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 93 FAPHDTVAQAVESAVRTV-RDAASAVDRTADALARapedegaatayaaaldtaerigawdvdtridVTLDGLGlggvdrD 171
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLgVPKEERKQRVKEALEL-------------------------------VDLAGFE------D 131
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586061923 172 RSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11432 132 RYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-232 |
2.83e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.15 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPL--------RVGLLYQEPP---FAphDT 98
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwvrsKVGLVFQDPDdqvFS--ST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 VAQAVESAVRTVRDAASAVDRTADALARApedegaatayaaaldtaerIGAWDVdtridvtldglglggvdRDRSTGALS 178
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEVERRVEEALKA-------------------VRMWDF-----------------RDKPPYHLS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG---PVLLASHD 232
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHD 197
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
30-221 |
2.89e-13 |
|
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: 68.73 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAP--DAGEVRAVGLGDPL-----RVGLLYQEPPFAPHDTVAQA 102
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKrsfrkIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 103 VESAVRtvrdaasavdrtadalarapedegaatayaaaldtaerigawdvdtridvtLDGLglggvdrdrstgalSGGQR 182
Cdd:cd03213 103 LMFAAK---------------------------------------------------LRGL--------------SGGER 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586061923 183 SRLSLAWLLLSTPDVLLLDEPTNHLdDAATDFLRA-TLRS 221
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGL-DSSSALQVMsLLRR 156
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
405-530 |
3.18e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH----AAPGVRVGLLDQDATL---PGADPEHTAA---HIYHE 474
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgePIRRQRDEYHQDLLYLghqPGIKTELTALenlRFYQR 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 475 LVGEDRAETVP--LGTFGLlAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK13538 101 LHGPGDDEALWeaLAQVGL-AGF-EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-213 |
3.25e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.88 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASY----GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGDPL--------- 82
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVL-VD-GVDLtalserelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 ----RVGLLYQeppfapHD------TVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdV 152
Cdd:COG1135 79 aarrKIGMIFQ------HFnllssrTVAENVALPLE---------------IAGVPKAE--------------------I 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 153 DTRIDVTLDGLGLGgvDR-DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD 213
Cdd:COG1135 118 RKRVAELLELVGLS--DKaDAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-208 |
4.27e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 8 PATPNTAAHIRVSGISASY-----------GSHRVLTDISFSVTAGDPTGLIGENGSGKST----LLRIVAGlrapdAGE 72
Cdd:PRK15134 267 PLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 73 VraVGLGDPL-------------RVGLLYQEPPFA--PHDTVAQAVESAVRTVRDAASAVDRTADALARAPEdegaatay 137
Cdd:PRK15134 342 I--WFDGQPLhnlnrrqllpvrhRIQVVFQDPNSSlnPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEE-------- 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 138 aaaldtaerigawdvdtridvtldgLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK15134 412 -------------------------VGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
404-531 |
4.39e-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: 68.67 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgvrvgLLDQDATlpgADPEHTAAHIYHELVG------ 477
Cdd:cd03255 23 VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR--------VDGTDIS---KLSEKELAAFRRRHIGfvfqsf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 478 --------------------------EDRAETVpLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03255 92 nllpdltalenvelplllagvpkkerRERAEEL-LERVGL--GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-208 |
4.98e-13 |
|
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: 68.84 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGlRAPDAGEVRAVGL--GDPL-------RVGLLYQEPPFAPHDTVA 100
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSGQILfnGQPRkpdqfqkCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 101 QAVESAVRtvrdaaSAVDRTADALARAPEDEgaatayaaaldtaerigawdvdtriDVTLDGLGLGGVdRDRSTGALSGG 180
Cdd:cd03234 100 ETLTYTAI------LRLPRKSSDAIRKKRVE-------------------------DVLLRDLALTRI-GGNLVKGISGG 147
|
170 180
....*....|....*....|....*...
gi 1586061923 181 QRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03234 148 ERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
406-571 |
5.91e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 406 LTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQDatlPGADPE------------HTAAHI-- 471
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQD---PPRNVEgtvydfvaegieEQAEYLkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 472 YHEL---VGEDRAETV-------------------------PLGTFGLlagrDENRRVGELSVGQRRRLALAVLLADPPH 523
Cdd:PRK11147 101 YHDIshlVETDPSEKNlnelaklqeqldhhnlwqlenrineVLAQLGL----DPDAALSSLSGGWLRKAALGRALVSNPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586061923 524 VLLLDEPTNHFSLVLATQLEAAVPDYPGTVLVASHDRWLRRNWTGR--DL 571
Cdd:PRK11147 177 VLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRivDL 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-221 |
7.31e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRA--------------VGLGDPL 82
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 R--VGLLYQEPPFAPHDTVAQAV-ESAV---RTVRDAASAVDRtaDALARapedegaatayaaaldtaerigawdvdtri 156
Cdd:PRK11264 84 RqhVGFVFQNFNLFPHRTVLENIiEGPVivkGEPKEEATARAR--ELLAK------------------------------ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 157 dvtldgLGLGGVDrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRS 221
Cdd:PRK11264 132 ------VGLAGKE-TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ 189
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
404-558 |
7.47e-13 |
|
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: 67.63 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGsvhaapgvRVGLLDQDATLPGADPEHTAAHI-----YHELVGE 478
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSG--------EITFDGKSYQKNIEALRRIGALIeapgfYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 479 DRaetvpLGTFGLLAGRDENR----------------RVGELSVGQRRRLALAVLLADPPHVLLLDEPTNH---FSLVLA 539
Cdd:cd03268 91 EN-----LRLLARLLGIRKKRidevldvvglkdsakkKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGldpDGIKEL 165
|
170
....*....|....*....
gi 1586061923 540 TQLEAAVPDYPGTVLVASH 558
Cdd:cd03268 166 RELILSLRDQGITVLISSH 184
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
403-530 |
9.15e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 68.58 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------AAPGVRVGLLDQDATL----------------- 459
Cdd:COG1116 29 DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVVFQEPALlpwltvldnvalglelr 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 460 --PGADPEHTAAHiYHELVGedraetvplgtfglLAGRdENRRVGELSVGQRRRLALA-VLLADPPhVLLLDEP 530
Cdd:COG1116 109 gvPKAERRERARE-LLELVG--------------LAGF-EDAYPHQLSGGMRQRVAIArALANDPE-VLLMDEP 165
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-220 |
9.68e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.06 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGD-------PLR--VG 85
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF---IGEkrmndvpPAErgVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGL 165
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLK---------------LAGAKKEE--------------------INQRVNQVAEVLQL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 166 GGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAatdfLRATLR 220
Cdd:PRK11000 124 AHL-LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA----LRVQMR 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-232 |
1.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 68.72 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 27 GSHrVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV---------RAVGLGDpLR--VGLLYQEPP--- 92
Cdd:PRK13636 18 GTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidySRKGLMK-LResVGMVFQDPDnql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 93 FAPhdTVAQAVESAVRTVRdaasavdrtadalarAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGVdRDR 172
Cdd:PRK13636 96 FSA--SVYQDVSFGAVNLK---------------LPEDE--------------------VRKRVDNALKRTGIEHL-KDK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 173 STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHD 232
Cdd:PRK13636 138 PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVseimKLLVEMQKELGLTIIIATHD 201
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-233 |
1.22e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 2 AHPPHSPATPNTAAHIRVSGIS-ASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGL--------RAPDAGE 72
Cdd:COG4178 348 LPEAASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 73 V-----RA-VGLGDpLRVGLLYqepPFAPHDTVAQAVESAVRTVR--DAASAVDRTADalarapedegaatayaaaldta 144
Cdd:COG4178 428 VlflpqRPyLPLGT-LREALLY---PATAEAFSDAELREALEAVGlgHLAERLDEEAD---------------------- 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 145 erigaWDvdtRIdvtldglglggvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSW-- 222
Cdd:COG4178 482 -----WD---QV--------------------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElp 533
|
250
....*....|....*....
gi 1586061923 223 --------HGPVLLASHDR 233
Cdd:COG4178 534 gttvisvgHRSTLAAFHDR 552
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
390-559 |
1.62e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 390 LTASAAEVAGRMAPVSLTVSAGESWLITGSNGVGKSTLLSLFArRLEPTRGSVH-----------AAPGVRVGLLDQDAT 458
Cdd:COG4138 1 LQLNDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMA-GLLPGQGEILlngrplsdwsaAELARHRAYLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 459 LPGADP--EHTAAHIYHELVGEDRAETVplgtfGLLAGRDE-----NRRVGELSVG--QRRRLALAVLLADP---PH--V 524
Cdd:COG4138 80 PPFAMPvfQYLALHQPAGASSEAVEQLL-----AQLAEALGledklSRPLTQLSGGewQRVRLAAVLLQVWPtinPEgqL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586061923 525 LLLDEPTNhfSLVLATQ-----LEAAVPDYPGTVLVASHD 559
Cdd:COG4138 155 LLLDEPMN--SLDVAQQaaldrLLRELCQQGITVVMSSHD 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-220 |
1.67e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 12 NTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---------LGDPL 82
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhkLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 RVGLLYQEppfaphdtvaqavesavRTVRDAASAVDRTadALARAPedegaatayaaaldTAERIGAWDVD-----TRID 157
Cdd:PRK09700 81 GIGIIYQE-----------------LSVIDELTVLENL--YIGRHL--------------TKKVCGVNIIDwremrVRAA 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 158 VTLDGLGLgGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:PRK09700 128 MMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMN 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
403-560 |
1.71e-12 |
|
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: 66.77 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR-VGLLDQDATL-------------- 459
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtGVPPERRnIGMVFQDYALfphltvaeniafgl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 460 ----PGADPEHTAAHIYHELVGEDRaetvplgtfgllagrDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFS 535
Cdd:cd03259 98 klrgVPKAEIRARVRELLELVGLEG---------------LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180
....*....|....*....|....*....
gi 1586061923 536 LVLATQLEAAVPDYPG----TVLVASHDR 560
Cdd:cd03259 163 AKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
404-559 |
2.22e-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: 66.76 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGV---------------RVGLLDQDATLPG------- 461
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEdisglseaelyrlrrRMGMLFQSGALFDsltvfen 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 462 -ADP--EHTA--AHIYHELVGEDraetvpLGTFGLLAgrDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSL 536
Cdd:cd03261 98 vAFPlrEHTRlsEEEIREIVLEK------LEAVGLRG--AEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180
....*....|....*....|....*..
gi 1586061923 537 VLATQLEAAVPD----YPGTVLVASHD 559
Cdd:cd03261 170 IASGVIDDLIRSlkkeLGLTSIMVTHD 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-208 |
2.41e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.45 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGLGDPL----------RVGLLYQEPpfaPHDTVAQ 101
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI--IIDGDLLteenvwdirhKIGMVFQNP---DNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 AVEsavrtvrdaasavdrtaDALARAPEDEGaatayaaaldtaerIGAWDVDTRIDVTLDGLGLGGVdRDRSTGALSGGQ 181
Cdd:PRK13650 98 TVE-----------------DDVAFGLENKG--------------IPHEEMKERVNEALELVGMQDF-KEREPARLSGGQ 145
|
170 180
....*....|....*....|....*..
gi 1586061923 182 RSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
404-558 |
2.46e-12 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 69.89 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGV---RVGLLDQDATL------------- 459
Cdd:TIGR03375 484 VSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlldgvdirQIDPADlrrNIGYVPQDPRLfygtlrdnialga 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 460 PGADPEhtaahiyhELVgeDRAETVPLGTF--GLLAGRDenRRVGE----LSVGQRRRLALA-VLLADPPhVLLLDEPTN 532
Cdd:TIGR03375 564 PYADDE--------EIL--RAAELAGVTEFvrRHPDGLD--MQIGErgrsLSGGQRQAVALArALLRDPP-ILLLDEPTS 630
|
170 180
....*....|....*....|....*...
gi 1586061923 533 HFSLVLATQLEAAVPDYPG--TVLVASH 558
Cdd:TIGR03375 631 AMDNRSEERFKDRLKRWLAgkTLVLVTH 658
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-213 |
2.65e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY--GSHRV--LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG-----LGDP-LR--- 83
Cdd:PRK11153 2 IELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltaLSEKeLRkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 --VGLLYQeppfapH----------DTVAQAVEsavrtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawd 151
Cdd:PRK11153 82 rqIGMIFQ------HfnllssrtvfDNVALPLE-------------------LAGTPKAE-------------------- 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 152 VDTRIDVTLDGLGLGgvD-RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD 213
Cdd:PRK11153 117 IKARVTELLELVGLS--DkADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR 177
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
404-559 |
4.08e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.26 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH-----AAP-GVRVGLldqdatlpgaDPEHTA-------AH 470
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvSALlELGAGF----------HPELTGreniylnGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 471 IYhelvGEDRAET---VP-------LGTFgllagrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEptnhfslVLAT 540
Cdd:COG1134 115 LL----GLSRKEIdekFDeivefaeLGDF-------IDQPVKTYSSGMRARLAFAVATAVDPDILLVDE-------VLAV 176
|
170 180 190
....*....|....*....|....*....|....
gi 1586061923 541 -----Q----------LEAAvpdypGTVLVASHD 559
Cdd:COG1134 177 gdaafQkkclarirelRESG-----RTVIFVSHS 205
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
32-232 |
4.20e-12 |
|
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: 65.95 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDPLRVgLLYQEPPFAPHDTVAQAVesav 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVilegKQITEPGPDRM-VVFQNYSLLPWLTVRENI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 108 rtvrdaASAVDRtadALARAPEDEgaatayaaaldtAERIgawdvdtrIDVTLDGLGLGGVdRDRSTGALSGGQRSRLSL 187
Cdd:TIGR01184 76 ------ALAVDR---VLPDLSKSE------------RRAI--------VEEHIALVGLTEA-ADKRPGQLSGGMKQRVAI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 188 AWLLLSTPDVLLLDEPTNHLDDAATDFLRATL-RSW--HGP-VLLASHD 232
Cdd:TIGR01184 126 ARALSIRPKVLLLDEPFGALDALTRGNLQEELmQIWeeHRVtVLMVTHD 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
31-208 |
5.04e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 66.64 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVglGDPLR------------VGLLYQEPP---FAP 95
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK--GEPIKydkksllevrktVGIVFQNPDdqlFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 hdTVAQAVesavrtvrdaasavdrtadalARAPEDEGAATAyaaaldtaerigawDVDTRIDVTLDGLGLGGVDRdRSTG 175
Cdd:PRK13639 95 --TVEEDV---------------------AFGPLNLGLSKE--------------EVEKRVKEALKAVGMEGFEN-KPPH 136
|
170 180 190
....*....|....*....|....*....|...
gi 1586061923 176 ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13639 137 HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
404-559 |
5.04e-12 |
|
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: 65.63 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVrVGLLDQDAtlpGADPEHTA---AHIYHELVGEDR 480
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-SSLLGLGG---GFNPELTGrenIYLNGRLLGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 481 AETVP----------LGTFGllagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT----NHFSL----VLATQL 542
Cdd:cd03220 117 KEIDEkideiiefseLGDFI-------DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEkcqrRLRELL 189
|
170
....*....|....*..
gi 1586061923 543 EAAvpdypGTVLVASHD 559
Cdd:cd03220 190 KQG-----KTVILVSHD 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-208 |
5.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.69 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG----------DPLR--VGLLYQEPPfaphd 97
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdiKQIRkkVGLVFQFPE----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 98 tvAQAVESAVrtVRDAA------SAVDRTADALARapedegaatayaaaldtaerigawdvdtridvtlDGLGLGGVD-- 169
Cdd:PRK13649 96 --SQLFEETV--LKDVAfgpqnfGVSQEEAEALAR----------------------------------EKLALVGISes 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586061923 170 -RDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13649 138 lFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
404-558 |
5.56e-12 |
|
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: 65.21 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQDAT-------LPGADPEHTAA---HIYH 473
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARgllylghAPGIKTTLSVLenlRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 474 ELVGEDRAETVpLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHF---SLVLATQLEAAVPDYP 550
Cdd:cd03231 99 ADHSDEQVEEA-LARVGL--NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALdkaGVARFAEAMAGHCARG 175
|
....*...
gi 1586061923 551 GTVLVASH 558
Cdd:cd03231 176 GMVVLTTH 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-204 |
5.78e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlGDplrvgllyqeppfaph 96
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG-GD---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 dtVAQAVEsavrtvRDAASAvdRTA--------------------DALARapedegaatayAAALDTAERigawdvDTRI 156
Cdd:NF033858 65 --MADARH------RRAVCP--RIAympqglgknlyptlsvfenlDFFGR-----------LFGQDAAER------RRRI 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1586061923 157 DVTLDGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPT 204
Cdd:NF033858 118 DELLRATGLAPF-ADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
404-560 |
5.87e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.46 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAA------------PGVR--VGLLDQDATLpgadpehtaa 469
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlkrreiPYLRrrIGVVFQDFRL---------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 hIYH-----------ELVGEDRAET---VP--LGTFGlLAGRdENRRVGELSVGQRRRLALA-VLLADPPhVLLLDEPTN 532
Cdd:COG2884 91 -LPDrtvyenvalplRVTGKSRKEIrrrVRevLDLVG-LSDK-AKALPHELSGGEQQRVAIArALVNRPE-LLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586061923 533 HFSLVLATQL--------EAAVpdypgTVLVASHDR 560
Cdd:COG2884 167 NLDPETSWEImelleeinRRGT-----TVLIATHDL 197
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
37-234 |
6.04e-12 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 65.64 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 37 FSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDP---LRVGLLYQEPPFA---PHDtVAQAVESAvRTV 110
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGkgwRHIGYVPQRHEFAwdfPIS-VAHTVMSG-RTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 111 RDAASAVDRTADALArapedegaatayaaaldtaerigawdvdtrIDVTLDGLGLGGVdRDRSTGALSGGQRSRLSLAWL 190
Cdd:TIGR03771 79 HIGWLRRPCVADFAA------------------------------VRDALRRVGLTEL-ADRPVGELSGGQRQRVLVARA 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586061923 191 LLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG---PVLLASHDRA 234
Cdd:TIGR03771 128 LATRPSVLLLDEPFTGLDMPTQELLTELFIELAGagtAILMTTHDLA 174
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
403-531 |
6.73e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 65.22 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------------HAAPGVRVGLLDQDatlPGA--DPEH 466
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrrlRKIRRKEIQMVFQD---PMSslNPRM 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 467 TAAHI--------YHELVGEDRAETVPLGTFGL-LAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03257 100 TIGEQiaeplrihGKLSKKEARKEAVLLLLVGVgLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPT 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
405-559 |
7.39e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.16 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR-VGLLDQDATL---------------P 460
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdltALPPAERpVSMLFQENNLfphltvaqniglglrP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 461 G---ADPEHTAAhiyhelvgEDRAETVPLGTFgllagrdENRRVGELSVGQRRRLALA-VLLADPPhVLLLDEPtnhFS- 535
Cdd:COG3840 99 GlklTAEQRAQV--------EQALERVGLAGL-------LDRLPGQLSGGQRQRVALArCLVRKRP-ILLLDEP---FSa 159
|
170 180 190
....*....|....*....|....*....|...
gi 1586061923 536 ---------LVLATQLEAavpDYPGTVLVASHD 559
Cdd:COG3840 160 ldpalrqemLDLVDELCR---ERGLTVLMVTHD 189
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-233 |
8.70e-12 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 66.36 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 47 LIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLR------VGLLYQEPPFAPHDTVAQAVESAVRTVRDAASAVD-R 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphlrhINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKpR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 120 TADALARapedegaatayaaaldtaerigawdvdtridVTLDGLGlggvdrDRSTGALSGGQRSRLSLAWLLLSTPDVLL 199
Cdd:TIGR01187 81 VLEALRL-------------------------------VQLEEFA------DRKPHQLSGGQQQRVALARALVFKPKILL 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 1586061923 200 LDEPTNHLDDAATDFLRATLRSWHGPV----LLASHDR 233
Cdd:TIGR01187 124 LDEPLSALDKKLRDQMQLELKTIQEQLgitfVFVTHDQ 161
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
404-531 |
9.57e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.50 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGV---RVGLLDQDATL------------- 459
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirDLTLESlrrQIGVVPQDTFLfsgtirenirygr 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 460 PGADPEH-----TAAHIyHELVgedraETVPLG--TfgllagrdenrRVGE----LSVGQRRRLALA-VLLADPPhVLLL 527
Cdd:COG1132 439 PDATDEEveeaaKAAQA-HEFI-----EALPDGydT-----------VVGErgvnLSGGQRQRIAIArALLKDPP-ILIL 500
|
....
gi 1586061923 528 DEPT 531
Cdd:COG1132 501 DEAT 504
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-212 |
1.09e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 26 YGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRA--PDA---GEVRAVGLG------DPL----RVGLLYQE 90
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNiyspdvDPIevrrEVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 P-PFaPHDTVAQAVESAVRTvrdaasavdrtaDALARAPEDegaatayaaaldtaerigawdVDTRIDVTLDGLGLGGVD 169
Cdd:PRK14267 94 PnPF-PHLTIYDNVAIGVKL------------NGLVKSKKE---------------------LDERVEWALKKAALWDEV 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 170 RDR---STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:PRK14267 140 KDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-232 |
1.25e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgDPLRvgllyqeppfaphdtvaqavesavrt 109
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VPFK-------------------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 110 vrdaasavDRTadALARapedegaatayaaaldtaeRIGA---------WDV----------------DTRIDVTLD--- 161
Cdd:COG4586 89 --------RRK--EFAR-------------------RIGVvfgqrsqlwWDLpaidsfrllkaiyripDAEYKKRLDelv 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 162 -GLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHD 232
Cdd:COG4586 140 eLLDLGEL-LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKeairEFLKEYNRERGTTILLTSHD 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-236 |
1.28e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrvgllyqeppFAP 95
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW------------------FSG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 HDtVAQAVESAVRTVR--------DAASAVDRTA-DALARAPEDEGAATAyaaaldtaerigawDVDTRIDVTLDGLGLg 166
Cdd:PRK10908 64 HD-ITRLKNREVPFLRrqigmifqDHHLLMDRTVyDNVAIPLIIAGASGD--------------DIRRRVSAALDKVGL- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 167 gVDRDRSTG-ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG---PVLLASHDRAFL 236
Cdd:PRK10908 128 -LDKAKNFPiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLI 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-213 |
1.29e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG----DPLR--VGLLYQE 90
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshvPPYQrpINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 PPFAPHDTVAQAVesavrtvrdaasAVDRTADALARApedegaatayaaaldtaerigawDVDTRIDVTLDGLGLGGVDR 170
Cdd:PRK11607 100 YALFPHMTVEQNI------------AFGLKQDKLPKA-----------------------EIASRVNEMLGLVHMQEFAK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586061923 171 dRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD 213
Cdd:PRK11607 145 -RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
395-530 |
1.55e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.72 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 395 AEVAGR--MAPVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------AAPGVRVGLLDQ-DATLPGADPE 465
Cdd:PRK11248 9 ADYGGKpaLEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvEGPGAERGVVFQnEGLLPWRNVQ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 466 HTAAhIYHELVGEDRAETVPLGTFGL----LAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK11248 89 DNVA-FGLQLAGVEKMQRLEIAHQMLkkvgLEGA-EKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
18-204 |
1.67e-11 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 64.08 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---LGDP----LRVGLLY-- 88
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGediTKLPpherARAGIAYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 QEPPFAPHDTVAQAVESAVRTVRDAASAVDrtADALARAPedegaatayaaaldtaerigawdvdtridVTLDGlglggv 168
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIP--DEIYELFP-----------------------------VLKEM------ 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586061923 169 dRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPT 204
Cdd:TIGR03410 125 -LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-212 |
1.77e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.55 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGL-----RAPDAGEVRAVG---LGDPL---- 82
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGqdiFKMDVielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 -RVGLLYQEPPFAPHDTVAQAVESAV---RTVRDAASAVDRTADALARAPedegaatayaaaldtaerigAWD-VDTRID 157
Cdd:PRK14247 82 rRVQMVFQIPNPIPNLSIFENVALGLklnRLVKSKKELQERVRWALEKAQ--------------------LWDeVKDRLD 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 158 VtldglglggvdrdrSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:PRK14247 142 A--------------PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENT 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-208 |
1.78e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 8 PATPNTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAG--LRAPDAGEVRavglgdpLRVG 85
Cdd:COG2401 22 DLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVD-------VPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPP----FAPHDTVAQAVEsavrtvrdAASAVDRTADALARAPEDEgaatayaaaldtaerigawdvdtridvtld 161
Cdd:COG2401 95 QFGREASlidaIGRKGDFKDAVE--------LLNAVGLSDAVLWLRRFKE------------------------------ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586061923 162 glglggvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG2401 137 ---------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-101 |
1.88e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---------LGDPLRVGLL 87
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarltpaKAHQLGIYLV 91
|
90
....*....|....
gi 1586061923 88 YQEPPFAPHDTVAQ 101
Cdd:PRK15439 92 PQEPLLFPNLSVKE 105
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-208 |
2.06e-11 |
|
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: 66.36 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY-----GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVrAVGLGD----------P 81
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV-NVRVGDewvdmtkpgpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 82 LR------VGLLYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADALARAPEDEgaatayaaalDTAERIgawdvdtr 155
Cdd:TIGR03269 359 GRgrakryIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDE----------EKAEEI-------- 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 156 idvtldglglggvdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:TIGR03269 421 --------------LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
404-559 |
2.24e-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: 63.89 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGV----------RVGL-LDQDATL----PGADPEHTA 468
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkflrRIGVvFGQKTQLwwdlPVIDSFYLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 AHIYH---ELVGEDRAETVPLgtfgLLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTnhFSLVLATQ---- 541
Cdd:cd03267 120 AAIYDlppARFKKRLDELSEL----LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT--IGLDVVAQenir 193
|
170 180
....*....|....*....|
gi 1586061923 542 --LEAAVPDYPGTVLVASHD 559
Cdd:cd03267 194 nfLKEYNRERGTTVLLTSHY 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
31-210 |
2.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.82 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGE-----VRAVGLGDPL------RVGLLYQEP--PFAP-- 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitVDGITLTAKTvwdireKVGIVFQNPdnQFVGat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 -HDTVAQAVES-------AVRTVRDAASAVDrTADALARAPEDegaatayaaaldtaerigawdvdtridvtldglglgg 167
Cdd:PRK13640 102 vGDDVAFGLENravprpeMIKIVRDVLADVG-MLDYIDSEPAN------------------------------------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586061923 168 vdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDA 210
Cdd:PRK13640 144 ---------LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
404-574 |
2.43e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 63.58 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV------------HAAPGVR--VGLLDQDATLpgadpehtaa 469
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgRAIPYLRrkIGVVFQDFRL---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 hIYHELVGEDRAetVPLGTFGlLAGRDENRRV-----------------GELSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:cd03292 90 -LPDRNVYENVA--FALEVTG-VPPREIRKRVpaalelvglshkhralpAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586061923 533 HFSLVLATQ---LEAAVPDYPGTVLVASHDRWLRRNWTGRDLALE 574
Cdd:cd03292 166 NLDPDTTWEimnLLKKINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
381-530 |
2.44e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 381 AALHRTGPVLTASAAEVAGRMAPV----SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----HAAPGVRVG 451
Cdd:PRK13543 3 EPLHTAPPLLAAHALAFSRNEEPVfgplDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgkTATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 452 LLDQDATLPGADPEHTAAHIYHELVGED--RAETVPLGTFGLLAGRD-ENRRVGELSVGQRRRLALAVLLADPPHVLLLD 528
Cdd:PRK13543 83 FMAYLGHLPGLKADLSTLENLHFLCGLHgrRAKQMPGSALAIVGLAGyEDTLVRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
..
gi 1586061923 529 EP 530
Cdd:PRK13543 163 EP 164
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-208 |
2.50e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.72 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 28 SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPL---------RVGLLYQEPpfaPHDT 98
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlwdirnKAGMVFQNP---DNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 VAQAVESAVrtvrdaasavdrtadalARAPEDEGaatayaaaldtaerIGAWDVDTRIDVTLDGLGLGGVdRDRSTGALS 178
Cdd:PRK13633 99 VATIVEEDV-----------------AFGPENLG--------------IPPEEIRERVDESLKKVGMYEY-RRHAPHLLS 146
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-231 |
2.50e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 4 PPHSPATPNTAAHIRVSGISASYGSH---RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVravgL-- 78
Cdd:TIGR00958 466 LTGTLAPLNLEGLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV----Lld 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 79 GDPLR----------VGLLYQEPpfaphdtvaqavesavrtVRDAASAVDRTADALARAPEDEgaatayaaALDTAERIG 148
Cdd:TIGR00958 542 GVPLVqydhhylhrqVALVGQEP------------------VLFSGSVRENIAYGLTDTPDEE--------IMAAAKAAN 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 149 AWDVDTRIDVTLDglglggVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAATDFLRATLRSWHG-PVL 227
Cdd:TIGR00958 596 AHDFIMEFPNGYD------TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL-DAECEQLLQESRSRASrTVL 668
|
....
gi 1586061923 228 LASH 231
Cdd:TIGR00958 669 LIAH 672
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
36-210 |
2.64e-11 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 63.34 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 36 SFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGD----PLR--VGLLYQEPPFAPHDTVAQAVESAVRT 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHtglaPYQrpVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 110 VRDAASAVDRTADALARApedegaatayaaaldtaerigawdvdtridvtldgLGLGGVdRDRSTGALSGGQRSRLSLAW 189
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQ-----------------------------------VGIADY-LDRLPEQLSGGQRQRVALAR 141
|
170 180
....*....|....*....|.
gi 1586061923 190 LLLSTPDVLLLDEPTNHLDDA 210
Cdd:TIGR01277 142 CLVRPNPILLLDEPFSALDPL 162
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-208 |
3.43e-11 |
|
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: 63.40 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHR-VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAG-------EVRAVGLgDPLR--VGL 86
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGsilidgqDIREVTL-DSLRraIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPP-FapHDTVA--------QAVESAVRTVRDAAsavdRTADALARAPEdegaatayaaaldtaerigawDVDTRid 157
Cdd:cd03253 80 VPQDTVlF--NDTIGynirygrpDATDEEVIEAAKAA----QIHDKIMRFPD---------------------GYDTI-- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 158 vtldgLGLGGVdrdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03253 131 -----VGERGL-------KLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
397-559 |
4.37e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 397 VAGRMAPVSLTVSAGESWLITGSNGVGKSTLLSLFARRLePTRGSVHaapgvrvgLLDQD-ATLPGADPEH--------- 466
Cdd:PRK03695 8 VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQ--------FAGQPlEAWSAAELARhraylsqqq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 467 ---TAAHIYHEL---VGEDRAETVPLGTFGLLAGR----DE-NRRVGELSVG--QRRRLALAVLLADP---PH--VLLLD 528
Cdd:PRK03695 79 tppFAMPVFQYLtlhQPDKTRTEAVASALNEVAEAlgldDKlGRSVNQLSGGewQRVRLAAVVLQVWPdinPAgqLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586061923 529 EPTNhfSLVLATQ-----LEAAVPDYPGTVLVASHD 559
Cdd:PRK03695 159 EPMN--SLDVAQQaaldrLLSELCQQGIAVVMSSHD 192
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
404-531 |
4.52e-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: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-------HAAPGVR---VGLLDQdatlpgadpehtAAHIYH 473
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvSDLEKALsslISVLNQ------------RPYLFD 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 474 ELVGEDraetvpLGTfgllagrdenrrvgELSVGQRRRLALA-VLLADPPhVLLLDEPT 531
Cdd:cd03247 89 TTLRNN------LGR--------------RFSGGERQRLALArILLQDAP-IVLLDEPT 126
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
404-559 |
4.53e-11 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 61.82 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgvrvgLLDQD-ATLPGADPEHtaahiyhelvgeDRAE 482
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL--------IDGEDlTDLEDELPPL------------RRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 483 TVPLGTFGLLAGRD--ENRRVGeLSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEA---AVPDYPG-TVLVA 556
Cdd:cd03229 79 GMVFQDFALFPHLTvlENIALG-LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRAllkSLQAQLGiTVVLV 157
|
...
gi 1586061923 557 SHD 559
Cdd:cd03229 158 THD 160
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
403-559 |
4.76e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGEswlIT---GSNGVGKSTLLSLFARRLEPTRGSVH-------AAPGV----RVGLLDQDatlpgadpEHTA 468
Cdd:COG4604 19 DVSLTIPKGG---ITaliGPNGAGKSTLLSMISRLLPPDSGEVLvdgldvaTTPSRelakRLAILRQE--------NHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 AHI-YHELVG-------------EDRA---ETvpLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:COG4604 88 SRLtVRELVAfgrfpyskgrltaEDREiidEA--IAYLDLEDLAD--RYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPL 163
|
170 180 190
....*....|....*....|....*....|..
gi 1586061923 532 N----HFSLVLATQLEAAVPDYPGTVLVASHD 559
Cdd:COG4604 164 NnldmKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
404-558 |
6.04e-11 |
|
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: 62.30 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH-------AAPGVRVGLLDQD----------------ATLP 460
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEErglypkmkvidqlvylAQLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 461 GADPEHTAAHIyhelvgEDRAETVPLGTFgllagrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLAT 540
Cdd:cd03269 99 GLKKEEARRRI------DEWLERLELSEY-------ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180
....*....|....*....|.
gi 1586061923 541 QLEAAVPDYPG---TVLVASH 558
Cdd:cd03269 166 LLKDVIRELARagkTVILSTH 186
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-231 |
6.79e-11 |
|
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: 62.49 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASYGS---HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGLGDPL---------- 82
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV--LLDGKPIsqyehkylhs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 RVGLLYQEPpfaphdtvaqavesavrtVRDAASAVDRTADALARAPedegaatayaaaldtAERIGAWDVDTRIDVTLDG 162
Cdd:cd03248 89 KVSLVGQEP------------------VLFARSLQDNIAYGLQSCS---------------FECVKEAAQKAHAHSFISE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 163 LGLG-GVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP--VLLASH 231
Cdd:cd03248 136 LASGyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERrtVLVIAH 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-208 |
7.82e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 64.71 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 27 GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLrAPDAGEVRAVG-----LGD----PLR--VGLLYQEPpFA- 94
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGqdldgLSRralrPLRrrMQVVFQDP-FGs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 --PHDTVAQAVESAVRTVRDAASAVDRTAdalarapedegaatayaaaldtaerigawdvdtRIDVTLDGLGLGGVDRDR 172
Cdd:COG4172 375 lsPRMTVGQIIAEGLRVHGPGLSAAERRA---------------------------------RVAEALEEVGLDPAARHR 421
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586061923 173 STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG4172 422 YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
404-531 |
8.18e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 62.29 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEP---TRGSVHAApGV---------RVGLLDQ-DATLPGADPEHTAAH 470
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFN-GQprkpdqfqkCVAYVRQdDILLPGLTVRETLTY 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 471 IYH--------ELVGEDRAETVPLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03234 105 TAIlrlprkssDAIRKKRVEDVLLRDLAL--TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-234 |
8.78e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrvgllYQEPPFAPHD 97
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-------------YRMRDGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 98 tVAQAVESAVRTVRdaasavdRTADALARAPEDEGAATAYAAALDTAERIGA--WDVDTRI-DVTLDGLGLGGVDRDR-- 172
Cdd:PRK11701 75 -LYALSEAERRRLL-------RTEWGFVHQHPRDGLRMQVSAGGNIGERLMAvgARHYGDIrATAGDWLERVEIDAARid 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 173 -STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHDRA 234
Cdd:PRK11701 147 dLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQarllDLLRGLVRELGLAVVIVTHDLA 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
403-531 |
8.99e-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: 61.83 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLItGSNGVGKSTLLSLFARRLEPTRGSVhAAPGV-----------RVGLLDQD--------------- 456
Cdd:cd03264 18 GVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTI-RIDGQdvlkqpqklrrRIGYLPQEfgvypnftvrefldy 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 457 -ATLPGADPEHTAAHIYHELvgedraETVPLGTFgllagrdENRRVGELSVGQRRRLALA-VLLADPPhVLLLDEPT 531
Cdd:cd03264 96 iAWLKGIPSKEVKARVDEVL------ELVNLGDR-------AKKKIGSLSGGMRRRVGIAqALVGDPS-ILIVDEPT 158
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-240 |
9.53e-11 |
|
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: 62.66 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVrAVGlGDPL--------------RVGLLYQEppFA--PHd 97
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV-LID-GQDIaamsrkelrelrrkKISMVFQS--FAllPH- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 98 tvaqavesavRTVRDAA------SAVDRtADALARAPEdegaatayaaaldtaerigawdvdtridvTLDGLGLGGvDRD 171
Cdd:cd03294 117 ----------RTVLENVafglevQGVPR-AEREERAAE-----------------------------ALELVGLEG-WEH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 172 RSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD-----DAATDFLRatLRSWHG-PVLLASHDrafLDTAV 240
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirrEMQDELLR--LQAELQkTIVFITHD---LDEAL 225
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
404-559 |
1.11e-10 |
|
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: 62.14 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPG-----------VRVGLLDQDA--------------- 457
Cdd:TIGR03873 20 VDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglsrraraRRVALVEQDSdtavpltvrdvvalg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 458 -----TLPGADPEHTAAHIYHELVgedRAETVPLGTfgllagrdenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:TIGR03873 100 riphrSLWAGDSPHDAAVVDRALA---RTELSHLAD----------RDMSTLSGGERQRVHVARALAQEPKLLLLDEPTN 166
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 533 HFSLVLATQLEAAVPDYPG---TVLVASHD 559
Cdd:TIGR03873 167 HLDVRAQLETLALVRELAAtgvTVVAALHD 196
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
404-531 |
1.22e-10 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 61.82 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------------AAPGVR--VGLLDQDATLPgadPEHTAa 469
Cdd:cd03256 20 VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkALRQLRrqIGMIFQQFNLI---ERLSV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 hIYHELVGedRAETVPL--GTFGLLAGRD----------------ENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03256 96 -LENVLSG--RLGRRSTwrSLFGLFPKEEkqralaalervglldkAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-213 |
1.46e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.83 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 4 PPHSPATPNTAAHIRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG--- 79
Cdd:PRK13657 322 PPGAIDLGRVKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirt 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 80 ---DPLR--VGLLYQEPP-FAphdtvaqavesavRTVRDAASA--VDRTADALARApedegaatayaaaldtAERIGAWD 151
Cdd:PRK13657 402 vtrASLRrnIAVVFQDAGlFN-------------RSIEDNIRVgrPDATDEEMRAA----------------AERAQAHD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 152 VdtrIDVTLDGLGLGGVDRDRStgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLdDAATD 213
Cdd:PRK13657 453 F---IERKPDGYDTVVGERGRQ---LSGGERQRLAIARALLKDPPILILDEATSAL-DVETE 507
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
32-242 |
1.58e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.03 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG--------LGDPLRVGLLYQEPpfaPHDTVAQAV 103
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvWNLRRKIGMVFQNP---DNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 104 EsavrtvrdaasavdrtaDALARAPEDEGaatayaaaldtaerIGAWDVDTRIDVTLdgLGLGGVD-RDRSTGALSGGQR 182
Cdd:PRK13642 100 E-----------------DDVAFGMENQG--------------IPREEMIKRVDEAL--LAVNMLDfKTREPARLSGGQK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 183 SRLSLAWLLLSTPDVLLLDEPTNHLDDAA-TDFLRATLR---SWHGPVLLASHDrafLDTAVTS 242
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGrQEIMRVIHEikeKYQLTVLSITHD---LDEAASS 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
404-559 |
1.64e-10 |
|
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: 63.53 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDATLPGAD--------- 463
Cdd:TIGR02868 354 VSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldQDEVRRRVSVCAQDAHLFDTTvrenlrlar 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 464 PEHTAAHIYHELvgedraETVPLGTfgLLAGRDE--NRRVGE----LSVGQRRRLALA-VLLADPPhVLLLDEPTNHFSL 536
Cdd:TIGR02868 434 PDATDEELWAAL------ERVGLAD--WLRALPDglDTVLGEggarLSGGERQRLALArALLADAP-ILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*
gi 1586061923 537 VLATQLEAAV--PDYPGTVLVASHD 559
Cdd:TIGR02868 505 ETADELLEDLlaALSGRTVVLITHH 529
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
31-213 |
1.68e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGLGDPL--------------RVGLLYQEPPFAPH 96
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV--IFNGQPMsklssaakaelrnqKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTvaqAVESAVRTVRDAASavdRTADALARAPEdegaatayaaaldtaerigawdvdtridvTLDGLGLGGVDRDRSTgA 176
Cdd:PRK11629 102 FT---ALENVAMPLLIGKK---KPAEINSRALE-----------------------------MLAAVGLEHRANHRPS-E 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD 213
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
404-531 |
1.93e-10 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 61.15 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-------HAAPG---VRVGLLDQDATLpgaDPEHTAA---H 470
Cdd:TIGR03864 20 VSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQIsvaghdlRRAPRaalARLGVVFQQPTL---DLDLSVRqnlR 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 471 IYHELVGEDRAETVP-----LGTFGLLAGRDEnrRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:TIGR03864 97 YHAALHGLSRAEARAriaelLARLGLAERADD--KVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
405-535 |
2.01e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.14 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR-VGLLDQDATL-----------PGADP 464
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqdhtTTPPSRRpVSMLFQENNLfshltvaqnigLGLNP 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 465 EHTAAHIYHELVgEDRAETVPLGTFgllagrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPtnhFS 535
Cdd:PRK10771 99 GLKLNAAQREKL-HAIARQMGIEDL-------LARLPGQLSGGQRQRVALARCLVREQPILLLDEP---FS 158
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
36-210 |
2.33e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.75 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 36 SFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG----LGDPLR--VGLLYQEPPFAPHDTVAQAV------ 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtTTPPSRrpVSMLFQENNLFSHLTVAQNIglglnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 104 -----ESAVRTVRDAASAVdRTADALARAPedegaatayaaaldtaerigawdvdtridvtldglglggvdrdrstGALS 178
Cdd:PRK10771 99 glklnAAQREKLHAIARQM-GIEDLLARLP----------------------------------------------GQLS 131
|
170 180 190
....*....|....*....|....*....|..
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDA 210
Cdd:PRK10771 132 GGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-249 |
2.34e-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: 60.91 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHR-------VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLrvgllyq 89
Cdd:COG4778 5 LEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWV------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 90 eppfaphdTVAQAVESAVRTVRDAA--------------SAVDRTADALARAPEDEGAATayaaaldtaERIGAWdvdtr 155
Cdd:COG4778 78 --------DLAQASPREILALRRRTigyvsqflrviprvSALDVVAEPLLERGVDREEAR---------ARAREL----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 156 idvtLDGLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSwhGPVLLA-S 230
Cdd:COG4778 136 ----LARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKAR--GTAIIGiF 209
|
250
....*....|....*....
gi 1586061923 231 HDRAFLDTAVTSLVDLDPA 249
Cdd:COG4778 210 HDEEVREAVADRVVDVTPF 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-232 |
2.34e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.95 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL--------------RVGLLYQEPPFAPH 96
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL--VGQPLhqmdeearaklrakHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVAQAVEsavrtvrdaasavdrtADALARAPEDegaatayaaaldTAERIGAWDVdtridvtLDGLGLGgvDR-DRSTG 175
Cdd:PRK10584 103 LNALENVE----------------LPALLRGESS------------RQSRNGAKAL-------LEQLGLG--KRlDHLPA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 176 ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD----DAATDFLRATLRSWHGPVLLASHD 232
Cdd:PRK10584 146 QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtgDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
405-558 |
2.51e-10 |
|
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: 60.58 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR-VGLLDQDATLpgadpehtAAHIYHE- 474
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvtAAPPADRpVSMLFQENNL--------FAHLTVEq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 475 -----------LVGEDR-AETVPLGTFGLlaGRDENRRVGELSVGQRRRLALA-VLLADPPhVLLLDEPTNHFSLVLATQ 541
Cdd:cd03298 90 nvglglspglkLTAEDRqAIEVALARVGL--AGLEKRLPGELSGGERQRVALArVLVRDKP-VLLLDEPFAALDPALRAE 166
|
170 180
....*....|....*....|.
gi 1586061923 542 LEAAVPDYPG----TVLVASH 558
Cdd:cd03298 167 MLDLVLDLHAetkmTVLMVTH 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-211 |
2.94e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.31 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGE-------VRAVGLGDpLR--VGLLYQEPPfaphdtvAQA 102
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifynnqaITDDNFEK-LRkhIGIVFQNPD-------NQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 103 VESAVRTvrDAASAVDRTAdalarAPEDEgaatayaaaldtAERIGAwDVDTRIDVTldglglggVDRDRSTGALSGGQR 182
Cdd:PRK13648 97 VGSIVKY--DVAFGLENHA-----VPYDE------------MHRRVS-EALKQVDML--------ERADYEPNALSGGQK 148
|
170 180
....*....|....*....|....*....
gi 1586061923 183 SRLSLAWLLLSTPDVLLLDEPTNHLDDAA 211
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-212 |
3.04e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.95 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 12 NTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLR-------IVAGLRAP---------------D 69
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVEgkvtfhgknlyapdvD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 70 AGEVRAvglgdplRVGLLYQEP-PFAP--HDTVAQAV----------ESAVRTVRDAAsavdrtadalarapedegaata 136
Cdd:PRK14243 86 PVEVRR-------RIGMVFQKPnPFPKsiYDNIAYGAringykgdmdELVERSLRQAA---------------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 137 yaaaldtaerigAWDvdtriDVTldglglggvDRDRSTG-ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:PRK14243 137 ------------LWD-----EVK---------DKLKQSGlSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIST 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-208 |
3.19e-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: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDP--LR--VGLLYQEPPFAPhdtvaqa 102
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdgHDLALADPawLRrqVGVVLQENVLFN------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 103 vesavRTVRDAASAVDrTADALARAPEdegaatayaaaldTAERIGAWDVDTRIDvtldgLGLGGVDRDRSTGaLSGGQR 182
Cdd:cd03252 90 -----RSIRDNIALAD-PGMSMERVIE-------------AAKLAGAHDFISELP-----EGYDTIVGEQGAG-LSGGQR 144
|
170 180
....*....|....*....|....*.
gi 1586061923 183 SRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALD 170
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
27-232 |
3.53e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 27 GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGLGDPLR----------VGLLYQEPP---F 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV--LIRGEPITkenirevrkfVGLVFQNPDdqiF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 94 APhdTVAQAVesavrtvrdaasavdrtadalARAPEDEGAATAYaaaldtaerigawdVDTRIDVTLDGLGLGGVdRDRS 173
Cdd:PRK13652 93 SP--TVEQDI---------------------AFGPINLGLDEET--------------VAHRVSSALHMLGLEEL-RDRV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 174 TGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD----DAATDFLRATLRSWHGPVLLASHD 232
Cdd:PRK13652 135 PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETYGMTVIFSTHQ 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-533 |
3.73e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 42 GDPTGLIGENGSGKSTLLRIVAGLRAPDagevravgLGDplrvgllYQEPP--------FAP---HDTVAQAVESAVRTV 110
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPN--------LGD-------YEEEPswdevlkrFRGtelQNYFKKLYNGEIKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 111 R-----DAASAV--DRTADALARApeDEgaatayaaaldtaerIGAWDvdtriDVtLDGLGLGGVdRDRSTGALSGGQRS 183
Cdd:PRK13409 164 HkpqyvDLIPKVfkGKVRELLKKV--DE---------------RGKLD-----EV-VERLGLENI-LDRDISELSGGELQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 184 RLSLAWLLLSTPDVLLLDEPTNHLD-----DAAtDFLRATLRSwhGPVLLASHDRAFLDtavtslvdldpaprphaVTSD 258
Cdd:PRK13409 220 RVAIAAALLRDADFYFFDEPTSYLDirqrlNVA-RLIRELAEG--KYVLVVEHDLAVLD-----------------YLAD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 259 LV----GDGTGTGIgVTRFGGTYS---QYV---LARMDTRerwertYRDEQAQLKKLraAVREQQTvghsgRSPKTEGRA 328
Cdd:PRK13409 280 NVhiayGEPGAYGV-VSKPKGVRVginEYLkgyLPEENMR------IRPEPIEFEER--PPRDESE-----RETLVEYPD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 329 AKKFYADrnatvvsrrvngarARLaTVEDEQIRKpprelyfqgltaglsgseaalhrtgpvltasaAEVAGrmapvsltv 408
Cdd:PRK13409 346 LTKKLGD--------------FSL-EVEGGEIYE--------------------------------GEVIG--------- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 409 sageswlITGSNGVGKSTLLSLFARRLEPTRGSVHAApgVRVG------LLDQDAT----LPGADPEHTAAHIYHELVge 478
Cdd:PRK13409 370 -------IVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKISykpqyiKPDYDGTvedlLRSITDDLGSSYYKSEII-- 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 479 draetVPLGTFGLLagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNH 533
Cdd:PRK13409 439 -----KPLQLERLL-----DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
404-531 |
3.98e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.87 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgvrvgLLDQDATlpgADPEH----------------T 467
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL--------IDGKDVT---KLPEYkrakyigrvfqdpmmgT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 468 AAHIYHE---LVGEDRAETVPLGtFGLLAGRD--------------ENR---RVGELSVGQRRrlALAVLLA--DPPHVL 525
Cdd:COG1101 94 APSMTIEenlALAYRRGKRRGLR-RGLTKKRRelfrellatlglglENRldtKVGLLSGGQRQ--ALSLLMAtlTKPKLL 170
|
....*.
gi 1586061923 526 LLDEPT 531
Cdd:COG1101 171 LLDEHT 176
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-219 |
4.01e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAglRAPD-------AGEVRAVG--LGDP-- 81
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN--RMNDlnpevtiTGSIVYNGhnIYSPrt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 82 ----LR--VGLLYQEP---PFAPHDTVAQAVEsaVRTVRDAASavdrtadalarapedegaatayaaaldtaerigawdV 152
Cdd:PRK14239 80 dtvdLRkeIGMVFQQPnpfPMSIYENVVYGLR--LKGIKDKQV------------------------------------L 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 153 DTRIDVTLDGLGLGGVDRDR---STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATL 219
Cdd:PRK14239 122 DEAVEKSLKGASIWDEVKDRlhdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-220 |
4.16e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 5 PHSPATPNTAAHIRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDaGEVRAVGLGDPl 82
Cdd:TIGR01271 1206 PHAQKCWPSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWN- 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 RVGLLYQEPPFAphdTVAQAVESAVRTVRdaasavdRTADALARAPEDEgaatayaaALDTAERIGAWDVDTRIDVTLD- 161
Cdd:TIGR01271 1284 SVTLQTWRKAFG---VIPQKVFIFSGTFR-------KNLDPYEQWSDEE--------IWKVAEEVGLKSVIEQFPDKLDf 1345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 162 GLGLGGVdrdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:TIGR01271 1346 VLVDGGY-------VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
402-531 |
4.42e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 402 APVSLTVSAGESWLITGSNGVGKSTLLSLFArRLEP-TRGSVHAAPGVRV-----------GLLDQDATLPGADPEHTAA 469
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIA-GLWPyGSGRIARPAGARVlflpqrpylplGTLREALLYPATAEAFSDA 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 470 HIYHELvgedraETVPLGTfglLAGR--DENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:COG4178 459 ELREAL------EAVGLGH---LAERldEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-208 |
5.34e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV--------RAVGLGDPLRV 84
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPPfAPHDTVAQAVESAVRTVRDAASAVDRT--ADALARAPEDEGAATayaaaldtaerIGAWDVDTridvtldg 162
Cdd:PRK10253 84 GLLAQNAT-TPGDITVQELVARGRYPHQPLFTRWRKedEEAVTKAMQATGITH-----------LADQSVDT-------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 163 lglggvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK10253 144 --------------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-208 |
5.42e-10 |
|
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: 59.93 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS-HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV-------RAVGLGDpLR--VGL 86
Cdd:cd03254 3 IEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidiRDISRKS-LRsmIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPPFAPhdtvaqavesavRTVRDAASAVDRTADAlarapEDEgaatayaaaLDTAERIGAWD-VDTRIDvtldglGL 165
Cdd:cd03254 82 VLQDTFLFS------------GTIMENIRLGRPNATD-----EEV---------IEAAKEAGAHDfIMKLPN------GY 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586061923 166 GGVDRDRSTGaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03254 130 DTVLGENGGN-LSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-208 |
6.15e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.39 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 10 TPNTAAHIRVSGISASYGSHR--VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL---GDPLR- 83
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItisKENLKe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 ----VGLLYQEPpfaphDTvaQAVESAVRtvrdaasavdrtaDALARAPEDegaatayaaaldtaERIGAWDVDTRIDVT 159
Cdd:PRK13632 81 irkkIGIIFQNP-----DN--QFIGATVE-------------DDIAFGLEN--------------KKVPPKKMKDIIDDL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 160 LDGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13632 127 AKKVGMEDY-LDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-208 |
6.24e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 59.73 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPT-----GLIGENGSGKSTLLRIVAGLRAPDAGEvravglgdplrvgllyqepPFAPHDTVA---QAV 103
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGD-------------------IEIELDTVSykpQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 104 ESAVR-TVRDAASavDRTADALARApedegaatayaaaldtaerigAWDVDTRIDVTLDGLglggvdRDRSTGALSGGQR 182
Cdd:cd03237 71 KADYEgTVRDLLS--SITKDFYTHP---------------------YFKTEIAKPLQIEQI------LDREVPELSGGEL 121
|
170 180
....*....|....*....|....*.
gi 1586061923 183 SRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03237 122 QRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
404-559 |
7.65e-10 |
|
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: 59.96 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV---------------HAAPGVRVGLLDQD-ATLPGADPEHT 467
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaamsrkelRELRRKKISMVFQSfALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 468 AAHIYhELVGEDRAE-----TVPLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPtnhFSLV----- 537
Cdd:cd03294 123 VAFGL-EVQGVPRAEreeraAEALELVGL--EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA---FSALdplir 196
|
170 180
....*....|....*....|....
gi 1586061923 538 --LATQLEAAVPDYPGTVLVASHD 559
Cdd:cd03294 197 reMQDELLRLQAELQKTIVFITHD 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-232 |
7.66e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLrAPDAGEVRAVG--LGD------PLRVGLLYQE--PPFAPHdtVAQ 101
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGqpLEAwsaaelARHRAYLSQQqtPPFAMP--VFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 AVE---SAVRTVRDAASAVDRTADALarapedegaatayaaaldtaerigawdvdtRIDvtlDGLGlggvdrdRSTGALS 178
Cdd:PRK03695 89 YLTlhqPDKTRTEAVASALNEVAEAL------------------------------GLD---DKLG-------RSVNQLS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 179 GG--QRSRLSlAWLLLSTPDV------LLLDEPTNHLD---DAATDFLRATLRSWHGPVLLASHD 232
Cdd:PRK03695 129 GGewQRVRLA-AVVLQVWPDInpagqlLLLDEPMNSLDvaqQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-208 |
7.98e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 58.09 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYG--SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVravglgdplrvgLLYQEPPFA 94
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI------------TLDGVPVSD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PHDTVAQAVesAVRTVRdaasavdrtadalarapedegaatayaaaldtaerigAWDVDTRIdvtLDGLGLggvdrdrst 174
Cdd:cd03247 69 LEKALSSLI--SVLNQR-------------------------------------PYLFDTTL---RNNLGR--------- 97
|
170 180 190
....*....|....*....|....*....|....
gi 1586061923 175 gALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03247 98 -RFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-210 |
8.22e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 1 MAHPPHSPATpntaahIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVravglgd 80
Cdd:PRK10575 2 QEYTNHSDTT------FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 81 plrvglLYQEPPFAPHDTVAQAVESAV--RTVRDAASAVDRTADALARAPedegaatayaaALDTAERIGAWDVDtRIDV 158
Cdd:PRK10575 69 ------LLDAQPLESWSSKAFARKVAYlpQQLPAAEGMTVRELVAIGRYP-----------WHGALGRFGAADRE-KVEE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 159 TLDGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDA 210
Cdd:PRK10575 131 AISLVGLKPL-AHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-210 |
8.96e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVravglgdplrvglLYQEPPFA-- 94
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-------------LFEGEDIStl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PHDTVAQAVESAVRTvrdAASAVDRTADALA-------RAPEdegaatayaaaldtaerigawdvDTRIDVTLDGLGLGG 167
Cdd:PRK10247 75 KPEIYRQQVSYCAQT---PTLFGDTVYDNLIfpwqirnQQPD-----------------------PAIFLDDLERFALPD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586061923 168 VDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDA 210
Cdd:PRK10247 129 TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-233 |
9.01e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 57.93 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 28 SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVravglGDPLRVGLLY--QEPPFAPHdtvaqaves 105
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPEGEDLLFlpQRPYLPLG--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 106 avrTVRDAasavdrtadaLARApedegaatayaaaldtaerigaWDvdtriDVtldglglggvdrdrstgaLSGGQRSRL 185
Cdd:cd03223 79 ---TLREQ----------LIYP----------------------WD-----DV------------------LSGGEQQRL 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 186 SLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSW--------HGPVLLASHDR 233
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELgitvisvgHRPSLWKFHDR 156
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
403-531 |
9.94e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLePTRGSVHAApGVRVGLLD------------QDATLPG--------- 461
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKIN-GIELRELDpeswrkhlswvgQNPQLPHgtlrdnvll 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 462 ADPEHTAAHIYHELVGEDRAETVPLGTFGLlagrdeNRRVGE----LSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK11174 446 GNPDASDEQLQQALENAWVSEFLPLLPQGL------DTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
404-531 |
1.04e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV---------HAAPGV--RVGLLDQDATLPGADpehtaahIY 472
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhYASKEVarRIGLLAQNATTPGDI-------TV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 473 HELVGEDRAETVPLgtFGLLAGRDE----------------NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK10253 99 QELVARGRYPHQPL--FTRWRKEDEeavtkamqatgithlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-208 |
1.07e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 61.29 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 9 ATPNTAAHIRVSGISASYGSHR-VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG-DPLRVGL 86
Cdd:TIGR01193 466 ELNNLNGDIVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlKDIDRHT 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 LYQEPPFAPHDTV---AQAVESAVRTVRDAAsavdrTADALARAPEDegaatayaaaldtaerigawdvdTRIDVTLDGL 163
Cdd:TIGR01193 546 LRQFINYLPQEPYifsGSILENLLLGAKENV-----SQDEIWAACEI-----------------------AEIKDDIENM 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 164 GLG-GVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:TIGR01193 598 PLGyQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
405-533 |
1.12e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAG-----ESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaaPGVRVG------LLDQDAT----LPGADPEHTAA 469
Cdd:COG1245 355 SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISykpqyiSPDYDGTveefLRSANTDDFGS 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 470 HIYHELVGEdraetvPLGTFGLLagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNH 533
Cdd:COG1245 433 SYYKTEIIK------PLGLEKLL-----DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-232 |
1.27e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.08 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 28 SHRvLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLrAPDAGEVRAvgLGDPL-----------RVGLLYQ-EPPFA- 94
Cdd:COG4138 9 AGR-LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILL--NGRPLsdwsaaelarhRAYLSQQqSPPFAm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 ----------PHDTVAQAVESAVrtvrdaasavdrtaDALARApedegaatayaaaldtaerigawdvdtridvtldgLG 164
Cdd:COG4138 85 pvfqylalhqPAGASSEAVEQLL--------------AQLAEA-----------------------------------LG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 165 LGgvDR-DRSTGALSGG--QRSRLSlAWLLLSTPDV------LLLDEPTNHLD---DAATDFLRATLRSWHGPVLLASHD 232
Cdd:COG4138 116 LE--DKlSRPLTQLSGGewQRVRLA-AVLLQVWPTInpegqlLLLDEPMNSLDvaqQAALDRLLRELCQQGITVVMSSHD 192
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-208 |
1.51e-09 |
|
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: 59.68 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY----GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGL---RAPDAGEVR-----AVGLGD---- 80
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILfdgedLLKLSEkelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 81 PLR---VGLLYQEpPFA---PHDTVAQAVESAVRTVRDaasaVDRtADALARAPEdegaatayaaaldtaerigawdvdt 154
Cdd:COG0444 82 KIRgreIQMIFQD-PMTslnPVMTVGDQIAEPLRIHGG----LSK-AEARERAIE------------------------- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 155 ridvTLDGLGLGGVDR--DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG0444 131 ----LLERVGLPDPERrlDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-208 |
1.53e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.61 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 5 PHSPATPNTAAHIRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLgdPL 82
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ--PI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 RVgllYQEPPFAPHDT-VAQAVESAVRTVRD-----AASAVD-RTADALAR------APEDEGaatayaaaldtaerIGA 149
Cdd:PRK11160 405 AD---YSEAALRQAISvVSQRVHLFSATLRDnlllaAPNASDeALIEVLQQvgleklLEDDKG--------------LNA 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 150 WdvdtridvtldgLGLGGvdRdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11160 468 W------------LGEGG--R-----QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
405-533 |
1.90e-09 |
|
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: 58.57 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAG-----ESWLITGSNGVGKSTLLSLFARRLEPTRGSVhAAPGVRVGLLDQ----------DATLPGADPEHTAA 469
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-EIELDTVSYKPQyikadyegtvRDLLSSITKDFYTH 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 470 HIYHELVGEdraetvPLGTFGLLagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNH 533
Cdd:cd03237 93 PYFKTEIAK------PLQIEQIL-----DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
404-531 |
1.96e-09 |
|
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: 58.45 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLDQDATLP-----------GA--D------- 463
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKELYElrrrigmlfqgGAlfDsltvfen 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 464 ---P--EHTaaHIYHELVgEDRAETVpLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:COG1127 103 vafPlrEHT--DLSEAEI-RELVLEK-LELVGL--PGAADKMPSELSGGMRKRVALARALALDPEILLYDEPT 169
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-219 |
1.99e-09 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 60.12 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSH--RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGLGDPLR----------V 84
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI--LLDGHDLAdytlaslrrqV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPpFAPHDTVA---------QAVESAVRTVRDAASAVDrTADALarapeDEGaatayaaaldtaerigawdVDTR 155
Cdd:TIGR02203 409 ALVSQDV-VLFNDTIAnniaygrteQADRAEIERALAAAYAQD-FVDKL-----PLG-------------------LDTP 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 156 IdvtldglGLGGVDrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATL 219
Cdd:TIGR02203 463 I-------GENGVL-------LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAL 512
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
403-531 |
2.88e-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: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLDQD--ATLPGAD-----------PEHTAa 469
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLA-GQDLFALDEDarARLRARHvgfvfqsfqllPTLTA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 hiyHELVGedraetVPLgtfgLLAGRDENR--------RVG----------ELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:COG4181 108 ---LENVM------LPL----ELAGRRDARararalleRVGlghrldhypaQLSGGEQQRVALARAFATEPAILFADEPT 174
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
405-530 |
2.95e-09 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 57.18 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR-VGLLDQDATL-----------PGADP 464
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIkvndqshtGLAPYQRpVSMLFQENNLfahltvrqnigLGLHP 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 465 EHTAAHIYHELVgEDRAETVPLGTFgllagrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:TIGR01277 98 GLKLNAEQQEKV-VDAAQQVGIADY-------LDRLPEQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
404-533 |
3.07e-09 |
|
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: 56.46 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLDqdatlpGADPEHTAAHIYHELVG----ED 479
Cdd:cd03246 21 VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV---------RLD------GADISQWDPNELGDHVGylpqDD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 480 RaetvplgtfgLLAGR-DENRrvgeLSVGQRRRLALAVLLADPPHVLLLDEPTNH 533
Cdd:cd03246 86 E----------LFSGSiAENI----LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
404-531 |
3.11e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRG--SVHAAP--------GVRVGLLDQDATLpgaDPEHTAAH--- 470
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGkiTVLGVPvpararlaRARIGVVPQFDNL---DLEFTVREnll 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 471 IYHELVG----EDRAETVPLGTFGLLAgRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK13536 137 VFGRYFGmstrEIEAVIPSLLEFARLE-SKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
404-533 |
3.33e-09 |
|
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: 57.63 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV----HAAPGV-------RVGLLDQDATL------------- 459
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidgHDVRDYtlaslrrQIGLVSQDVFLfndtvaeniaygr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 460 PGADPEHT--AAHI--YHELVgedraETVPLGTfgllagrdeNRRVGE----LSVGQRRRLALA-VLLADPPhVLLLDEP 530
Cdd:cd03251 101 PGATREEVeeAARAanAHEFI-----MELPEGY---------DTVIGErgvkLSGGQRQRIAIArALLKDPP-ILILDEA 165
|
...
gi 1586061923 531 TNH 533
Cdd:cd03251 166 TSA 168
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
402-530 |
3.38e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 57.11 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 402 APVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEP---------------TRGSVHAApgvRVGLLDQDA--------- 457
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsasgevllngrrlTALPAEQR---RIGILFQDDllfphlsvg 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 458 -TLPGADPEHTAAHIYHELVgEDRAETVPLGTFGllagrdeNRRVGELSVGQRRRLALA-VLLADPpHVLLLDEP 530
Cdd:COG4136 95 eNLAFALPPTIGRAQRRARV-EQALEEAGLAGFA-------DRDPATLSGGQRARVALLrALLAEP-RALLLDEP 160
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
404-531 |
3.41e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLDQD--ATLPgadPE----------HTAA-- 469
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---------LFEGEdiSTLK---PEiyrqqvsycaQTPTlf 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 470 --HIYHELV---------GEDRAETVPLGTFGLlagrDEN---RRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK10247 94 gdTVYDNLIfpwqirnqqPDPAIFLDDLERFAL----PDTiltKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
177-280 |
3.87e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVdldpaprphavt 256
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELW------------ 695
|
90 100
....*....|....*....|....
gi 1586061923 257 sdLVGDGTgtgigVTRFGGTYSQY 280
Cdd:PLN03073 696 --VVSEGK-----VTPFHGTFHDY 712
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
404-531 |
4.93e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 56.73 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGV---RVGLLD---------QDATL-PG-----ADP- 464
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID-GVdisKIGLHDlrsrisiipQDPVLfSGtirsnLDPf 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 465 -EHTAAHIYH--ELVG-EDRAETVPLGTFGLLAGRDENrrvgeLSVGQRRRLALA-VLLADPPhVLLLDEPT 531
Cdd:cd03244 102 gEYSDEELWQalERVGlKEFVESLPGGLDTVVEEGGEN-----LSVGQRQLLCLArALLRKSK-ILVLDEAT 167
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-222 |
5.02e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 56.73 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASYGSHR--VLTDISFSVTAGDPTGLIGENGSGKST----LLRIVaglrAPDAGEVR-------AVGLGDpL 82
Cdd:cd03244 2 DIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLHD-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 R--VGLLYQEPpfaphdtvaqAVESAvrTVRDaasavdrTADALARAPEDEgaatayaaALDTAERIGAWDVdtrIDVTL 160
Cdd:cd03244 77 RsrISIIPQDP----------VLFSG--TIRS-------NLDPFGEYSDEE--------LWQALERVGLKEF---VESLP 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 161 DGLGLggvDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSW 222
Cdd:cd03244 127 GGLDT---VVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREA 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
404-559 |
5.58e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV----HAAPGVRVGLLD--QDATLPGADPEHT--AAHIYhel 475
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgKPIDYSRKGLMKlrESVGMVFQDPDNQlfSASVY--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 476 vgedraETVPLGTFGLLAGRDE-NRRVGE-----------------LSVGQRRRLALAVLLADPPHVLLLDEPT------ 531
Cdd:PRK13636 102 ------QDVSFGAVNLKLPEDEvRKRVDNalkrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTagldpm 175
|
170 180 190
....*....|....*....|....*....|.
gi 1586061923 532 ---NHFSLVLATQLEAAVpdypgTVLVASHD 559
Cdd:PRK13636 176 gvsEIMKLLVEMQKELGL-----TIIIATHD 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
404-531 |
5.68e-09 |
|
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: 56.82 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFaRRLE-PTRGSVHAApGVRVGLLDQDA------------------------- 457
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLErPTSGSVLVD-GTDLTLLSGKElrkarrrigmifqhfnllssrtvfe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 458 --TLP----GADPEHTAAHIYH--ELVG-EDRAETVPlgtfgllagrdenrrvGELSVGQRRRLALAVLLADPPHVLLLD 528
Cdd:cd03258 102 nvALPleiaGVPKAEIEERVLEllELVGlEDKADAYP----------------AQLSGGQKQRVGIARALANNPKVLLCD 165
|
...
gi 1586061923 529 EPT 531
Cdd:cd03258 166 EAT 168
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
404-566 |
6.04e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLE--PTRGSV---HAAPGVRVGLLDQdatLPGADPEHTAAHIYHelvge 478
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVdvpDNQFGREASLIDA---IGRKGDFKDAVELLN----- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 479 draeTVPLGTFGLLAgrdenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNH----FSLVLATQLEAAVPDYPGTVL 554
Cdd:COG2401 121 ----AVGLSDAVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHldrqTAKRVARNLQKLARRAGITLV 191
|
170
....*....|....*.
gi 1586061923 555 VASHD----RWLRRNW 566
Cdd:COG2401 192 VATHHydviDDLQPDL 207
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
416-559 |
6.16e-09 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 56.53 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 416 ITGSNGVGKSTLLSLFARRLEPTRG--------------SVHAAPGVR-VGLLDQDATL-PGADPEHTAAHIYHELV-GE 478
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGtivlngtvlfdsrkKINLPPQQRkIGLVFQQYALfPHLNVRENLAFGLKRKRnRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 479 DR-AETVPLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAV----PDYPGTV 553
Cdd:cd03297 108 DRiSVDELLDLLGL--DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPV 185
|
....*.
gi 1586061923 554 LVASHD 559
Cdd:cd03297 186 IFVTHD 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-232 |
6.54e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 20 SGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGLGDPL---RVGLLYQEPPFAph 96
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV--LWQGKPLdysKRGLLALRQQVA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 dTVAQAVESAVRTVrDAASAVDRTADALArAPEDEgaatayaaaldtaerigawdVDTRIDvtlDGLGLggVD----RDR 172
Cdd:PRK13638 81 -TVFQDPEQQIFYT-DIDSDIAFSLRNLG-VPEAE--------------------ITRRVD---EALTL--VDaqhfRHQ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 173 STGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGP---VLLASHD 232
Cdd:PRK13638 133 PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHD 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-234 |
8.01e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 9 ATPNTAAhirvSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRI-------VAGLRApdAGEVRAVGLG-- 79
Cdd:PRK14271 18 AAPAMAA----VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRSif 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 80 ---DPL----RVGLLYQEP---PFAPHDTVAQAVESAVRTVRDAASAVdrtadALARAPEdegaatayaaaldtaerIGA 149
Cdd:PRK14271 92 nyrDVLefrrRVGMLFQRPnpfPMSIMDNVLAGVRAHKLVPRKEFRGV-----AQARLTE-----------------VGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 150 WD-VDTRIDvtldglglggvdrdRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG--PV 226
Cdd:PRK14271 150 WDaVKDRLS--------------DSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTV 215
|
....*...
gi 1586061923 227 LLASHDRA 234
Cdd:PRK14271 216 IIVTHNLA 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-208 |
8.69e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSH-----RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrVGLLYQEP 91
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQ---------VGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 92 PFaphDTVAQAVESAVRTVRDAASaVDRTADALARAPEDE------------GAATAYAAALDTAERIGAWdvdtridvt 159
Cdd:PRK13631 93 KK---NNHELITNPYSKKIKNFKE-LRRRVSMVFQFPEYQlfkdtiekdimfGPVALGVKKSEAKKLAKFY--------- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 160 LDGLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
404-530 |
9.15e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 9.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLD-QDATL--PGADPEHTAAHIY----HELV 476
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI---------MLDgVDLSHvpPYQRPINMMFQSYalfpHMTV 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 477 GEDRAetvplgtFGL----LAGRDENRRVGE-----------------LSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK11607 109 EQNIA-------FGLkqdkLPKAEIASRVNEmlglvhmqefakrkphqLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
404-559 |
1.03e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.32 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH-----------AAPGVRVGLLDQDATL--P---------G 461
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwspAELARRRAVLPQHSSLsfPftveevvamG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 462 ADPEHTAAHIYHELVGEDRAETVPLGtfglLAGRDenrrVGELSVGQRRRLALAVLLA------DPPHVLLLDEPTNhfS 535
Cdd:PRK13548 101 RAPHGLSRAEDDALVAAALAQVDLAH----LAGRD----YPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS--A 170
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 536 LVLATQ---LEAA---VPDYPGTVLVASHD 559
Cdd:PRK13548 171 LDLAHQhhvLRLArqlAHERGLAVIVVLHD 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
404-531 |
1.15e-08 |
|
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: 55.65 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFAR-----RLEPTRGSVH------AAPGV-------RVGLLDQDATL-PGADP 464
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLldgkdiYDLDVdvlelrrRVGMVFQKPNPfPGSIY 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 465 EHTA----AHIYHELVGEDRAETVPLGTFGLLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03260 99 DNVAyglrLHGIKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-220 |
1.32e-08 |
|
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: 54.75 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 18 RVSGISAsygsHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavGLGDPLRvgllyqeppfaphd 97
Cdd:cd03215 6 EVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT--LDGKPVT-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 98 tvaqavesaVRTVRDAASAvdrtadALARAPEDegaatayaaaldtaeRIGawdvdtridvtlDGLGLG-GVDRDRSTGA 176
Cdd:cd03215 66 ---------RRSPRDAIRA------GIAYVPED---------------RKR------------EGLVLDlSVAENIALSS 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1586061923 177 -LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:cd03215 104 lLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-221 |
1.38e-08 |
|
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: 55.11 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSH--RVLTDISFSVTAGDPTGLIGENGSGKSTLlrIVAGLRAPDAGE---------VRAVGLGDpLR-- 83
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEgkieidgidISTIPLED-LRss 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 84 VGLLYQEPPFaphdtvaqaVESAVRTVRDaasavdrtadalaraPEDEGAatayaaaldtaerigawDVDTRIDVTLDGL 163
Cdd:cd03369 84 LTIIPQDPTL---------FSGTIRSNLD---------------PFDEYS-----------------DEEIYGALRVSEG 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 164 GLGgvdrdrstgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRS 221
Cdd:cd03369 123 GLN----------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
397-543 |
1.57e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 397 VAGR--MAPVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDatLPGAD 463
Cdd:PRK10575 21 VPGRtlLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsSKAFARKVAYLPQQ--LPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 464 ----PEHTAAHIY--HELVG----EDRA---ETVPLGTFGLLAgrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK10575 99 gmtvRELVAIGRYpwHGALGrfgaADREkveEAISLVGLKPLA----HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170
....*....|...
gi 1586061923 531 TNhfSLVLATQLE 543
Cdd:PRK10575 175 TS--ALDIAHQVD 185
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
405-558 |
1.64e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.42 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLDQDatlPGADPEHtaaHIYHELVGEDRAETV 484
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV---------LLDGV---PLVQYDH---HYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 485 PLG-------TFGLLAGRDE----------------------NRRVGE----LSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:TIGR00958 566 LFSgsvreniAYGLTDTPDEeimaaakaanahdfimefpngyDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|.
gi 1586061923 532 NhfslVLATQLEAAVPDYPG----TVLVASH 558
Cdd:TIGR00958 646 S----ALDAECEQLLQESRSrasrTVLLIAH 672
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-208 |
1.70e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 13 TAAHIRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPLRVGLLYQEP 91
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI--LGQPTRQALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 92 PFAPHD-----TVAQAVESAVRTVRDAASAVDRTADALARAPEDEGaatayaaaldtAERIGAWDVdtridvtldglglg 166
Cdd:PRK15056 81 AYVPQSeevdwSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAA-----------LARVDMVEF-------------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586061923 167 gvdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK15056 136 ---RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
404-532 |
1.72e-08 |
|
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: 55.07 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLDQDATLP-GADPEHTAahIYHELVGEDRae 482
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVKEPAEARRRlGFVSDSTG--LYDRLTAREN-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 483 tvpLGTFGLLAG--RDE------------------NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:cd03266 99 ---LEYFAGLYGlkGDEltarleeladrlgmeellDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-208 |
1.73e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.51 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---LGDP------LR--VGLLYQEpPFA---P 95
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADpeaqklLRqkIQIVFQN-PYGslnP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 HDTVAQAVES--AVRTVRDAASAVDRTADALARapedegaatayaaaldtaerigawdvdtridvtldgLGLGGVDRDRS 173
Cdd:PRK11308 108 RKKVGQILEEplLINTSLSAAERREKALAMMAK------------------------------------VGLRPEHYDRY 151
|
170 180 190
....*....|....*....|....*....|....*
gi 1586061923 174 TGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
404-531 |
1.77e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.21 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGV--------------RVGLLDQDatlpgadPEHtaa 469
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-GVditdkkvklsdirkKVGLVFQY-------PEY--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 HIYHELVGEDRAetvplgtFGL----LAGRDENRRVG-------------------ELSVGQRRRLALAVLLADPPHVLL 526
Cdd:PRK13637 95 QLFEETIEKDIA-------FGPinlgLSEEEIENRVKramnivgldyedykdkspfELSGGQKRRVAIAGVVAMEPKILI 167
|
....*
gi 1586061923 527 LDEPT 531
Cdd:PRK13637 168 LDEPT 172
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
404-535 |
1.87e-08 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 53.97 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVglldqdatlPGADPEHTAAH-IyhelvgedraE 482
Cdd:cd03216 19 VSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-GKEV---------SFASPRDARRAgI----------A 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 483 TVPlgtfgllagrdenrrvgELSVGQRRRLALAVLLADPPHVLLLDEPTNHFS 535
Cdd:cd03216 79 MVY-----------------QLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
404-531 |
1.89e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 55.13 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVRV----GLLDQD----ATLPGADPEHT 467
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrditGLPPHERAragiGYVPEGrrifPELTVEENLLL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 468 AAHIYHELVGEDRAETVpLGTFGLLAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03224 99 GAYARRRAKRKARLERV-YELFPRLKER-RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
403-530 |
1.97e-08 |
|
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: 55.32 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGsvhaapgvRVGLLDQDAT--LPGADPEHTAAHIY----HELV 476
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSG--------EILLDGKDITnlPPHKRPVNTVFQNYalfpHLTV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 477 GEDRAetvplgtFGL-LAGRD--------------------ENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03300 90 FENIA-------FGLrLKKLPkaeikervaealdlvqlegyANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
404-531 |
1.97e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV----HAAPG------VRVGLLDQDATLpgaDPEHTAAH--- 470
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgEPVPSrarharQRVGVVPQFDNL---DPDFTVREnll 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 471 IYHELVG----EDRAETVPLGTFGLLAGRDEnRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK13537 103 VFGRYFGlsaaAARALVPPLLEFAKLENKAD-AKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-208 |
2.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPL------------RVGLLYQEPP---FapH 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknlkklrkKVSLVFQFPEaqlF--E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVAQAVESAVRTVrdaasavdrtadalaRAPEDEGaatayaaaldtAERIGAWdvdtridvtLDGLGLGGVDRDRSTGA 176
Cdd:PRK13641 101 NTVLKDVEFGPKNF---------------GFSEDEA-----------KEKALKW---------LKKVGLSEDLISKSPFE 145
|
170 180 190
....*....|....*....|....*....|..
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
404-531 |
2.48e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHA-----APGVR----------VGLLDQDatlpgadPEHta 468
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgerviTAGKKnkklkplrkkVGIVFQF-------PEH-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 aHIYHELVGEDRAetvpLG--TFGL--------------LAGRDEN---RRVGELSVGQRRRLALAVLLADPPHVLLLDE 529
Cdd:PRK13634 97 -QLFEETVEKDIC----FGpmNFGVseedakqkaremieLVGLPEEllaRSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
..
gi 1586061923 530 PT 531
Cdd:PRK13634 172 PT 173
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
26-239 |
2.79e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 26 YGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLRVGLLYQEPPFAPHDTVAqaveS 105
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI----N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 106 AVRTVRDAASAVDRTADalarapedegaatayaaaldtaeriGAWDVDTRidVTLDGLGLggvDRDRSTGALSGGQRSRL 185
Cdd:PRK13540 87 PYLTLRENCLYDIHFSP-------------------------GAVGITEL--CRLFSLEH---LIDYPCGLLSSGQKRQV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 186 SLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATL---RSWHGPVLLASHDRAFLDTA 239
Cdd:PRK13540 137 ALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIqehRAKGGAVLLTSHQDLPLNKA 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
404-533 |
3.31e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 54.54 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDATL-PG--------AD 463
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVLQDTFLfSGtimenirlGR 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 464 PEHTAAHIyhelvgEDRAETVPLGTFG--LLAGRDENrrVGE----LSVGQRRRLALA-VLLADPPhVLLLDEPTNH 533
Cdd:cd03254 102 PNATDEEV------IEAAKEAGAHDFImkLPNGYDTV--LGEnggnLSQGERQLLAIArAMLRDPK-ILILDEATSN 169
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
403-529 |
3.52e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 56.34 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLDqDATLPGADPE----HTAA-----HIYH 473
Cdd:COG4615 350 PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI---------LLD-GQPVTADNREayrqLFSAvfsdfHLFD 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 474 ELVGEDRAETVPLGTFGL----LAG--RDENRRVG--ELSVGQRRRLALAV-LLADPPhVLLLDE 529
Cdd:COG4615 420 RLLGLDGEADPARARELLerleLDHkvSVEDGRFSttDLSQGQRKRLALLVaLLEDRP-ILVFDE 483
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-239 |
4.28e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSH-----RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV------------------ 73
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 74 --RAVGLGDPL------------RVGLLYQeppFAPHDTVAQAVESAVrtVRDAASAVDRTADALARApedegaatayaa 139
Cdd:PRK13651 83 vlEKLVIQKTRfkkikkikeirrRVGVVFQ---FAEYQLFEQTIEKDI--IFGPVSMGVSKEEAKKRA------------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 140 aldtaerigawdvdtridvtLDGLGLGGVDRD---RSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLR 216
Cdd:PRK13651 146 --------------------AKYIELVGLDESylqRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEIL 205
|
250 260
....*....|....*....|....*.
gi 1586061923 217 ATLRSWH---GPVLLASHDrafLDTA 239
Cdd:PRK13651 206 EIFDNLNkqgKTIILVTHD---LDNV 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-208 |
4.91e-08 |
|
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: 54.08 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS---HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV-------RAVGLGDpLR--V 84
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdiRDLNLRW-LRsqI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GLLYQEPP-FAphDTVAQAV----ESAVRTVRDAASAVDRTADALARAPEdegaatayaaaldtaerigawDVDTRIdvt 159
Cdd:cd03249 80 GLVSQEPVlFD--GTIAENIrygkPDATDEEVEEAAKKANIHDFIMSLPD---------------------GYDTLV--- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 160 ldglGLGGvdrdrstGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03249 134 ----GERG-------SQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
411-560 |
5.11e-08 |
|
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: 52.38 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 411 GESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApgvrvglldqdatlpgadpehtaahiyhelvgedRAETVPLGTFG 490
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI----------------------------------DGEDILEEVLD 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 491 LLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNH---------FSLVLATQLEAAVPDYPGTVLVASHDR 560
Cdd:smart00382 48 QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLldaeqeallLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
404-530 |
5.25e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 55.10 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGEswLIT--GSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR-VGLLDQDATL------------- 459
Cdd:COG3842 24 VSLSIEPGE--FVAllGPSGCGKTTLLRMIAGFETPDSGRIlldgrdvtGLPPEKRnVGMVFQDYALfphltvaenvafg 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 460 ------PGADPEHTAAHIYhELVGedraetvpLGTFgllagrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:COG3842 102 lrmrgvPKAEIRARVAELL-ELVG--------LEGL-------ADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-220 |
6.29e-08 |
|
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: 55.22 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAP---------DAGEVRAVGLGDPLRVG-- 85
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtwdgeiywSGSPLKASNIRDTERAGiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAV----ESAVRTVRDAASAVDRTADALARapedegaatayaaaldtaerigawdvDTRIDVTLD 161
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLR--------------------------ELQLDADNV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 162 GlglggvdrdRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:TIGR02633 136 T---------RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIR 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-220 |
6.48e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPD-AGEVRAVGLGDPL-RVGLLYQEppfa 94
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDkSAGSHIELLGRTVqREGRLARD---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 phdtvaqavesaVRTVRDAASAVDRTADALARAPEDEGAATAYAAALDTAERIGAWDVDTRIDVTLDGL---GLGGVDRD 171
Cdd:PRK09984 81 ------------IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALtrvGMVHFAHQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1586061923 172 RSTgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:PRK09984 149 RVS-TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLR 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
404-531 |
6.69e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.35 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQDATLP-----GADPEHTAAHIYHELVGE 478
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkkvGVVFQFPESQLFEETVLK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 479 DraetVPLGTFGLLAGRDENRRVG-------------------ELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK13643 105 D----VAFGPQNFGIPKEKAEKIAaeklemvgladefwekspfELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-212 |
7.25e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.89 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDaGEVRAVG----LGDPL---------- 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrvefFNQNIyerrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 --RVGLLYQEP---PFAPHDTVAQAVEsaVRTVRDAASAVDRTADALARAPedegaatayaaaldtaerigAWD-VDTRI 156
Cdd:PRK14258 87 rrQVSMVHPKPnlfPMSVYDNVAYGVK--IVGWRPKLEIDDIVESALKDAD--------------------LWDeIKHKI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 157 DvtldglglggvdrdRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT 212
Cdd:PRK14258 145 H--------------KSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
404-559 |
7.53e-08 |
|
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: 55.29 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPT---RGSVH-----------AAPGVRVGLLDQDAtlpgadpehtAA 469
Cdd:COG1123 25 VSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLldgrdllelseALRGRRIGMVFQDP----------MT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 HIYHELVGEDRAETVPLGTFGLLAGRDE--------------NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNhfS 535
Cdd:COG1123 95 QLNPVTVGDQIAEALENLGLSRAEARARvlelleavglerrlDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTT--A 172
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 536 LVLATQ------LEAAVPDYPGTVLVASHD 559
Cdd:COG1123 173 LDVTTQaeildlLRELQRERGTTVLLITHD 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-202 |
8.67e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.80 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 2 AHPPHSPATPNTAAHIRVSGISASYGSHR-----VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAV 76
Cdd:COG4615 313 AADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 77 GlgdplrvgllyqeppfaphdtvaQAVESAVR-TVRDAASAV-------DRTADaLARAPEDegaatayaaaldtaERIG 148
Cdd:COG4615 393 G-----------------------QPVTADNReAYRQLFSAVfsdfhlfDRLLG-LDGEADP--------------ARAR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 149 AWdvdtridvtLDGLGLGG---VDRDR-STGALSGGQRSRLSLAWLLLSTPDVLLLDE 202
Cdd:COG4615 435 EL---------LERLELDHkvsVEDGRfSTTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-231 |
9.32e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 39 VTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLRVGLLYQEPPFAPH-DTVAQAVesavrTVRDAASAV 117
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQfDAIDDLL-----TGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 118 DRtadaLARAPEDEgaatayaaaldtAERIGAWDVDTridvtldgLGLGgVDRDRSTGALSGGQRSRLSLAWLLLSTPDV 197
Cdd:TIGR01257 2037 AR----LRGVPAEE------------IEKVANWSIQS--------LGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586061923 198 LLLDEPTNHLDDAATDFLRATLRSW---HGPVLLASH 231
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSH 2128
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-232 |
9.70e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG---LGDP----LRVGL--- 86
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqhiEGLPghqiARMGVvrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 -----LYQEPPFAPHDTVAQ--AVESAVRTVRDAASAVDRT-ADALARAPEdegaatayaaaldtaerigaWdvdtridv 158
Cdd:PRK11300 86 fqhvrLFREMTVIENLLVAQhqQLKTGLFSGLLKTPAFRRAeSEALDRAAT--------------------W-------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 159 tLDGLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRA---TLRSWHG-PVLLASHD 232
Cdd:PRK11300 138 -LERVGLLEH-ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDEliaELRNEHNvTVLLIEHD 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
404-542 |
9.90e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLD---------------QDAtlPGA-DPEHT 467
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNraqrkafrrdiqmvfQDS--ISAvNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 468 AAHIYHE----LVGEDRAETVP-----LGTFGLLAGrDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVL 538
Cdd:PRK10419 108 VREIIREplrhLLSLDKAERLArasemLRAVDLDDS-VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVL 186
|
....
gi 1586061923 539 ATQL 542
Cdd:PRK10419 187 QAGV 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
404-531 |
1.02e-07 |
|
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: 53.06 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgvrvgLLDQDATlpGADPEHTAA----------HIYH 473
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR--------FDGEDIT--GLPPHRIARlgigyvpegrRIFP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 474 EL-----------------VGEDRAETVpLGTFGLLAGRdENRRVGELSVGQRRRLALA-VLLADPpHVLLLDEPT 531
Cdd:COG0410 92 SLtveenlllgayarrdraEVRADLERV-YELFPRLKER-RRQRAGTLSGGEQQMLAIGrALMSRP-KLLLLDEPS 164
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
31-208 |
1.05e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.30 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlgdplRVGLLYQEPPFAP---HDTVAQAVESAV 107
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----RISFSPQTSWIMPgtiKDNIIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 108 RTVRDAASAVDRTADaLARAPEDEGAAtayaaaldtaerigawdvdtridvtldgLGLGGVdrdrstgALSGGQRSRLSL 187
Cdd:TIGR01271 516 YRYTSVIKACQLEED-IALFPEKDKTV----------------------------LGEGGI-------TLSGGQRARISL 559
|
170 180
....*....|....*....|.
gi 1586061923 188 AWLLLSTPDVLLLDEPTNHLD 208
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLD 580
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-237 |
1.11e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 42 GDPTGLIGENGSGKSTLLRIVAGLRAPDAGEvravglgdplrvgllYQEPP-----------FAPHDTVAQAVESAVRTV 110
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK---------------FDDPPdwdeildefrgSELQNYFTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 111 RDAA------SAVDRTADALARAPEDEGaatayaaaldtaerigawdvdtRIDVTLDGLGLGGVdRDRSTGALSGGQRSR 184
Cdd:cd03236 91 VKPQyvdlipKAVKGKVGELLKKKDERG----------------------KLDELVDQLELRHV-LDRNIDQLSGGELQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 185 LSLAWLLLSTPDVLLLDEPTNHLD-----DAAtdflrATLRSWHGP---VLLASHDRAFLD 237
Cdd:cd03236 148 VAIAAALARDADFYFFDEPSSYLDikqrlNAA-----RLIRELAEDdnyVLVVEHDLAVLD 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
404-531 |
1.33e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGV-----------RVGLLDQDatlpgadPEHtaaHIY 472
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsKVGLVFQD-------PDD---QVF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 473 HELVGEDraetVPLGTFGLLAGRDE-NRRVGE-----------------LSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK13647 94 SSTVWDD----VAFGPVNMGLDKDEvERRVEEalkavrmwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
403-559 |
1.35e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLDqDATLPGADPEH---------TAAHIYH 473
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI---------LLD-GKPVTAEQPEDyrklfsavfTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 474 ELVGEDRAETVPLGTFGLLAG-------RDENRRVG--ELSVGQRRRLALAVLLADPPHVLLLDE------PtnHFSLVL 538
Cdd:PRK10522 411 QLLGPEGKPANPALVEKWLERlkmahklELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEwaadqdP--HFRREF 488
|
170 180
....*....|....*....|.
gi 1586061923 539 ATQLEAAVPDYPGTVLVASHD 559
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHD 509
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-213 |
1.40e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPL---------RVGL------LYQEPpfaphdT 98
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL--FGQPVdagdiatrrRVGYmsqafsLYGEL------T 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 VAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLDGLGLGGVdRDRSTGALS 178
Cdd:NF033858 356 VRQNLELHAR---------------LFHLPAAE--------------------IAARVAEMLERFDLADV-ADALPDSLP 399
|
170 180 190
....*....|....*....|....*....|....*
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATD 213
Cdd:NF033858 400 LGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-224 |
1.54e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV---RAVGLGD------PLRVGLLYQEPPFAPhDTVAQ 101
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiinDSHNLKDinlkwwRSKIGVVSQDPLLFS-NSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 AVESAVRTVRDAasavdrtaDALARAPEDEGAATAYAAALDTAERIGAWDVDTRIDVTLDGLGLGGVDRDRST------- 174
Cdd:PTZ00265 479 NIKYSLYSLKDL--------EALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTikdsevv 550
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 175 ---------------------------GALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHG 224
Cdd:PTZ00265 551 dvskkvlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-220 |
1.59e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 21 GISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRaP----------DAGEVRAVGLGDPLRVG--LLY 88
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtyegeiifEGEELQASNIRDTERAGiaIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 89 QEPPFAPHDTVAQAVesavrtvrdaasavdrtadALARAPEDEGaatayaaaldtaerIGAWD-VDTRIDVTLDGLGLgG 167
Cdd:PRK13549 89 QELALVKELSVLENI-------------------FLGNEITPGG--------------IMDYDaMYLRAQKLLAQLKL-D 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 168 VDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:PRK13549 135 INPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIR 187
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
404-559 |
1.61e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 53.16 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVR--VGLLDQDatlpgadPEHtaaH 470
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikydkKSLLEVRktVGIVFQN-------PDD---Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 471 IYHELVGEDraetVPLGTFGLLAGRDE-NRRVGE-----------------LSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:PRK13639 91 LFAPTVEED----VAFGPLNLGLSKEEvEKRVKEalkavgmegfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 533 HFSLVLATQLEAAVPDYPG---TVLVASHD 559
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-208 |
1.63e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 11 PNTAAHIRVSGISASYGS-HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVglGDP-------- 81
Cdd:PRK10790 335 PLQSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD--GRPlsslshsv 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 82 LRVGL-LYQEPPFAPHDTV-----------AQAVESAVRTVRDAasavdrtadALARAPEDegaatayaaaldtaeriga 149
Cdd:PRK10790 413 LRQGVaMVQQDPVVLADTFlanvtlgrdisEEQVWQALETVQLA---------ELARSLPD------------------- 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 150 wDVDTRidvtldgLGLGGvdrdrstGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK10790 465 -GLYTP-------LGEQG-------NNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-220 |
1.64e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASY-GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGDPLRVGL--- 86
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggRVVNELEPADRDIamv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 87 -----LYqeppfaPHDTVAQAVESAVRtvrdaasavdrtadaLARAPEDEgaatayaaaldtaerigawdVDTRIDVTLD 161
Cdd:PRK11650 82 fqnyaLY------PHMSVRENMAYGLK---------------IRGMPKAE--------------------IEERVAEAAR 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 162 GLGLGGVdRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAatdfLRATLR 220
Cdd:PRK11650 121 ILELEPL-LDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK----LRVQMR 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-208 |
2.08e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV----RAVGLGD----PLRVGLLYQEPPFA--PHDTVAQAV 103
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddHPLHFGDysyrSQRIRMIFQDPSTSlnPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 104 ESAVRtvrdaasaVDRTADALARapedegaatayaaaldtaerigawdvDTRIDVTLDGLGLGGVDRDRSTGALSGGQRS 183
Cdd:PRK15112 111 DFPLR--------LNTDLEPEQR--------------------------EKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180
....*....|....*....|....*
gi 1586061923 184 RLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLD 181
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
404-555 |
2.08e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGV---------------RVGLLDQDatlpgadPEhta 468
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkKVGLVFQF-------PE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 AHIYHELVGEDRA-----------ETVPLGTFGL-LAGRDEN---RRVGELSVGQRRRLALAVLLADPPHVLLLDEPT-- 531
Cdd:PRK13649 96 SQLFEETVLKDVAfgpqnfgvsqeEAEALAREKLaLVGISESlfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTag 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586061923 532 ------------------NHFSLVLATQLEAAVPDYPGTVLV 555
Cdd:PRK13649 176 ldpkgrkelmtlfkklhqSGMTIVLVTHLMDDVANYADFVYV 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-232 |
2.14e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.52 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 28 SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAG-LRAPDAGEvravglGDPLRVGLLYQEPPFAPHDTVAQAVESA 106
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAPR------GARVTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 107 V--RTVRDAASAVDRTADALARAPEdegaatayaaaldtAERIGAWDVDTRiDVTLDGLGLGGVD----RDRSTgaLSGG 180
Cdd:PRK13547 87 VlpQAAQPAFAFSAREIVLLGRYPH--------------ARRAGALTHRDG-EIAWQALALAGATalvgRDVTT--LSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 181 QRSRLSLAWLL---------LSTPDVLLLDEPTNHLDDAAT----DFLRATLRSWHGPVLLASHD 232
Cdd:PRK13547 150 ELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHD 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
404-530 |
2.16e-07 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 52.30 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRG-------SVHAAPGVR-----------VGLL------DQDATL 459
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGeifidgeDIREQDPVElrrkigyviqqIGLFphmtveENIALV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 460 P---GADPEHTAAHIYH--ELVGEDRAETVplgtfgllagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03295 100 PkllKWPKEKIRERADEllALVGLDPAEFA-------------DRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-73 |
2.27e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.46 E-value: 2.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 12 NTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV 73
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
369-559 |
2.40e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 369 FQGLTAGLSgSEAALHRTGPVLTASAAevagrmapvSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhAAPGV 448
Cdd:PRK10070 22 FKYIEQGLS-KEQILEKTGLSLGVKDA---------SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQV-LIDGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 449 RVGLLdQDATLPGADPEHTA------AHIYHELVGEDRAETVPLGTFGLLAGR----DENRRVG----------ELSVGQ 508
Cdd:PRK10070 91 DIAKI-SDAELREVRRKKIAmvfqsfALMPHMTVLDNTAFGMELAGINAEERRekalDALRQVGlenyahsypdELSGGM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 509 RRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAV----PDYPGTVLVASHD 559
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-208 |
2.57e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGL----------------RAPDAGEVRAVGLGDplRVGLLYQEPPFA 94
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydskikvdgkvlyFGKDIFQIDAIKLRK--EVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PH----DTVAQAVES-AVRTVRDAASAVDRTadalarapedegaatayaaaldtAERIGAW-DVDTRIDvtldglglggv 168
Cdd:PRK14246 103 PHlsiyDNIAYPLKShGIKEKREIKKIVEEC-----------------------LRKVGLWkEVYDRLN----------- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586061923 169 drdRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK14246 149 ---SPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-101 |
2.65e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvgLGDPLR-----------VG 85
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY--LGKEVTfngpkssqeagIG 82
|
90
....*....|....*.
gi 1586061923 86 LLYQEPPFAPHDTVAQ 101
Cdd:PRK10762 83 IIHQELNLIPQLTIAE 98
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-237 |
3.25e-07 |
|
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: 53.25 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 3 HPPhsPATPNTAAHIRVSGISASYGShrvltdisFSVTA-------GDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVra 75
Cdd:COG1245 330 HAP--RREKEEETLVEYPDLTKSYGG--------FSLEVeggeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 76 vglgdPLRVGLLYQeppfaphdtvAQAVESAV-RTVRDAASAVdrtadalarapedegaatayaaaldTAERIGAWDVDT 154
Cdd:COG1245 398 -----DEDLKISYK----------PQYISPDYdGTVEEFLRSA-------------------------NTDDFGSSYYKT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 155 RIdvtLDGLGLggvDR--DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDD----AATDFLRATLRSWHGPVLL 228
Cdd:COG1245 438 EI---IKPLGL---EKllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAENRGKTAMV 511
|
....*....
gi 1586061923 229 ASHDRAFLD 237
Cdd:COG1245 512 VDHDIYLID 520
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
404-531 |
3.27e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQ----DATLPgadpeHTAAHIYHELVGED 479
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklylDTTLP-----LTVNRFLRLRPGTK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 480 RAETVPlGTFGLLAGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK09544 98 KEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
404-558 |
3.40e-07 |
|
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: 51.32 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDATLPGADPEHTAAH-- 470
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyeHKYLHSKVSLVGQEPVLFARSLQDNIAYgl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 471 --IYHELVGEdRAETVPLGTF--GLLAGRDEN--RRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEA 544
Cdd:cd03248 113 qsCSFECVKE-AAQKAHAHSFisELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ 191
|
170
....*....|....*.
gi 1586061923 545 AVPDYPG--TVLVASH 558
Cdd:cd03248 192 ALYDWPErrTVLVIAH 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-203 |
3.80e-07 |
|
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: 50.93 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 23 SASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlgdplRVGLLYQEPpFAPHDTV--- 99
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----SIAYVSQEP-WIQNGTIren 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 100 --------AQAVESAVRtvrdaASAVDRTADALARApeDEgaatayaaaldtaerigawdvdTRIdvtldglGLGGVdrd 171
Cdd:cd03250 86 ilfgkpfdEERYEKVIK-----ACALEPDLEILPDG--DL----------------------TEI-------GEKGI--- 126
|
170 180 190
....*....|....*....|....*....|..
gi 1586061923 172 rstgALSGGQRSRLSLAWLLLSTPDVLLLDEP 203
Cdd:cd03250 127 ----NLSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-73 |
3.89e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 3.89e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1586061923 29 HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV 73
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-204 |
5.13e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 5 PHSPATPNTAAhIRVSGISAsygsHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRaVGlGDPLRV 84
Cdd:COG1129 246 PKRAAAPGEVV-LEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR-LD-GKPVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 85 GllyqeppfaphdTVAQAVESAV---------------RTVRD--AASAVDRTADA--LARAPEDEgaatayaaalDTAE 145
Cdd:COG1129 319 R------------SPRDAIRAGIayvpedrkgeglvldLSIREniTLASLDRLSRGglLDRRRERA----------LAEE 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 146 RIGAWDVDTRidvtldglglggvDRDRSTGALSGGQRSRLSLA-WLLLStPDVLLLDEPT 204
Cdd:COG1129 377 YIKRLRIKTP-------------SPEQPVGNLSGGNQQKVVLAkWLATD-PKVLILDEPT 422
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-208 |
5.19e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.05 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 15 AHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAG-------EVRAVGLGDPLR--VG 85
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddeDISLLPLHARARrgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPPFAPHDTVAQAVeSAVRTVRDAASAVDRtadalarapedegaatayaaaldtAERIGAWDVDTRIDVTLDGLGl 165
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNL-MAVLQIRDDLSAEQR------------------------EDRANELMEEFHIEHLRDSMG- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1586061923 166 ggvdrdrstGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK10895 136 ---------QSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-250 |
5.29e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 1 MAHPPHSpATPNTAAHirvsGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVglGD 80
Cdd:PRK13543 1 MIEPLHT-APPLLAAH----ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID--GK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 81 PLRVGLLYQEPPFAPHDTVAQAVESAVRTVRDAASAVDRTADalaRAPEDegaatayaaaldtaerigawdvdtridvTL 160
Cdd:PRK13543 74 TATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAK---QMPGS----------------------------AL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 161 DGLGLGGVDrDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLR----ATLRSwHGPVLLASHDRAFL 236
Cdd:PRK13543 123 AIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNrmisAHLRG-GGAALVTTHGAYAA 200
|
250
....*....|....
gi 1586061923 237 DTAVTSLVDLDPAP 250
Cdd:PRK13543 201 PPVRTRMLTLEAAA 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-208 |
6.17e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.36 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL-GDPL-------RVGLLYQEPPFAPHDTVAQ 101
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLnGMPIdakemraISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 A--VESAVRTVRDAASAVDRTadalarapedegaatayaaaldtaerigawdvdtRIDVTLDGLGL--------GGVDRD 171
Cdd:TIGR00955 119 HlmFQAHLRMPRRVTKKEKRE----------------------------------RVDEVLQALGLrkcantriGVPGRV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586061923 172 RStgaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:TIGR00955 165 KG---LSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
404-531 |
6.49e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 51.66 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLD---------------QD--ATLpgaDPEH 466
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-GQDITGLSgrelrplrrrmqmvfQDpyASL---NPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 467 TAAHIyhelVGEdraetvPLGTFGLLAGRDENRRVGEL------------------SVGQRRRLALAVLLADPPHVLLLD 528
Cdd:COG4608 113 TVGDI----IAE------PLRIHGLASKAERRERVAELlelvglrpehadryphefSGGQRQRIGIARALALNPKLIVCD 182
|
...
gi 1586061923 529 EPT 531
Cdd:COG4608 183 EPV 185
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
406-530 |
6.99e-07 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 50.62 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 406 LTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAA-----PGVR-VGLLDQDATLPGADP---EHT-----AAHI 471
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAgaspgKGWRhIGYVPQRHEFAWDFPisvAHTvmsgrTGHI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 472 ---YHELVGEDRAETVPLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:TIGR03771 81 gwlRRPCVADFAAVRDALRRVGLTELAD--RPVGELSGGQRQRVLVARALATRPSVLLLDEP 140
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
404-531 |
7.02e-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: 50.22 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVR--VGLLDQDATLpgaDPEHTA-- 468
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkKNINELRqkVGMVFQQFNL---FPHLTVle 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 469 ----AHIyhELVGEDRAETVPLGtfgllagRDENRRVG----------ELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03262 96 nitlAPI--KVKGMSKAEAEERA-------LELLEKVGladkadaypaQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
404-531 |
7.12e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLDQDAtLPGADPEH--------------TAA 469
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA-GQDVATLDADA-LAQLRREHfgfifqryhllshlTAA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 470 H------IYHELVGEDRAETVP--LGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK10535 105 QnvevpaVYAGLERKQRLLRAQelLQRLGL--EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
404-531 |
8.39e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.75 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV---------------HAAPGV---RVGLLDqdATLPG---- 461
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpiadyseaalRQAISVvsqRVHLFS--ATLRDnlll 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 462 ADPEHTAAHIYHELvgedraETVPLGTfgLLAGRDE-NRRVGE----LSVGQRRRLALA-VLLADPPhVLLLDEPT 531
Cdd:PRK11160 437 AAPNASDEALIEVL------QQVGLEK--LLEDDKGlNAWLGEggrqLSGGEQRRLGIArALLHDAP-LLLLDEPT 503
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-220 |
9.01e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.62 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASY--GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDaGEVRAVGLGDPlRVGLLYQEPPFA 94
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWN-SVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 phdTVAQAVESAVRTVRdaasavdRTADALARAPEDEgaatayaaALDTAERIGAWDVDTRIDVTLD-GLGLGGVdrdrs 173
Cdd:cd03289 81 ---VIPQKVFIFSGTFR-------KNLDPYGKWSDEE--------IWKVAEEVGLKSVIEQFPGQLDfVLVDGGC----- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586061923 174 tgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLR 220
Cdd:cd03289 138 --VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK 182
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
404-530 |
1.00e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----HAAPGV----------RVGLLDQDatlpgadPEhta 468
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyHITPETgnknlkklrkKVSLVFQF-------PE--- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 469 AHIYHELVGEDrAETVPLgTFGLLAGRDEN------RRVG-----------ELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK13641 96 AQLFENTVLKD-VEFGPK-NFGFSEDEAKEkalkwlKKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
404-530 |
1.05e-06 |
|
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: 50.03 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--------HAAPGVR-VGLLDQDATL--------------- 459
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedatDVPVQERnVGFVFQHYALfrhmtvfdnvafglr 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 460 --PGAD--PEHTAAHIYHELVgedraETVPLGTFgllagrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03296 101 vkPRSErpPEAEIRAKVHELL-----KLVQLDWL-------ADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-220 |
1.05e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 2 AHPPHSPATPNTAAhIRVSGISA-SYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV------- 73
Cdd:COG3845 244 LRVEKAPAEPGEVV-LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIrldgedi 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 74 --------RAVGLG----DPLRVGLlyqeppfAPHDTVAQAVesAVRTVRDAASA----VDR-TADALARapedegaata 136
Cdd:COG3845 323 tglsprerRRLGVAyipeDRLGRGL-------VPDMSVAENL--ILGRYRRPPFSrggfLDRkAIRAFAE---------- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 137 yaaaldtaERIGAWDVDTRidvtldglglggvDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLR 216
Cdd:COG3845 384 --------ELIEEFDVRTP-------------GPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIH 442
|
....
gi 1586061923 217 ATLR 220
Cdd:COG3845 443 QRLL 446
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
404-575 |
1.15e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 50.92 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGEswLIT--GSNGVGKSTLLSLFARRLEPTRGSV---------HAAPGVR-VGLLDQD--------------A 457
Cdd:COG1118 21 VSLEIASGE--LVAllGPSGSGKTTLLRIIAGLETPDSGRIvlngrdlftNLPPRERrVGFVFQHyalfphmtvaeniaF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 458 TLPGADP-EHTAAHIYHELvgedraetvpLGTFGL--LAgrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEPtnhF 534
Cdd:COG1118 99 GLRVRPPsKAEIRARVEEL----------LELVQLegLA----DRYPSQLSGGQRQRVALARALAVEPEVLLLDEP---F 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 535 SlvlAtqLEAAV------------PDYPGTVLVASHDrwlrrnwtgRDLALEV 575
Cdd:COG1118 162 G---A--LDAKVrkelrrwlrrlhDELGGTTVFVTHD---------QEEALEL 200
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-208 |
1.23e-06 |
|
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: 49.16 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 27 GSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRapDAGEVRAVGLGDPLRVGLLYQ-EPPFAPHdtvaQAVES 105
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVITGEILINGRPLDKNFQrSTGYVEQ----QDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 106 AVRTVRDAAsavdrtadalarapedegaatayaaaldtaeRIGAWdvdtridvtLDGLGLggvdrdrstgalsgGQRSRL 185
Cdd:cd03232 92 PNLTVREAL-------------------------------RFSAL---------LRGLSV--------------EQRKRL 117
|
170 180
....*....|....*....|...
gi 1586061923 186 SLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:cd03232 118 TIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-208 |
1.47e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 51.00 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 25 SYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLrAPDAGEVRAVGLgdPLR----------VGLLYQEPPFa 94
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGI--ELReldpeswrkhLSWVGQNPQL- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 95 PHDTVAQAVesavrTVRDAASAVDRTADALARApedegaatayaaaldtaeriGAWDVdtridVTLDGLGLGGVDRDRST 174
Cdd:PRK11174 435 PHGTLRDNV-----LLGNPDASDEQLQQALENA--------------------WVSEF-----LPLLPQGLDTPIGDQAA 484
|
170 180 190
....*....|....*....|....*....|....
gi 1586061923 175 GaLSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11174 485 G-LSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
400-558 |
1.49e-06 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 51.19 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 400 RMAPVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH-----------AAPGVRVGLLDQDATL-PG------ 461
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRldgadlkqwdrETFGKHIGYLPQDVELfPGtvaeni 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 462 ------ADPEHT--AAHI--YHELVG--EDRAETVpLGTFGllagrdenrrvGELSVGQRRRLALAVLLADPPHVLLLDE 529
Cdd:TIGR01842 413 arfgenADPEKIieAAKLagVHELILrlPDGYDTV-IGPGG-----------ATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190
....*....|....*....|....*....|....*.
gi 1586061923 530 PTNHfslvLATQLEAAVPD-------YPGTVLVASH 558
Cdd:TIGR01842 481 PNSN----LDEEGEQALANaikalkaRGITVVVITH 512
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
404-546 |
1.50e-06 |
|
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: 49.46 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH---------AAPGVR--VGLLDQDATL------------- 459
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirdlNLRWLRsqIGLVSQEPVLfdgtiaenirygk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 460 -PGADPEHTAA--------------HIYHELVGEdraetvplgtfgllagrdenrRVGELSVGQRRRLALAVLLADPPHV 524
Cdd:cd03249 102 pDATDEEVEEAakkanihdfimslpDGYDTLVGE---------------------RGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180
....*....|....*....|..
gi 1586061923 525 LLLDEPTNhfslVLATQLEAAV 546
Cdd:cd03249 161 LLLDEATS----ALDAESEKLV 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
404-531 |
1.61e-06 |
|
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: 50.84 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLlslfAR---RLEPTRGSVHAApGVRVGLLDQDATLP-------------GA-DPEH 466
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTL----GLallRLIPSEGEIRFD-GQDLDGLSRRALRPlrrrmqvvfqdpfGSlSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 467 TAAhiyhELVGEdraetvPLGTFGLLAGRDENRR--------VG-----------ELSVGQRRRLALAVLLADPPHVLLL 527
Cdd:COG4172 380 TVG----QIIAE------GLRVHGPGLSAAERRArvaealeeVGldpaarhryphEFSGGQRQRIAIARALILEPKLLVL 449
|
....
gi 1586061923 528 DEPT 531
Cdd:COG4172 450 DEPT 453
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
31-208 |
1.72e-06 |
|
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: 49.86 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGlgdplRVGLLYQEPPFAPHdtvaqavesavrTV 110
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISFSSQFSWIMPG------------TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 111 RDaasavdrtaDALARAPEDEGAATAYAAALDTAERIGAW-DVDTRIdvtldgLGLGGVDrdrstgaLSGGQRSRLSLAW 189
Cdd:cd03291 115 KE---------NIIFGVSYDEYRYKSVVKACQLEEDITKFpEKDNTV------LGEGGIT-------LSGGQRARISLAR 172
|
170
....*....|....*....
gi 1586061923 190 LLLSTPDVLLLDEPTNHLD 208
Cdd:cd03291 173 AVYKDADLYLLDSPFGYLD 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
396-532 |
2.03e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 396 EVAGRMAPVSLTVSAGESWLIT--GSNGVGKSTLLSLFARRLEPTRGSVhaapgvRVGLLDQDATLP------GADPEHT 467
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQITAflGHNGAGKTTTLSILTGLLPPTSGTV------LVGGKDIETNLDavrqslGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 468 --------AAHI--YHELVGEDRAET-----VPLGTFGLLAGRDENRRvgELSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:TIGR01257 1013 ilfhhltvAEHIlfYAQLKGRSWEEAqlemeAMLEDTGLHHKRNEEAQ--DLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
404-531 |
2.53e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 49.24 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGEsWL-ITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGV-----------RVGLLDQdatlpgaDPEhtaahi 471
Cdd:PRK13635 26 VSFSVYEGE-WVaIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrQVGMVFQ-------NPD------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 472 yHELVGEDRAETVplgTFGLlagrdENR---------RVGE-----------------LSVGQRRRLALAVLLADPPHVL 525
Cdd:PRK13635 92 -NQFVGATVQDDV---AFGL-----ENIgvpreemveRVDQalrqvgmedflnrephrLSGGQKQRVAIAGVLALQPDII 162
|
....*.
gi 1586061923 526 LLDEPT 531
Cdd:PRK13635 163 ILDEAT 168
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
404-531 |
2.65e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.69 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARrLE-PTRGSVHAApGVRVGLLDQDA---------------------T--- 458
Cdd:COG1135 24 VSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSVLVD-GVDLTALSERElraarrkigmifqhfnllssrTvae 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 459 ---LP----GADPEHTAAHIYH--ELVG-EDRAETVPlgtfgllagrdenrrvGELSVGQRRRLALAVLLADPPHVLLLD 528
Cdd:COG1135 102 nvaLPleiaGVPKAEIRKRVAEllELVGlSDKADAYP----------------SQLSGGQKQRVGIARALANNPKVLLCD 165
|
...
gi 1586061923 529 EPT 531
Cdd:COG1135 166 EAT 168
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
404-531 |
2.93e-06 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 48.64 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhAAPGVRVGLLD------------QDATL------------ 459
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHDLALADpawlrrqvgvvlQENVLfnrsirdniala 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 460 -PGADPEHT--AAHI--YHELVGEdraetVPLGtFGLLAGRdenRRVGeLSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03252 100 dPGMSMERVieAAKLagAHDFISE-----LPEG-YDTIVGE---QGAG-LSGGQRQRIAIARALIHNPRILIFDEAT 166
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
404-559 |
3.23e-06 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 48.49 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGsvhaapgvRVGLLDQDAT-LPgadPE-HTAAHIYHE------- 474
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG--------KILLNGKDITnLP---PEkRDISYVPQNyalfphm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 475 -----------LVGEDRAE--------TVPLGTFGLLagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFS 535
Cdd:cd03299 87 tvykniayglkKRKVDKKEierkvleiAEMLGIDHLL-----NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180
....*....|....*....|....*...
gi 1586061923 536 L----VLATQLEAAVPDYPGTVLVASHD 559
Cdd:cd03299 162 VrtkeKLREELKKIRKEFGVTVLHVTHD 189
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
404-531 |
3.32e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.59 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvRVGLLDQDATLPGAD-------------------- 463
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI------RVGDITIDTARSLSQqkglirqlrqhvgfvfqnfn 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 464 --PEHTAAHIYHE----LVGEDRAETVPLGTFGL----LAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK11264 96 lfPHRTVLENIIEgpviVKGEPKEEATARARELLakvgLAGK-ETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
404-530 |
3.63e-06 |
|
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: 48.02 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH--------AAPGVR-VGLLDQDATLPgadPEHTAA-HIYH 473
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdIAMVFQNYALY---PHMTVYdNIAF 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 474 --ELVGEDRAETVP--------LGTFGLLagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03301 96 glKLRKVPKDEIDErvrevaelLQIEHLL-----DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-64 |
3.80e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 3.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 2 AHPPHSPATPNTAAHIRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAG 64
Cdd:PRK10938 246 DEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
404-546 |
4.20e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH---------AAPGVR--VGLLDQDATL------------- 459
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtvTRASLRrnIAVVFQDAGLfnrsiednirvgr 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 460 PGADPE--HTAAHIYHELvgeDRAETVPLGtFGLLAGrdenRRVGELSVGQRRRLALA-VLLADPPhVLLLDEPTNHFSL 536
Cdd:PRK13657 434 PDATDEemRAAAERAQAH---DFIERKPDG-YDTVVG----ERGRQLSGGERQRLAIArALLKDPP-ILILDEATSALDV 504
|
170
....*....|
gi 1586061923 537 VLATQLEAAV 546
Cdd:PRK13657 505 ETEAKVKAAL 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-208 |
4.52e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 46 GLIGENGSGKSTLLRIVAGLRAPDAGEVRAvglgdPLRVGllyqeppFAPhdtvaQAVESAVR-TVRDAasavdrtadaL 124
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-----ELKIS-------YKP-----QYIKPDYDgTVEDL----------L 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 125 ARAPEDEGaatayaaaldtaeriGAWdVDTRIdvtLDGLGLggvDR--DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDE 202
Cdd:PRK13409 422 RSITDDLG---------------SSY-YKSEI---IKPLQL---ERllDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
....*.
gi 1586061923 203 PTNHLD 208
Cdd:PRK13409 480 PSAHLD 485
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-204 |
4.75e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.95 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 22 ISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGlrAPDAGEVRAVGLGDPLrvgllyqeppfaphdTVAQ 101
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDI---------------TDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 102 avesAVRTVRDAASAVDRTADALARAPEDEGAAtayaaaldtaerIGAWDVD-----TRIDVTLDGLGLGGVDRDRSTGA 176
Cdd:PRK11614 74 ----TAKIMREAVAIVPEGRRVFSRMTVEENLA------------MGGFFAErdqfqERIKWVYELFPRLHERRIQRAGT 137
|
170 180
....*....|....*....|....*...
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPT 204
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-260 |
4.92e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASygSHRVLT-DISFSVTAGDPTGLIGENGSGKS-----TLLRIVAGLRAPdAGEVRAVGLgdplrvgllyqe 90
Cdd:PRK10418 5 IELRNIALQ--AAQPLVhGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQT-AGRVLLDGK------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 91 pPFAPHD-------TVAQAVESAVRTVRDAASAVDRTADALARAPedegaatayaaaldtaerigawdVDTRIDVTLDGL 163
Cdd:PRK10418 70 -PVAPCAlrgrkiaTIMQNPRSAFNPLHTMHTHARETCLALGKPA-----------------------DDATLTAALEAV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 164 GLGGVDR--DRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAAT----DFLRATLRSwHGP-VLLASHD---- 232
Cdd:PRK10418 126 GLENAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQarilDLLESIVQK-RALgMLLVTHDmgvv 204
|
250 260 270
....*....|....*....|....*....|....*...
gi 1586061923 233 -RAFLDTAVTS---LVDLDP------APRpHAVTSDLV 260
Cdd:PRK10418 205 aRLADDVAVMShgrIVEQGDvetlfnAPK-HAVTRSLV 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-208 |
5.24e-06 |
|
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: 49.30 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISASYGS----HRVLTDISFSVTAGDPTGLIGENGSGKS----TLLRIVAGLRAPDAGEVRAVG---LGDPL--- 82
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGqdlLGLSErel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 ------RVGLLYQEPPFA--PHDTV-AQAVESAV--RTVRDAAsAVDRTADALARA--PEDEgaatayaaaldtaERIGA 149
Cdd:COG4172 87 rrirgnRIAMIFQEPMTSlnPLHTIgKQIAEVLRlhRGLSGAA-ARARALELLERVgiPDPE-------------RRLDA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 150 WdvdtridvtldglglggvdrdrsTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:COG4172 153 Y-----------------------PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-74 |
5.35e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 49.43 E-value: 5.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 4 PPHSPATPNTAAHIRVSGISASYGSHR-VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVR 74
Cdd:COG5265 345 APDAPPLVVGGGEVRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL 416
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
404-530 |
5.50e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.79 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaapgvrvgLLDQDATlpGADPEH----TAAHIY----HEL 475
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM--------LDGQDIT--HVPAENrhvnTVFQSYalfpHMT 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 476 VGEDRAetvplgtFGLL---AGRDE------------------NRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK09452 103 VFENVA-------FGLRmqkTPAAEitprvmealrmvqleefaQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-208 |
5.55e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 17 IRVSGISAsygsHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGL-------GDPLRVGLLyq 89
Cdd:PRK11288 258 LRLDGLKG----PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirspRDAIRAGIM-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 90 eppFAPHDTVAQAVeSAVRTVRD--AASAVDRTADA---LARAPEDEgaatayaaalDTAERIGAWDVDTRidvtldglg 164
Cdd:PRK11288 332 ---LCPEDRKAEGI-IPVHSVADniNISARRHHLRAgclINNRWEAE----------NADRFIRSLNIKTP--------- 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 165 lggvDRDRSTGALSGGQRSRLSLA-WllLSTP-DVLLLDEPTNHLD 208
Cdd:PRK11288 389 ----SREQLIMNLSGGNQQKAILGrW--LSEDmKVILLDEPTRGID 428
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
175-239 |
6.42e-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: 47.22 E-value: 6.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 175 GALSGGQRS------RLSLAWLLLSTPDVLLLDEPTNHLDD-----AATDFLRATLRSWHGPVLLASHDRAFLDTA 239
Cdd:cd03240 114 GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenieeSLAEIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
404-531 |
6.82e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 47.41 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHaAPGVRVGLLDQDA-----TLPGADPEHTAAHIYHELVGE 478
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE-IDGIDISTIPLEDlrsslTIIPQDPTLFSGTIRSNLDPF 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 479 DRAETVPLgtFGLLagrdenrRVGE----LSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:cd03369 106 DEYSDEEI--YGAL-------RVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
404-530 |
6.87e-06 |
|
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: 47.65 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV------------HAAPGVRVGLLDQDAT----LPGADPEHT 467
Cdd:TIGR04406 20 VSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIlidgqdithlpmHERARLGIGYLPQEASifrkLTVEENIMA 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 468 AAHIYHELVGEDRAETVP--LGTFGLLAGRDEnrRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:TIGR04406 100 VLEIRKDLDRAEREERLEalLEEFQISHLRDN--KAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-208 |
7.11e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 16 HIRVSGISASYGS--HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV--RAVGLGD----PLR--VG 85
Cdd:PRK11176 341 DIEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIllDGHDLRDytlaSLRnqVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 86 LLYQEPpfapH---DTVAQAVESAvRTVRDAASAVDRTADaLARAPE-----DEGaatayaaaldtaerigawdVDTRId 157
Cdd:PRK11176 421 LVSQNV----HlfnDTIANNIAYA-RTEQYSREQIEEAAR-MAYAMDfinkmDNG-------------------LDTVI- 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1586061923 158 vtldglGLGGVdrdrstgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11176 475 ------GENGV-------LLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-77 |
8.17e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.50 E-value: 8.17e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1586061923 32 LTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVG 77
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
404-559 |
1.32e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV------------HAAPGVR---VGLLDQDATLPgadPEHTA 468
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklssAAKAELRnqkLGFIYQFHHLL---PDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 469 AH--IYHELVGEDRAETVPLGTFGLLAG----RDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLAT-- 540
Cdd:PRK11629 105 LEnvAMPLLIGKKKPAEINSRALEMLAAvgleHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADsi 184
|
170 180
....*....|....*....|.
gi 1586061923 541 -QLEAAVPDYPGTV-LVASHD 559
Cdd:PRK11629 185 fQLLGELNRLQGTAfLVVTHD 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
404-533 |
1.34e-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: 46.00 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEP--TRGSVH--------AAPGVRVGLLDQDATLPGADPEHTAAHIYH 473
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLingrpldkRSFRKIIGYVPQDDILHPTLTVRETLMFAA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 474 ELVGedraetvplgtfgllagrdenrrvgeLSVGQRRRLALAVLLADPPHVLLLDEPTNH 533
Cdd:cd03213 108 KLRG--------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
404-535 |
1.93e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLDQDATLpgadpEHTAAHIYHEL--VGE-DR 480
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-GQEMRFASTTAAL-----AAGVAIIYQELhlVPEmTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 481 AETVPLG----TFGLLAGR-----------------DENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFS 535
Cdd:PRK11288 97 AENLYLGqlphKGGIVNRRllnyeareqlehlgvdiDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
34-207 |
2.22e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.53 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGdPTGLIGENGSGKSTLLR-IVAGLRAPDAGEVRAVGLGDPLRVG-LLYQEPPFAPHDTVAQAVESAVRTVR 111
Cdd:COG3950 18 EIDFDNPPR-LTVLVGENGSGKTTLLEaIALALSGLLSRLDDVKFRKLLIRNGeFGDSAKLILYYGTSRLLLDGPLKKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 112 DAASAVDRTADALARAPEDEGAATAYAAALDTAERIGAWDVDTRIDVTLDGL---------GLGGVDRDRSTG------- 175
Cdd:COG3950 97 RLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVrealnkllpDFKDIRIDRDPGrlvildk 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 176 --------ALSGGQRSRLSLAWLL--------------LSTPDVLLLDEPTNHL 207
Cdd:COG3950 177 ngeelplnQLSDGERSLLALVGDLarrlaelnpalenpLEGEGIVLIDEIDLHL 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
393-566 |
2.68e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 393 SAAEVAGRMA--PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV------------HAAPGVR--VGLLDQD 456
Cdd:PRK10908 8 SKAYLGGRQAlqGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknREVPFLRrqIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 457 atlpgadpehtaahiYHELVGEDRAETV--PLGTFGLlAGRDENRRVG-----------------ELSVGQRRRLALAVL 517
Cdd:PRK10908 88 ---------------HHLLMDRTVYDNVaiPLIIAGA-SGDDIRRRVSaaldkvglldkaknfpiQLSGGEQQRVGIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 518 LADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPG---TVLVASHDRWL--RRNW 566
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLisRRSY 205
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-220 |
2.77e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.15 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGE-----------VRAVGLGDPLR--VGLLYQEPPFAP- 95
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanLKKIKEVKRLRkeIGLVFQFPEYQLf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 96 HDTVAQAVesavrtvrdaasavdrtadalARAPEDEGAATAyaaaldtaerigawDVDTRIDVTLDGLGLGGVDRDRSTG 175
Cdd:PRK13645 105 QETIEKDI---------------------AFGPVNLGENKQ--------------EAYKKVPELLKLVQLPEDYVKRSPF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 176 ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD-DAATDFLRATLR 220
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDpKGEEDFINLFER 195
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-221 |
2.78e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAG-LRAPD-AGEVRAVG--LGDPL--RVGLLYQEPPFAPHdtvaqave 104
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNrkPTKQIlkRTGFVTQDDILYPH-------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 105 savRTVRDAASAVdrtadALARAPEDEGAATAYAAALDTAERIGAwdvdTRIDVTLDGlglggvdrDRSTGALSGGQRSR 184
Cdd:PLN03211 155 ---LTVRETLVFC-----SLLRLPKSLTKQEKILVAESVISELGL----TKCENTIIG--------NSFIRGISGGERKR 214
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586061923 185 LSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRS 221
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
159-250 |
3.13e-05 |
|
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: 44.62 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 159 TLDGLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPD--VLLLDEPTNHLDDAATDFLRA---TLRSWHGPVLLASHDR 233
Cdd:cd03238 70 FLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEvikGLIDLGNTVILIEHNL 149
|
90
....*....|....*..
gi 1586061923 234 AFLDTAVTsLVDLDPAP 250
Cdd:cd03238 150 DVLSSADW-IIDFGPGS 165
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
403-532 |
3.19e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 45.33 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGsvhaapgvrvglLDQDATLPGADPEHTAAHIYHEL--VGEDR 480
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS------------VEGDIHYNGIPYKEFAEKYPGEIiyVSEED 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 481 aETVPLGT------FGLLAGRDENRRVgeLSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:cd03233 93 -VHFPTLTvretldFALRCKGNEFVRG--ISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
405-530 |
3.26e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV--HAAPGVRVG------LLDQ-------DATLPGADPE-HTA 468
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsQFSHITRLSfeqlqkLVSDewqrnntDMLSPGEDDTgRTT 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 469 AHIYHELVgEDRAETVPLGT-FG---LLagrdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK10938 103 AEIIQDEV-KDPARCEQLAQqFGitaLL-----DRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
411-531 |
3.43e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.58 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 411 GESWLITGSNGVGKSTLLSLFARRLEP--TRGSVHAAPGVRVGL---------LDQDATLPGA--------------DPE 465
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLNGMPIDAkemraisayVQQDDLFIPTltvrehlmfqahlrMPR 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 466 HTAAHIYHELVGE--------DRAETVpLGTFGLLAGrdenrrvgeLSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:TIGR00955 131 RVTKKEKRERVDEvlqalglrKCANTR-IGVPGRVKG---------LSGGERKRLAFASELLTDPPLLFCDEPT 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
29-215 |
3.44e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.95 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 29 HRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGdplrvGLLYQEPPFAPHDTVAQAVES--- 105
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYN-----GIPYKEFAEKYPGEIIYVSEEdvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 106 -AVRTVRdaasavdRTADALARAPEDEGaatayaaaldtaerigawdvdtridvtldglgLGGVdrdrstgalSGGQRSR 184
Cdd:cd03233 95 fPTLTVR-------ETLDFALRCKGNEF--------------------------------VRGI---------SGGERKR 126
|
170 180 190
....*....|....*....|....*....|..
gi 1586061923 185 LSLAWLLLSTPDVLLLDEPTNHLDDA-ATDFL 215
Cdd:cd03233 127 VSIAEALVSRASVLCWDNSTRGLDSStALEIL 158
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
404-528 |
4.44e-05 |
|
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: 44.77 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPgvRVGLLDQDATLPGA------------DPEHtaahi 471
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQNGtirenilfgkpfDEER----- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 472 YHELV-----GEDraetvplgtFGLLAGRDENrRVGE----LSVGQRRRLALA-VLLADPPHVLLLD 528
Cdd:cd03250 97 YEKVIkacalEPD---------LEILPDGDLT-EIGEkginLSGGQKQRISLArAVYSDADIYLLDD 153
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-114 |
4.45e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 4.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 42 GDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLGDPLRVGLLYQEPPFAPHDTVAQAVESAVRTVRDAA 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-211 |
5.28e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAG-------EVRAVGLGDPLRVGLLYqeppfAPHdtvaqavesa 106
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGrimlngkEINALSTAQRLARGLVY-----LPE---------- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 107 vrtvrdaasavDRTADAL-ARAPedegaaTAYAAALDTAERIGAWDVDTRIDVTLDG----LGLGGVDRDRSTGALSGGQ 181
Cdd:PRK15439 346 -----------DRQSSGLyLDAP------LAWNVCALTHNRRGFWIKPARENAVLERyrraLNIKFNHAEQAARTLSGGN 408
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 182 RSRLSLAWLLLSTPDVLLLDEPTNHLDDAA 211
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
404-531 |
7.31e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV----HAAPGVRVGLLDQDATLPGADPEHTAAHIYHEL---- 475
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVtlgr 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 476 -VGEDRA----ETVPLGTF--GLLAGRdeNRRVGE----LSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK10790 440 dISEEQVwqalETVQLAELarSLPDGL--YTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEAT 504
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
404-543 |
7.49e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRgsvHAAPGVRVGLLDQDATLPGADPEHTAAHI----------YH 473
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE---EARVEGEVRLFGRNIYSPDVDPIEVRREVgmvfqypnpfPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 474 ELVGEDRAETVPLGtfGLLAGRDE----------------------NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK14267 100 LTIYDNVAIGVKLN--GLVKSKKEldervewalkkaalwdevkdrlNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170
....*....|..
gi 1586061923 532 NHFSLVLATQLE 543
Cdd:PRK14267 178 ANIDPVGTAKIE 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-208 |
7.59e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 29 HRVLTDISFSVTAGDPTGLIGENGSGKS-TLLRIVAGLRAPDA----GEVRAVG--------------LGDplRVGLLYQ 89
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGesllhaseqtlrgvRGN--KIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 90 EP-----PFapHDTVAQAVE--SAVRTVRDAAsavdrtadalARApedegaatayaAALDTAERIGAWDVDTRIdvtldg 162
Cdd:PRK15134 100 EPmvslnPL--HTLEKQLYEvlSLHRGMRREA----------ARG-----------EILNCLDRVGIRQAAKRL------ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1586061923 163 lglggvdRDRSTgALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK15134 151 -------TDYPH-QLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
404-530 |
8.52e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.50 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV------------HAAPGVRVGLLDQDAT----LPGADPEHT 467
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQEASifrrLSVYDNLMA 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 468 AAHIYHELVGE---DRAETVpLGTFGLLAGRDEnrrVGE-LSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK10895 102 VLQIRDDLSAEqreDRANEL-MEEFHIEHLRDS---MGQsLSGGERRRVEIARALAANPKFILLDEP 164
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
403-531 |
9.82e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.79 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAApGVRVGLLDqdatlpgaDPEHTAAH-----IY-H--- 473
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-GQDLTALS--------EKELRKARrqigmIFqHfnl 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 474 --------------ELVGEDRAE-----TVPLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK11153 94 lssrtvfdnvalplELAGTPKAEikarvTELLELVGLSDKAD--RYPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-64 |
1.02e-04 |
|
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: 43.67 E-value: 1.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1586061923 17 IRVSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAG 64
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG 48
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
404-531 |
1.05e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhAAPGV---RVGLLDQDATL---PGA------------DP- 464
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI-LIDGCdisKFGLMDLRKVLgiiPQApvlfsgtvrfnlDPf 1336
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 465 -EHTAAHIYHELvgeDRA---ETVPLGTFGLLAgrdENRRVGE-LSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PLN03130 1337 nEHNDADLWESL---ERAhlkDVIRRNSLGLDA---EVSEAGEnFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
418-532 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 418 GSNGVGKSTLLSLFARRLEPtrgsvhaapGVRVGLLDQDATLPGADPEHTAAHIYHELVGEDRAeTV--PLGTFGLLAGr 495
Cdd:cd03232 40 GESGAGKTTLLDVLAGRKTA---------GVITGEILINGRPLDKNFQRSTGYVEQQDVHSPNL-TVreALRFSALLRG- 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 1586061923 496 denrrvgeLSVGQRRRLALAVLLADPPHVLLLDEPTN 532
Cdd:cd03232 109 --------LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
404-559 |
1.17e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 44.83 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH-----------AAPGVRVGLLDQDATLP-----------G 461
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVASVPQDTSLSfefdvrqvvemG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 462 ADPEHTAAHIYHElvGEDRAETVPLGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT-----NHfsL 536
Cdd:PRK09536 102 RTPHRSRFDTWTE--TDRAAVERAMERTGVAQFAD--RPVTSLSGGERQRVLLARALAQATPVLLLDEPTasldiNH--Q 175
|
170 180
....*....|....*....|...
gi 1586061923 537 VLATQLEAAVPDYPGTVLVASHD 559
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIHD 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
404-559 |
1.18e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.31 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH------AAPGV-----RVGLLDQ--DATLPGADPEHTAAh 470
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgellTAENVwnlrrKIGMVFQnpDNQFVGATVEDDVA- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 471 IYHELVGEDRAETVPLGTFGLLAGRD---ENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVP 547
Cdd:PRK13642 105 FGMENQGIPREEMIKRVDEALLAVNMldfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH 184
|
170
....*....|....*.
gi 1586061923 548 D----YPGTVLVASHD 559
Cdd:PRK13642 185 EikekYQLTVLSITHD 200
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
492-531 |
1.25e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.31 E-value: 1.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1586061923 492 LAGRDEN---RRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK13651 151 LVGLDESylqRSPFELSGGQKRRVALAGILAMEPDFLVFDEPT 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-73 |
1.27e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 1.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 20 SGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV 73
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
404-531 |
1.40e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.62 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVhaapgvrvgLLDqDATLPGADPEHTAAH----IYHEL---- 475
Cdd:COG1129 23 VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI---------LLD-GEPVRFRSPRDAQAAgiaiIHQELnlvp 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 476 ---VGE--------------------DRAETVpLGTFGLlaGRDENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:COG1129 93 nlsVAEniflgreprrgglidwramrRRAREL-LARLGL--DIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
404-531 |
1.42e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.54 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRG-------SVHAaPGVRVGLLDQDATLPGAD----PEHTAAhiy 472
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglKVND-PKVDERLIRQEAGMVFQQfylfPHLTAL--- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586061923 473 hELV--------------GEDRAETVpLGTFGLlAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK09493 96 -ENVmfgplrvrgaskeeAEKQAREL-LAKVGL-AER-AHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
416-531 |
1.44e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 416 ITGSNGVGKSTLLSLFARRLEPTRGSV--HAAPGVRVGLLDQDATLpGADPEHTAAHIYHELVGEDRA----------ET 483
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVliRGEPITKENIREVRKFV-GLVFQNPDDQIFSPTVEQDIAfgpinlgldeET 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 484 VP------LGTFGLLAGRDenRRVGELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK13652 114 VAhrvssaLHMLGLEELRD--RVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
405-535 |
1.55e-04 |
|
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: 42.53 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVGLLDQdatlpgadpehtaaHIYhelvgedraetV 484
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ--------------RPY-----------L 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 485 PLGTFgllagrdenRRV------GELSVGQRRRLALAVLLADPPHVLLLDEPTNHFS 535
Cdd:cd03223 76 PLGTL---------REQliypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
404-443 |
1.62e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.76 E-value: 1.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSVH 443
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
404-530 |
1.66e-04 |
|
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: 43.30 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV------------HAAPGVRVGLLDQDAT----LPGADPEHT 467
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmHKRARLGIGYLPQEASifrkLTVEENILA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586061923 468 AAHIYHELVGE--DRAETVpLGTFGLLAGRdeNRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03218 99 VLEIRGLSKKEreEKLEEL-LEEFHITHLR--KSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
270-310 |
1.67e-04 |
|
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: 40.63 E-value: 1.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1586061923 270 VTRFGGTYSQYVLARMDTRERWERTYRDEQAQLKKLRAAVR 310
Cdd:pfam12848 8 LTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFID 48
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-64 |
1.95e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 1.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1586061923 21 GISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAG 64
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
176-219 |
2.07e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 2.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1586061923 176 ALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATL 219
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
34-208 |
2.48e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 43.54 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 34 DISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGLGDPLR-------------VGLLYQEP--PFAPHDT 98
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV--AWLGKDLLgmkddewravrsdIQMIFQDPlaSLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 99 VAQAVESAVRTVRdaasavdrtadalaraPEdegaatayaaaldtaerIGAWDVDTRIDVTLDGLGLGGVDRDRSTGALS 178
Cdd:PRK15079 117 IGEIIAEPLRTYH----------------PK-----------------LSRQEVKDRVKAMMLKVGLLPNLINRYPHEFS 163
|
170 180 190
....*....|....*....|....*....|
gi 1586061923 179 GGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
45-208 |
2.60e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.32 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 45 TGLIGENGSGKSTLLRIVAGLRAPDAGEVRavgLGDPL---------------RVGLLYQEPPFAPHDTVAQAVESAVRT 109
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIV---LNGRVlfdaekgiclppekrRIGYVFQDARLFPHYKVRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 110 VRDAasavdrtadalarapedegaatayaaaldTAERIgawdvdtridVTLdgLGLGGVdRDRSTGALSGGQRSRLSLAW 189
Cdd:PRK11144 104 SMVA-----------------------------QFDKI----------VAL--LGIEPL-LDRYPGSLSGGEKQRVAIGR 141
|
170
....*....|....*....
gi 1586061923 190 LLLSTPDVLLLDEPTNHLD 208
Cdd:PRK11144 142 ALLTAPELLLMDEPLASLD 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
498-559 |
3.17e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 42.73 E-value: 3.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586061923 498 NRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAVPDYPG--TVLVASHD 559
Cdd:PRK14246 148 NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-244 |
3.62e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.55 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 28 SHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAVGLG------DPLRVGL-LYQEPPFAPHDTVA 100
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPltklqlDSWRSRLaVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 101 QAVE----SAVRTVRDAASAVDRTADALARAPEdegaatayaaaldtaerigawDVDTRIdvtldglGLGGVdrdrstgA 176
Cdd:PRK10789 407 NNIAlgrpDATQQEIEHVARLASVHDDILRLPQ---------------------GYDTEV-------GERGV-------M 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 177 LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSW--HGPVLLASHDRAFLDTAVTSLV 244
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWgeGRTVIISAHRLSALTEASEILV 521
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
403-542 |
3.68e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.47 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 403 PVSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-----------HAAPGVRVGLLDQDATlPGADPEHTAAHI 471
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdYSYRSQRIRMIFQDPS-TSLNPRQRISQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 472 YH-------ELVGEDRAETV--PLGTFGLLAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQL 542
Cdd:PRK15112 110 LDfplrlntDLEPEQREKQIieTLRQVGLLPDH-ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQL 188
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-73 |
3.81e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 3.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEV 73
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
24-64 |
4.93e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 4.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1586061923 24 ASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAG 64
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
47-202 |
5.08e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 47 LIGENGSGKSTLLRIVAGLRAPDAGEVravglgdplrvgLLYQEPpfaphdtVAQAVESAVRTVrdaASAVDRTADALAR 126
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEI------------LLDGKP-------VTAEQPEDYRKL---FSAVFTDFHLFDQ 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 127 APEDEGAATAYAAALDTAERIGAWDvdtriDVTLDGLGLggvdrdrSTGALSGGQRSRLSLAWLLLSTPDVLLLDE 202
Cdd:PRK10522 412 LLGPEGKPANPALVEKWLERLKMAH-----KLELEDGRI-------SNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
404-530 |
5.68e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV-------HAAPG---VRVGL--------LDQDAT----LPG 461
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgqhiEGLPGhqiARMGVvrtfqhvrLFREMTvienLLV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 462 ADPEHTAAHIYHELV---GEDRAET-------VPLGTFGLLAGrdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK11300 104 AQHQQLKTGLFSGLLktpAFRRAESealdraaTWLERVGLLEH--ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
498-530 |
6.02e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 42.38 E-value: 6.02e-04
10 20 30
....*....|....*....|....*....|...
gi 1586061923 498 NRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK10851 131 DRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
405-441 |
6.14e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 6.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 405 SLTVSAGESWLITGSNGVGKSTLLS---------------LFARRleptRGS 441
Cdd:PRK10938 280 SWQVNPGEHWQIVGPNGAGKSTLLSlitgdhpqgysndltLFGRR----RGS 327
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
404-531 |
7.04e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRG--SVHAAPGVRVGLLDQDATLP---------------GADP-- 464
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGriMIDDCDVAKFGLTDLRRVLSiipqspvlfsgtvrfNIDPfs 1334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586061923 465 EHTAAHIYHELVGEDRAETVPLGTFGLLAGRDENrrvGE-LSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEG---GEnFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-211 |
7.31e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 19 VSGISASyGSHrvltDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRavglgdplrvglLYQEP--PFAPH 96
Cdd:PRK10762 260 VDNLSGP-GVN----DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT------------LDGHEvvTRSPQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 97 DTVAQAVesavrtvrdAASAVDRTAD---------------ALARAPEDEGAATAYAAALDTAERIGAWDVDTRidvtld 161
Cdd:PRK10762 323 DGLANGI---------VYISEDRKRDglvlgmsvkenmsltALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTP------ 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586061923 162 glglggvDRDRSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAA 211
Cdd:PRK10762 388 -------SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
146-253 |
8.44e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.09 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 146 RIGawdVDTRIDVTLDgLGLGGVDRDRSTGALSGGQRSRLSLAWLLLSTPDVLL--LDEPTNHLDDAATDFLRATLRSW- 222
Cdd:cd03270 111 RVG---IRERLGFLVD-VGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLr 186
|
90 100 110
....*....|....*....|....*....|...
gi 1586061923 223 -HG-PVLLASHDRAFLDTAVTsLVDLDPAPRPH 253
Cdd:cd03270 187 dLGnTVLVVEHDEDTIRAADH-VIDIGPGAGVH 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
503-531 |
9.23e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 41.76 E-value: 9.23e-04
10 20
....*....|....*....|....*....
gi 1586061923 503 ELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPT 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-237 |
1.31e-03 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 40.82 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 19 VSGISASYGSHRVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRA--PDAGEV--------------RAvGLGdpl 82
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSIlldgedilelspdeRA-RAG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 83 rVGLLYQEPPFAPHDTVAQAVESAVRTVRDaasavdrtadalarapedegaatayaaaldtaERIGAWDVDTRIDVTLDG 162
Cdd:COG0396 79 -IFLAFQYPVEIPGVSVSNFLRTALNARRG--------------------------------EELSAREFLKLLKEKMKE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 163 LGLggvDRD---RSTGA-LSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD-DAatdfLRA------TLRSWHGPVLLASH 231
Cdd:COG0396 126 LGL---DEDfldRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDiDA----LRIvaegvnKLRSPDRGILIITH 198
|
....*.
gi 1586061923 232 DRAFLD 237
Cdd:COG0396 199 YQRILD 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-221 |
1.35e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 30 RVLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPD--AGEVRAVGLgdPLRvgllyQEPpFAPHDTVAQA--VES 105
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGF--PKK-----QET-FARISGYCEQndIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 106 AVRTVRDAAsavdrTADALARAPEDEGAATAYAAaldtaerigawdVDTRID-VTLDGL-----GLGGVdrdrsTGaLSG 179
Cdd:PLN03140 966 PQVTVRESL-----IYSAFLRLPKEVSKEEKMMF------------VDEVMElVELDNLkdaivGLPGV-----TG-LST 1022
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1586061923 180 GQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRS 221
Cdd:PLN03140 1023 EQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
492-530 |
1.59e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 40.86 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1586061923 492 LAGRdENRRVGELSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:PRK11432 126 LAGF-EDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
404-530 |
1.70e-03 |
|
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: 39.82 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFA--RRLEPTRGSVhaapgvrvgLLD-QDATlpgadpehtaahiyhELVGEDR 480
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEI---------LFKgEDIT---------------DLPPEER 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586061923 481 AEtvpLGTFglLA--------G---RDENRRVGE-LSVGQRRRLALAVLLADPPHVLLLDEP 530
Cdd:cd03217 75 AR---LGIF--LAfqyppeipGvknADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
502-544 |
2.17e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 2.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1586061923 502 GELSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEA 544
Cdd:PRK14247 145 GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIES 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
503-531 |
2.30e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 40.02 E-value: 2.30e-03
10 20
....*....|....*....|....*....
gi 1586061923 503 ELSVGQRRRLALAVLLADPPHVLLLDEPT 531
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
31-208 |
2.70e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVRAvglgdplrvgllyqEPPFAphdTVAQAVESAVRTV 110
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA--------------ERSIA---YVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 111 RDAASAVD-----RTADALaRAPEDEGaatayaaaldtaerigawdvdtriDVTLDGLGL------GGVDrdrstgaLSG 179
Cdd:PTZ00243 738 RGNILFFDeedaaRLADAV-RVSQLEA------------------------DLAQLGGGLeteigeKGVN-------LSG 785
|
170 180
....*....|....*....|....*....
gi 1586061923 180 GQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
404-531 |
2.75e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.40 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 404 VSLTVSAGESWLITGSNGVGKSTLLSLFARRLEPTRGSV------------HAAPGVRVGLLDQDATLPgadPEHTAAhi 471
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvrirspRDAIALGIGMVHQHFMLV---PNLTVA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 472 yhelvgedraETVPLG---TFGLLAGRDE------------------NRRVGELSVGQRRRLA-LAVLLADPPhVLLLDE 529
Cdd:COG3845 99 ----------ENIVLGlepTKGGRLDRKAararirelserygldvdpDAKVEDLSVGEQQRVEiLKALYRGAR-ILILDE 167
|
..
gi 1586061923 530 PT 531
Cdd:COG3845 168 PT 169
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
504-558 |
2.84e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 39.76 E-value: 2.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586061923 504 LSVGQRRRLALAVLLADPPHVLLLDEPTNHFSLVLATQLEAAV----PDYpgTVLVASH 558
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTR 205
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
167-237 |
3.21e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 3.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586061923 167 GVDRDRSTGALSGGQRSRLSLAWLLLST---PDVLLLDEPTNHLD-DAATDFLR--ATLRSWHGPVLLASHDRAFLD 237
Cdd:pfam13304 227 GGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHpKLLRRLLEllKELSRNGAQLILTTHSPLLLD 303
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
45-63 |
3.95e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 39.36 E-value: 3.95e-03
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
151-243 |
4.77e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 151 DVDTRIDVTLDGLGLG-GVDrdrstgALSGGQRS------RLSLAWLLLSTPDVLLLDEPTNHLDD----AATDFLRATL 219
Cdd:PRK01156 781 DVDQDFNITVSRGGMVeGID------SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEdrrtNLKDIIEYSL 854
|
90 100
....*....|....*....|....*.
gi 1586061923 220 RSWHG--PVLLASHDRAFLDTAVTSL 243
Cdd:PRK01156 855 KDSSDipQVIMISHHRELLSVADVAY 880
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
174-208 |
4.81e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|....*
gi 1586061923 174 TGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
172-208 |
7.69e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.95 E-value: 7.69e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1586061923 172 RSTGALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLD 208
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
31-85 |
9.26e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 37.73 E-value: 9.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586061923 31 VLTDISFSVTAGDPTGLIGENGSGKSTLLRIVAGLRAPDAGEVraVGL-GDPLRVG 85
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDF--IGLrGDALPLG 55
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
98-528 |
9.30e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 39.07 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 98 TVAQAVESAVRTVRDAASAVDRTADALARAPEDEGAATAYAAALDTAERIGAWDVDTRIDVTLDGLGLGGVDRDRSTGAL 177
Cdd:COG3899 11 AVARLRGLLLALAAALALLAAALLLLLLLALRLALLLLALALLLLLLLALLLLLALLLALLLLALLLLALALLRLLAAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 178 SGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAATDFLRATLRSWHGPVLLASHDRAFLDTAVTSLVDLDPAPRPHAVTS 257
Cdd:COG3899 91 LALLLALALALLAALLLLLALALLLLALLALALLALLLALLLAAGVLGLLLGGLLLAALAALLALAALAAAAAAAAAAAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 258 DLVGDGTGTGIGVTRFGGTYSQYVLARMDTRERWERTYRDEQAQLKKLRAAVREQQTVGHSGRSPKTEGRAAKKFYADRN 337
Cdd:COG3899 171 ARAARLRRARAARLAALALRALLLLVLLLLLLLLLLGLLLAAAAALAAAAAAAAAAAPAAPVVLVAALLLALAALLALLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 338 ATVVSRRVNGARARLATVEDEQIRKPPRELYFQGLTAGLSGSEAALHRtgpvLTASAAEVAGRmapvsltvsAGESWLIT 417
Cdd:COG3899 251 LAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGREAELAA----LLAALERARAG---------RGELVLVS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586061923 418 GSNGVGKSTLLSLFARRLEPTRGSVHAAPGVRVG----------LLDQDATLPGADPEHTAAHIYHELVGEDRAETVPLg 487
Cdd:COG3899 318 GEAGIGKSRLVRELARRARARGGRVLRGKCDQLErgvpyaplaqALRALLGQLPEDELAAWRARLLAALGANGRLLADL- 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1586061923 488 tFGLLAGRDENRRVGELSVGQRRRLA----LAVLLADPPHVLLLD 528
Cdd:COG3899 397 -LPELELQPAPPELDPEEARNRLFRAllrlLRALAAERPLVLVLD 440
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
175-211 |
9.54e-03 |
|
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: 38.65 E-value: 9.54e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1586061923 175 GALSGGQRSRLSLAWLLLSTPDVLLLDEPTNHLDDAA 211
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
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