|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
298-821 |
3.02e-134 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 409.84 E-value: 3.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 298 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRA------LSIPPNIDVLLCEQEVVADET-PAVQ 370
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELepdsgeVSIPKGLRIGYLPQEPPLDDDlTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 371 AVLRADTKRLRLLEEERRLQGQLEQGDDtAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRM 450
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDE-DLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 451 RVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKK 530
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 531 MYQQKQKELLKQYEkqekklkelkaggkstKQAEK--QTKEVLTR--------KQQKCRRKNQDE-ESQEPPellkrPKE 599
Cdd:COG0488 240 QRAERLEQEAAAYA----------------KQQKKiaKEEEFIRRfrakarkaKQAQSRIKALEKlEREEPP-----RRD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 600 YTVRFTFPDPPPLSPPVLGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHR 679
Cdd:COG0488 299 KTVEIRFPPPERLGKKVLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 680 LKIGFFNQQYaEQLHMEETPTEYLQR-SFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLIL 758
Cdd:COG0488 378 VKIGYFDQHQ-EELDPDKTVLDELRDgAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 759 DEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDYKR 821
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
256-821 |
3.99e-129 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 403.09 E-value: 3.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 256 QMDYERQVESLKAANAAENDFSVSQAEVSSRQAmlenASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKT 335
Cdd:PLN03073 142 EVQYQAHVAEMEAAKAGMPGVYVNHDGNGGGPA----IKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 336 TLLKHIANRALS-IPPNIDVLLCEQEVVADETPAVQAVLRAD--------------TKRLRLLEEERRLQGQLEQGD--- 397
Cdd:PLN03073 218 TFLRYMAMHAIDgIPKNCQILHVEQEVVGDDTTALQCVLNTDiertqlleeeaqlvAQQRELEFETETGKGKGANKDgvd 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 398 -DTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL 476
Cdd:PLN03073 298 kDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 477 NAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKKMYQQKQKELLKQYEKQEKKLKELKAG 556
Cdd:PLN03073 378 HAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAF 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 557 GKSTKQAEKQTKEVLTRKQQKCRRKNQDEESQEPpellkrpkEYTVRFTfPDPPPLSPPVLGLHGVTFGYEGQKPLFKNL 636
Cdd:PLN03073 458 IDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDP--------DYKFEFP-TPDDRPGPPIISFSDASFGYPGGPLLFKNL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 637 DFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETPTEYLQRSF-NLPYQDAR 715
Cdd:PLN03073 529 NFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFpGVPEQKLR 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 716 KCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLIT 795
Cdd:PLN03073 609 AHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLIS 688
|
570 580
....*....|....*....|....*.
gi 39930335 796 ETNCQLWVVEEQGVSQIDGDFDDYKR 821
Cdd:PLN03073 689 GSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
310-821 |
1.83e-76 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 260.87 E-value: 1.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 310 LFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANR------ALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLrll 383
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEisadggSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYR--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 384 eeerrlqgQLEQGDDTAAEK-----LEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARAL 458
Cdd:PRK10636 93 --------QLEAQLHDANERndghaIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 459 FMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKK-------- 530
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVqratrlaq 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 531 ---MYQQKQKEL--LKQYEKQEKklkelkagGKSTKQaekqtkevltrKQQKCRRKNQDEESQEPPELLKRPkeytVRFT 605
Cdd:PRK10636 245 qqaMYESQQERVahLQSYIDRFR--------AKATKA-----------KQAQSRIKMLERMELIAPAHVDNP----FHFS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 606 FPDPPPLSPPVLGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFF 685
Cdd:PRK10636 302 FRAPESLPNPLLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYF 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 NQQYAEQLHMEETPTEYLQR-SFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNN 764
Cdd:PRK10636 381 AQHQLEFLRADESPLQHLARlAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 765 LDIESIDALGEAINDYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDYKR 821
Cdd:PRK10636 461 LDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
308-819 |
3.51e-57 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 205.13 E-value: 3.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 308 KELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhIANRAL-------SIPPNIDVLLCEQEVVADETPAV-QAVLRADTKR 379
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMK-ILGGDLepsagnvSLDPNERLGKLRQDQFAFEEFTVlDTVIMGHTEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 380 LRLLEEERRLQGQLEQGDD---TAAEkLEKVYEELRATGAAAAEAKarrILAGLGFDPEMQNRPTQKFSGGWRMRVSLAR 456
Cdd:PRK15064 93 WEVKQERDRIYALPEMSEEdgmKVAD-LEVKFAEMDGYTAEARAGE---LLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 457 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFKKMYQQKQ 536
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQAR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 537 KELLKQYEKqekklkelkaggKSTKQAEKQTkeVLTR--------KQQKCRRKNQDEESQEPPELLKRPKEYtVRFTFPD 608
Cdd:PRK15064 249 ERLLADNAK------------KKAQIAELQS--FVSRfsanaskaKQATSRAKQIDKIKLEEVKPSSRQNPF-IRFEQDK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 609 PPPLSppVLGLHGVTFGYEGqKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQ 688
Cdd:PRK15064 314 KLHRN--ALEVENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 YAEQLHMEETPTEYLQ--RSFNLPYQDARKCLGR--FGLESHAHTIQICklSGGQKARVVFAELACREPDVLILDEPTNN 764
Cdd:PRK15064 391 HAYDFENDLTLFDWMSqwRQEGDDEQAVRGTLGRllFSQDDIKKSVKVL--SGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 765 LDIESIDALGEAINDYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDY 819
Cdd:PRK15064 469 MDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
310-809 |
5.78e-47 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 177.84 E-value: 5.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 310 LFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralsippniDVLLCEQEVVAdETPAVQAVLRADT-KRLRLLEEERR 388
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG---------EVLLDDGRIIY-EQDLIVARLQQDPpRNVEGTVYDFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 389 LQGQLEQGD-----------------DTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMqnrPTQKFSGGWRMR 451
Cdd:PRK11147 88 AEGIEEQAEylkryhdishlvetdpsEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 452 VSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYmtfkKM 531
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNY----DQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 532 YQQKQKELLKQyekqekklkelkaggKSTKQAEKQTK----EVLTRKQQKCRR----------KNQDEESQEppellKRP 597
Cdd:PRK11147 241 YLLEKEEALRV---------------EELQNAEFDRKlaqeEVWIRQGIKARRtrnegrvralKALRRERSE-----RRE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 598 KEYTVRFTFPDPPPLSPPVLGLHGVTFGYEGqKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN 677
Cdd:PRK11147 301 VMGTAKMQVEEASRSGKIVFEMENVNYQIDG-KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 678 HRLKIGFFNqQYAEQLHMEETPTE--------------------YLQrSFNLPYQDARkclgrfgleshahtIQICKLSG 737
Cdd:PRK11147 380 TKLEVAYFD-QHRAELDPEKTVMDnlaegkqevmvngrprhvlgYLQ-DFLFHPKRAM--------------TPVKALSG 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 738 GQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLITETNCQLWVVEEQGV 809
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGK 515
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
307-836 |
1.24e-46 |
|
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: 175.51 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 307 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA------NRALSIPPNIDVLLCEQEVVADETPAVQAVLR---ADT 377
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvdkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEegvAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 378 KRLRLLEEERRLQGQLEQGD-DTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQnrPTQKFSGGWRMRVSLAR 456
Cdd:TIGR03719 97 KDALDRFNEISAKYAEPDADfDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDA--DVTKLSGGERRRVALCR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 457 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTF-----KKM 531
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWleqkqKRL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 532 YQQKQKE--LLKQYEKQEKKLKELKAGGKSTKQAEKQTKEVLTRKQQKcrRKNQDEESQEPP-ELLkrpkeytvrftfpd 608
Cdd:TIGR03719 255 EQEEKEEsaRQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQ--KRNETAEIYIPPgPRL-------------- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 609 ppplSPPVLGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQ 688
Cdd:TIGR03719 319 ----GDKVIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 YAeqlHMEETPTEYLQRSFNLPYQD-------ARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEP 761
Cdd:TIGR03719 394 RD---ALDPNKTVWEEISGGLDIIKlgkreipSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 762 TNNLDIESIDALGEAINDYKGAVIVVSHDA----RLITEtncqlwVVEEQGVSQI---DGDFDDYKREVLEALGEVMVNR 834
Cdd:TIGR03719 471 TNDLDVETLRALEEALLNFAGCAVVISHDRwfldRIATH------ILAFEGDSHVewfEGNFSEYEEDKKRRLGEDADQP 544
|
..
gi 39930335 835 PR 836
Cdd:TIGR03719 545 HR 546
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
296-517 |
2.50e-46 |
|
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: 162.23 E-value: 2.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVllceqevvadetpavqavlra 375
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 dtkrlrlleEERRLQGQLEQgddtaaeklekvyeelratgaaaaeakarrilaglgfdpemqnrptqkFSGGWRMRVSLA 455
Cdd:cd03221 60 ---------GSTVKIGYFEQ------------------------------------------------LSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 456 RALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQR 517
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
619-808 |
1.05e-40 |
|
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: 146.05 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGqKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQqyaeqlhmeet 698
Cdd:cd03221 3 LENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 699 pteylqrsfnlpyqdarkclgrfgleshahtiqickLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIN 778
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 39930335 779 DYKGAVIVVSHDARLITETNCQLWVVEEQG 808
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
260-525 |
4.04e-37 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 146.75 E-value: 4.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 260 ERQVESLKAANAAEND----FSVSQAEVSSRQAmlenasdIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKT 335
Cdd:COG0488 283 IKALEKLEREEPPRRDktveIRFPPPERLGKKV-------LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 336 TLLKHIANR------ALSIPPNIDVLLCEQEvvadetpavQAVLRADtkrlrlleeerrlqgqleqgddtaaeklEKVYE 409
Cdd:COG0488 356 TLLKLLAGElepdsgTVKLGETVKIGYFDQH---------QEELDPD----------------------------KTVLD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 410 ELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGW 489
Cdd:COG0488 399 ELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
250 260 270
....*....|....*....|....*....|....*.
gi 39930335 490 RKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNY 525
Cdd:COG0488 479 PGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGY 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
325-790 |
1.92e-35 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 142.18 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 325 GLVGPNGKGKTTLLKHIA------NRALSIPPNIDVLLCEQEVVADETPAV-----QAVlrADTKRlrlleeerrlqgql 393
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAgvdkefEGEARPAPGIKVGYLPQEPQLDPEKTVrenveEGV--AEVKA-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 394 eqgddtAAEKLEKVYEELRATGAAAAE------AKARRILAGLGFDPEMQ-------------NRPTQKFSGGWRMRVSL 454
Cdd:PRK11819 101 ------ALDRFNEIYAAYAEPDADFDAlaaeqgELQEIIDAADAWDLDSQleiamdalrcppwDAKVTKLSGGERRRVAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 455 ARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYYRGNYMTFkkmYQQ 534
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSW---LEQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 535 KQKELLKQyekqekklKELKAGGKSTKQAE----------KQTK---------EVLTRKQQKcrrKNQDEESQEPP-ELL 594
Cdd:PRK11819 252 KAKRLAQE--------EKQEAARQKALKRElewvrqspkaRQAKskarlaryeELLSEEYQK---RNETNEIFIPPgPRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 595 krpkeytvrftfpdppplSPPVLGLHGVTFGYeGQKPLFKNLDF-----GIdmdsrICIVGPNGVGKSTLLLLLTGKLTP 669
Cdd:PRK11819 321 ------------------GDKVIEAENLSKSF-GDRLLIDDLSFslppgGI-----VGIIGPNGAGKSTLFKMITGQEQP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 670 TNGEMRKNHRLKIGFFNQQYAeqlHMEETPT---------EYLQ---RSFNlpyqdARKCLGRFGLESHAHTIQICKLSG 737
Cdd:PRK11819 377 DSGTIKIGETVKLAYVDQSRD---ALDPNKTvweeisgglDIIKvgnREIP-----SRAYVGRFNFKGGDQQKKVGVLSG 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 39930335 738 GQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHD 790
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
296-518 |
1.21e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.06 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLsIPPNI-DVLLCEQEVvaDETPAVQ---- 370
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD--L-DPPTSgEIYLDGKPL--SAMPPPEwrrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 371 -AVLRADTkrlrlleeerrlqgQLeqGDDTAAEKLEKVYEelrATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWR 449
Cdd:COG4619 76 vAYVPQEP--------------AL--WGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPDILDKPVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 450 MRVSLARALFMEPTLLMLDEPTNHLDLN---AVI-WLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPEntrRVEeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
297-514 |
3.46e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 99.63 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 297 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVVADETPAVQAvlrad 376
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG--LLKPTSGEILIDGKDIAKLPLEELRR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 377 tkrlrlleeerrlqgqleqgddtaaeklekvyeelratgaaaaeakarrilaGLGFDPEMqnrptqkfSGGWRMRVSLAR 456
Cdd:cd00267 74 ----------------------------------------------------RIGYVPQL--------SGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 457 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLK 154
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
616-797 |
1.78e-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: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKS---------TLLLLltgkltptnGEMRKNHRlKIGFFN 686
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTtllrilaglLPPSA---------GEVLWNGE-PIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 687 QQYAEQLHM---------EETPTEYLQ-----RSFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACRE 752
Cdd:COG4133 71 EDYRRRLAYlghadglkpELTVRENLRfwaalYGLRADREAIDEALEAVGLAGLADL-PVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 39930335 753 PDVLILDEPTNNLDIESIDALGEAINDYK---GAVIVVSHDARLITET 797
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
296-520 |
6.51e-23 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 98.39 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAVQAVLra 375
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG---LLKPDSGSILIDGEDVRKEPREARRQI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 dtkrlrlleeerrlqGQLEQG----DDTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMqNRPTQKFSGGWRMR 451
Cdd:COG4555 77 ---------------GVLPDErglyDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 452 VSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLDTQRLHY 520
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkegKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
619-790 |
2.36e-22 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 96.00 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYE-GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-----------KNHRLKIGF-F 685
Cdd:cd03225 2 LKNLSFSYPdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdltklslKELRRKVGLvF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 nqQYAE-QLHMEeTPTEYL---QRSFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLI 757
Cdd:cd03225 82 --QNPDdQFFGP-TVEEEVafgLENLGLPEEEIEErveeALELVGLEGLRDR-SPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 39930335 758 LDEPTNNLDIESIDALGEAINDYKGA---VIVVSHD 790
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHD 193
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
616-790 |
2.72e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 96.70 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKStlllllt------gkltptNGEMRKNHRLKIGFFNQQY 689
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKStllkailgllpptsgtvrlFGKPPRRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 AEQLHMEETPTE------YLQRSFNLPY-----QDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLIL 758
Cdd:COG1121 85 EVDWDFPITVRDvvlmgrYGRRGLFRRPsradrEAVDEALERVGLEDLADR-PIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 39930335 759 DEPTNNLDIESIDALGEAINDYKG---AVIVVSHD 790
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRRegkTILVVTHD 198
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
619-796 |
5.13e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 95.48 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKStllllltgkltptNG------------------EMRKNHRL 680
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKStll-------rllNGllkptsgevlvdgkditkKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 681 KIGF-FnqQYAE-QLHM----EE----------TPTEYLQRsfnlpyqdARKCLGRFGLESHAHTiQICKLSGGQKARVV 744
Cdd:COG1122 76 KVGLvF--QNPDdQLFAptveEDvafgpenlglPREEIRER--------VEEALELVGLEHLADR-PPHELSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 745 FAE-LACrEPDVLILDEPTNNLDIESIDALGEAINDYKGA---VIVVSHDARLITE 796
Cdd:COG1122 145 IAGvLAM-EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAE 199
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
313-514 |
7.91e-22 |
|
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: 93.23 E-value: 7.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVVADETPAVQAVlradtkrlrlleeerrlqGQ 392
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKPDSGEIKVLGKDIKKEPEEVKRRI------------------GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 LEQGDdtaaeklekvyeelratgaaaaeakarrilaglGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTN 472
Cdd:cd03230 78 LPEEP---------------------------------SLYENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 39930335 473 HLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:cd03230 125 GLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILN 169
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
619-796 |
5.97e-21 |
|
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: 91.83 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR------KNHRLKIGFFNQQyaeq 692
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 693 lhmEETPTE-------------YLQRSFNLPYQDARKC-----LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPD 754
Cdd:cd03235 77 ---RSIDRDfpisvrdvvlmglYGHKGLFRRLSKADKAkvdeaLERVGLSELADR-QIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 39930335 755 VLILDEPTNNLDIESIDALGEAINDYKG---AVIVVSHDARLITE 796
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLE 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
313-511 |
2.85e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 90.51 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVVADETPAVQAVlradtkrlrlleeerrlqGQ 392
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG--LLRPTSGEVRVLGEDVARDPAEVRRRI------------------GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 LEQGDD-----TAAEKLEkVYEELRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLML 467
Cdd:COG1131 78 VPQEPAlypdlTVRENLR-FFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 39930335 468 DEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDqgfLDDV---CTDII 511
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAaegKTVLLSTHY---LEEAerlCDRVA 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
296-806 |
2.97e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 95.36 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFV--NADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVllcEQEVVADETPAVQAVL 373
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPHGGRI---SGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 374 RADTKRLrlleeerrlqGQLEQGDDTA----------AEKLekvyeELRATGAAAAEAKARRILAGLGFDPEMQNRPTQk 443
Cdd:COG1123 79 ALRGRRI----------GMVFQDPMTQlnpvtvgdqiAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPHQ- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIWLNNYLQGWR-KTLLIVSHDQGFLDDVCTDIIHLDTQRLh 519
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRI- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 520 yyrgnymtfkkmyqqkqkellkqyekqekklkelkaggkstkQAEKQTKEVLTRkqqkcrrknqdeesqePPELLKRPKE 599
Cdd:COG1123 222 ------------------------------------------VEDGPPEEILAA----------------PQALAAVPRL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 600 YTVRFTFPDPPPLSPPVLGLHGVTFGYEGQKP-LFKNLDfGIDMD----SRICIVGPNGVGKS----------------- 657
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKgGVRAVD-DVSLTlrrgETLGLVGESGSGKStlarlllgllrptsgsi 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 658 -TLLLLLTGKLTPTNGEMRK-------------NHRLKIGffnQQYAE--QLHMEETPTEYLQRsfnlpyqdARKCLGRF 721
Cdd:COG1123 323 lFDGKDLTKLSRRSLRELRRrvqmvfqdpysslNPRMTVG---DIIAEplRLHGLLSRAERRER--------VAELLERV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 722 GLESHA-----HTiqickLSGGQKARVVFAE-LACrEPDVLILDEPTNNLDIeSI-----DALGEAINDYKGAVIVVSHD 790
Cdd:COG1123 392 GLPPDLadrypHE-----LSGGQRQRVAIARaLAL-EPKLLILDEPTSALDV-SVqaqilNLLRDLQRELGLTYLFISHD 464
|
570
....*....|....*.
gi 39930335 791 arlitetncqLWVVEE 806
Cdd:COG1123 465 ----------LAVVRY 470
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
619-806 |
3.68e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 89.49 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN-----------HRLKIGFFNQ 687
Cdd:COG4619 3 LEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgkplsampppeWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 688 QyaEQLhMEETPTEYLQRSFNL-----PYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPT 762
Cdd:COG4619 82 E--PAL-WGGTVRDNLPFPFQLrerkfDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 39930335 763 NNLDIESIDALGEAINDYK----GAVIVVSHDARLITETNCQLWVVEE 806
Cdd:COG4619 159 SALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
619-790 |
5.18e-20 |
|
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: 88.26 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltptngemrknhrLKI--GFFNQQyAEQLHME 696
Cdd:cd03214 2 VENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTL--------------------LKTlaGLLKPS-SGEILLD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 697 ETPTEYLQRSfnlpyQDARK------CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESI 770
Cdd:cd03214 60 GKDLASLSPK-----ELARKiayvpqALELLGLAHLADR-PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180
....*....|....*....|....
gi 39930335 771 DALGEAINDYKG----AVIVVSHD 790
Cdd:cd03214 134 IELLELLRRLARergkTVVMVLHD 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
313-472 |
1.32e-19 |
|
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: 86.16 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQAVLradtkrlrlleeerrlqGQ 392
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIA--GLLSPTEGTILLDGQDLTDDERKSLRKEI-----------------GY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 LEQGDD-----TAAEKLeKVYEELRATGAAAAEAKARRILAGLG---FDPEMQNRPTQKFSGGWRMRVSLARALFMEPTL 464
Cdd:pfam00005 64 VFQDPQlfprlTVRENL-RLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKL 142
|
....*...
gi 39930335 465 LMLDEPTN 472
Cdd:pfam00005 143 LLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
619-796 |
2.04e-19 |
|
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: 87.31 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM--------RKNHRLKIGFFNQQYA 690
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikAKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 691 EQLHMEETPTEYLQRSFNLP--YQDARKCLGRFGL----ESHAHTiqickLSGGQKARVVFAELACREPDVLILDEPTNN 764
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDagNEQAETVLKDLDLyalkERHPLS-----LSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190
....*....|....*....|....*....|....*
gi 39930335 765 LDIESIDALGEAINDYKG---AVIVVSHDARLITE 796
Cdd:cd03226 157 LDYKNMERVGELIRELAAqgkAVIVITHDYEFLAK 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
296-520 |
1.70e-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: 85.46 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAvqavLR 374
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN--GLLKPTSGEVLVDGKDITKKNLRE----LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 375 ---------ADTkrlrlleeerrlqgQL-----EqgDDTA----------AEKLEKVYEelratgaaaaeakarrILAGL 430
Cdd:COG1122 75 rkvglvfqnPDD--------------QLfaptvE--EDVAfgpenlglprEEIRERVEE----------------ALELV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 431 GFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVC 507
Cdd:COG1122 123 GLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELA 201
|
250
....*....|...
gi 39930335 508 TDIIHLDTQRLHY 520
Cdd:COG1122 202 DRVIVLDDGRIVA 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
301-514 |
2.20e-18 |
|
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: 84.44 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 301 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADET-------------P 367
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN--GLLGPTSGEVLVDGKDLTKLSLkelrrkvglvfqnP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 368 AVQAVlrADTkrlrlleeerrlqgqleqgddtaaeklekVYEEL------RATGAAAAEAKARRILAGLGFDpEMQNRPT 441
Cdd:cd03225 85 DDQFF--GPT-----------------------------VEEEVafglenLGLPEEEIEERVEEALELVGLE-GLRDRSP 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 442 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:cd03225 133 FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
616-790 |
3.36e-18 |
|
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: 85.10 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR---KN-HRL-------KIGF 684
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlASLsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 685 FNQQY--AEQLHMEE------TPteYLQRSFNLPYQD---ARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREP 753
Cdd:COG1120 80 VPQEPpaPFGLTVRElvalgrYP--HLGLFGRPSAEDreaVEEALERTGLEHLADR-PVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 39930335 754 DVLILDEPTNNLDI----ESIDALgEAINDYKG-AVIVVSHD 790
Cdd:COG1120 157 PLLLLDEPTSHLDLahqlEVLELL-RRLARERGrTVVMVLHD 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
296-520 |
4.04e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.76 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLsIPP---NIDVLLCE-------------Q 359
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG--L-LPPtsgTVRLFGKPprrarrrigyvpqR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 360 EVVADETPA-VQAVLRAdtkrlrLLEEERRLQGQLEQGDDTAAEK-LEKVyeelratgaaaaeakarrilaGLGfdpEMQ 437
Cdd:COG1121 84 AEVDWDFPItVRDVVLM------GRYGRRGLFRRPSRADREAVDEaLERV---------------------GLE---DLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:COG1121 134 DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGAVREYFDRVLLLN 213
|
....*.
gi 39930335 515 TQRLHY 520
Cdd:COG1121 214 RGLVAH 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
297-499 |
5.89e-18 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 82.48 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 297 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnRALSiPPNIDVLLCEQEVvADETPAVQAVLRAd 376
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLK-PSSGEILLDGKDL-ASLSPKELARKIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 377 tkrlrlleeeRRLQgQLEQGDdtAAEKLEKVYEELratgaaaaeakarrilaglgfdpemqnrptqkfSGGWRMRVSLAR 456
Cdd:cd03214 77 ----------YVPQ-ALELLG--LAHLADRPFNEL---------------------------------SGGERQRVLLAR 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 39930335 457 ALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHD 499
Cdd:cd03214 111 ALAQEPPILLLDEPTSHLDIAHQIELLELLRRLArergKTVVMVLHD 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
619-794 |
8.45e-18 |
|
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: 81.14 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltptngemrknhrLK-IGFFNQQYAEQLHMEE 697
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTL--------------------LRaIAGLLKPTSGEILIDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 698 TPTEylqrsfNLPYQDARKCLG-RFGLeshahtiqicklSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEA 776
Cdd:cd00267 61 KDIA------KLPLEELRRRIGyVPQL------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180
....*....|....*....|.
gi 39930335 777 INDYKG---AVIVVSHDARLI 794
Cdd:cd00267 123 LRELAEegrTVIIVTHDPELA 143
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
296-514 |
8.61e-18 |
|
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: 82.53 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNI-DVLLCEQEVVADETPAVQAV 372
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLL-----RILAglLPPSAgEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 L----RADTKrlrlleeerrlqGQLeqgddTAAEKLE---KVYEelratgAAAAEAKARRILAGLGFDPeMQNRPTQKFS 445
Cdd:COG4133 78 AylghADGLK------------PEL-----TVRENLRfwaALYG------LRADREAIDEALEAVGLAG-LADLPVRQLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 446 GGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVctDIIHLD 514
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELAAA--RVLDLG 203
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
295-518 |
1.63e-17 |
|
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: 83.33 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 295 DIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAVQAVLR 374
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAG---ALRPDAGTVDLAGVDLHGLSRRARARRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 375 AdtkrlrlleeerrlqgQLEQGDDTAA--EKLEKV------YEELRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSG 446
Cdd:TIGR03873 78 A----------------LVEQDSDTAVplTVRDVValgripHRSLWAGDSPHDAAVVDRALARTELS-HLADRDMSTLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 447 GWRMRVSLARALFMEPTLLMLDEPTNHLDLNA---VIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:TIGR03873 141 GERQRVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
619-790 |
2.80e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 82.03 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKStlllllt------gkltptNGE-MRKNH---RLKIGFFNQQ 688
Cdd:COG1131 3 VRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTttirmllgllrptsgevrvLGEdVARDPaevRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 YAeqLHMEETPTEYLQ---RSFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVvfaELAC---REPDVLIL 758
Cdd:COG1131 82 PA--LYPDLTVRENLRffaRLYGLPRKEARErideLLELFGLTDAADR-KVGTLSGGMKQRL---GLALallHDPELLIL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 39930335 759 DEPTNNLDIESIDALGEAINDYKG---AVIVVSHD 790
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
296-499 |
5.35e-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: 81.63 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNI-DVLLCEQE-------------- 360
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG---LLKPSSgEVLLDGRDlaslsrrelarria 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 361 VVADETPAV------QAVLRADTkrlrlleEERRLQGQLEQGDDTAAEK-LEKVyeelratgaaaaeakarrilaGLGfd 433
Cdd:COG1120 79 YVPQEPPAPfgltvrELVALGRY-------PHLGLFGRPSAEDREAVEEaLERT---------------------GLE-- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 434 pEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHD 499
Cdd:COG1120 129 -HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArergRTVVMVLHD 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
619-797 |
6.04e-17 |
|
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: 81.06 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDmDSRI-CIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN----------HRLKIGFFNQ 687
Cdd:COG4555 4 VENLSKKY-GKVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkepreARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 688 QYAeqLHMEETPTEYLQ---RSFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDE 760
Cdd:COG4555 82 ERG--LYDRLTVRENIRyfaELYGLFDEELKKrieeLIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 39930335 761 PTNNLDIESIDALGEAINDYKG---AVIVVSHDARLITET 797
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEAL 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
284-525 |
6.82e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 84.56 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 284 SSRQ----------AMLENAsdIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPP--- 350
Cdd:PRK15064 300 SSRQnpfirfeqdkKLHRNA--LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE---LEPdsg 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 351 ------NIDVLLCEQEVVADetpavqavlradtKRLRLLEEERRLQGQLEQGDDTAAEklekvyeelratgaaaaeakar 424
Cdd:PRK15064 375 tvkwseNANIGYYAQDHAYD-------------FENDLTLFDWMSQWRQEGDDEQAVR---------------------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 425 RILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLD 504
Cdd:PRK15064 420 GTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVS 499
|
250 260
....*....|....*....|.
gi 39930335 505 DVCTDIIHLDTQRLHYYRGNY 525
Cdd:PRK15064 500 SLATRIIEITPDGVVDFSGTY 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
619-794 |
5.66e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 82.31 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQ----------- 687
Cdd:PRK11147 6 IHGAWLSF-SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegtvy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 688 ---------------QYAEQLHMEETptEYLQRSFN--------LPYQDA-------RKCLGRFGLESHAhtiQICKLSG 737
Cdd:PRK11147 85 dfvaegieeqaeylkRYHDISHLVET--DPSEKNLNelaklqeqLDHHNLwqlenriNEVLAQLGLDPDA---ALSSLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 738 GQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLI 794
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFI 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
301-514 |
6.27e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 78.31 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 301 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNidvllcEQEVVADETPAVQAVLRADTK 378
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLL-----RALAglERPW------SGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 379 rlrlleeerrlQGQLEQGDDTAA----EKLEKVYEE-LRATGAAAAEAKARRILAGLGFDPEMQNR-PTQkFSGGWRMRV 452
Cdd:COG1124 80 -----------RVQMVFQDPYASlhprHTVDRILAEpLRIHGLPDREERIAELLEQVGLPPSFLDRyPHQ-LSGGQRQRV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 453 SLARALFMEPTLLMLDEPTNHLDLN--AVIWlnNYLQGWRK----TLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSvqAEIL--NLLKDLREerglTYLFVSHDLAVVAHLCDRVAVMQ 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
296-518 |
9.31e-16 |
|
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: 76.87 E-value: 9.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPPNIDVLLCEQEVVADETPAVQAVlra 375
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL---IKPDSGEITFDGKSYQKNIEALRRI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 dtkrlrlleeerrlqGQLEQ-----GDDTAAEKLEkvyeeLRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRM 450
Cdd:cd03268 75 ---------------GALIEapgfyPNLTARENLR-----LLARLLGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 451 RVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
619-790 |
2.04e-15 |
|
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: 79.98 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQyaEQLHMEET 698
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQE--PQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 699 PTE-----------YLQR------SFNLPYQDARKCLGRFG-----LESH-AHTIQ------------------ICKLSG 737
Cdd:TIGR03719 85 VREnveegvaeikdALDRfneisaKYAEPDADFDKLAAEQAelqeiIDAAdAWDLDsqleiamdalrcppwdadVTKLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 39930335 738 GQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHD 790
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
297-521 |
2.83e-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: 75.65 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 297 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA---------------------NRA------LSIP 349
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllkptsgsirvfgkplekerKRIgyvpqrRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 350 PN--IDVLlceqEVVAdetpavqavLRADTKRLRlleeerrlQGQLEQGDDTAA-EKLEKVyeelratgaaaaeakarri 426
Cdd:cd03235 81 RDfpISVR----DVVL---------MGLYGHKGL--------FRRLSKADKAKVdEALERV------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 427 laGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFL 503
Cdd:cd03235 121 --GLS---ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLV 195
|
250
....*....|....*...
gi 39930335 504 DDVCTDIIHLDtQRLHYY 521
Cdd:cd03235 196 LEYFDRVLLLN-RTVVAS 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
296-514 |
3.51e-15 |
|
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: 74.15 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLlCEQEVVADETPAVQAvLRA 375
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA--GLEEPDSGSIL-IDGEDLTDLEDELPP-LRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 DTkrlrlleEERRLQGQLEQGDdTAAEKlekvyeelratgaaaaeakarrILAGLgfdpemqnrptqkfSGGWRMRVSLA 455
Cdd:cd03229 77 RI-------GMVFQDFALFPHL-TVLEN----------------------IALGL--------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 456 RALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQaqlgITVVLVTHDLDEAARLADRVVVLR 175
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
625-801 |
3.82e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.58 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 625 GYEGQkPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQ----LHMEETPT 700
Cdd:NF040873 1 GYGGR-PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPdslpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 701 EYLQRSFNL---PYQDAR----KCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDAL 773
Cdd:NF040873 80 MGRWARRGLwrrLTRDDRaavdDALERVGLADLAGR-QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|.
gi 39930335 774 GEAINDYKG---AVIVVSHDARLITETNCQL 801
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHDLELVRRADPCV 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
296-500 |
4.82e-15 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 74.86 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQeVVADETPAVQAVlra 375
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA--GLERPDSGEILIDGR-DVTGVPPERRNI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 dtkrlrlleeerrlqGQLEQGDD-----TAAE------KLEKVYEElratgaaAAEAKARRILAGLGFDPEMQNRPTQkF 444
Cdd:cd03259 75 ---------------GMVFQDYAlfphlTVAEniafglKLRGVPKA-------EIRARVRELLELVGLEGLLNRYPHE-L 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQ 500
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQ 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
619-790 |
1.25e-14 |
|
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: 72.43 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKS----------TLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQ 688
Cdd:cd03230 3 VRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTtlikiilgllKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 YAEQLHMeeTPTEYLqrsfnlpyqdarkclgrfgleshahtiqicKLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 768
Cdd:cd03230 82 PSLYENL--TVRENL------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180
....*....|....*....|....*
gi 39930335 769 SIDALGEAINDYK---GAVIVVSHD 790
Cdd:cd03230 130 SRREFWELLRELKkegKTILLSSHI 154
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
633-763 |
1.51e-14 |
|
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: 71.53 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 633 FKNLDFGIDMDSRICIVGPNGVGKS-----------TLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQyaEQLHMEETPTE 701
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKStllkliagllsPTEGTILLDGQDLTDDERKSLRKEIGYVFQD--PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 702 YLQRSFNLPYQDARKC-------LGRFGLESHAHTI---QICKLSGGQKARVVFAELACREPDVLILDEPTN 763
Cdd:pfam00005 79 NLRLGLLLKGLSKREKdaraeeaLEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
621-793 |
4.51e-14 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 72.14 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 621 GVTFGYEGQK---PLFKNLDFGIDMDSRICIVGPNGVGKS---------------TLLLLLTGKLTPTNGEMRKNHRLKI 682
Cdd:cd03255 5 NLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKStllnilggldrptsgEVRVDGTDISKLSEKELAAFRRRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 683 GFFNQQYA--------EQLhmeETPTEYLQRSFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAE-LACrEP 753
Cdd:cd03255 85 GFVFQSFNllpdltalENV---ELPLLLAGVPKKERRERAEELLERVGLGDRLNH-YPSELSGGQQQRVAIARaLAN-DP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 39930335 754 DVLILDEPTNNLDIES----IDALGEaINDYKG-AVIVVSHDARL 793
Cdd:cd03255 160 KIILADEPTGNLDSETgkevMELLRE-LNKEAGtTIVVVTHDPEL 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
616-818 |
5.61e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 75.32 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGY-EGQKPLFKNLDFGIDMDSRICIVGPNGVGKS---TLLLLLTGKLTPTNGEMRKNHR-----------L 680
Cdd:COG1123 4 LLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKStlaLALMGLLPHGGRISGEVLLDGRdllelsealrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 681 KIGFFNQQYAEQLHM---EETPTEYLqRSFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREP 753
Cdd:COG1123 84 RIGMVFQDPMTQLNPvtvGDQIAEAL-ENLGLSRAEARArvleLLEAVGLERRLDR-YPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 754 DVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSHDARLITETnCQLWVVEEQGVSQIDGDFDD 818
Cdd:COG1123 162 DLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEI-ADRVVVMDDGRIVEDGPPEE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
313-511 |
6.23e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 75.32 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLsIPP--------NIDVLLCEQEVVADETPAVQAV------------ 372
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLG--L-LRPtsgsilfdGKDLTKLSRRSLRELRRRVQMVfqdpysslnprm 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 ---------LRAdtkrlrlleeerrlqgqleQGDDTAAEKLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQK 443
Cdd:COG1123 360 tvgdiiaepLRL-------------------HGLLSRAERRERVAE----------------LLERVGLPPDLADRYPHE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIwlnNYLQGWRK----TLLIVSHDQGFLDDVCTDII 511
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqAQIL---NLLRDLQRelglTYLFISHDLAVVRYIADRVA 476
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
619-808 |
1.32e-13 |
|
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: 69.33 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRknhrlkigfFNQQYAEQLhmee 697
Cdd:cd03228 3 FKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL---------IDGVDLRDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 698 tPTEYLQRSFNLPYQDARkclgRFgleshAHTIQ--IckLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGE 775
Cdd:cd03228 70 -DLESLRKNIAYVPQDPF----LF-----SGTIRenI--LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*
gi 39930335 776 AINDYKG--AVIVVSHdaRLITETNCQLWVVEEQG 808
Cdd:cd03228 138 ALRALAKgkTVIVIAH--RLSTIRDADRIIVLDDG 170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
315-520 |
1.78e-13 |
|
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: 70.47 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 315 DLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAVQAVLradtkrlrlleeerrlqGQLE 394
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAG---LLEPDAGFATVDGFDVVKEPAEARRRL-----------------GFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 395 QGDD-----TAAEKLEkVYEELRATGAAAAEAKARRILAGLGFDPEMqNRPTQKFSGGWRMRVSLARALFMEPTLLMLDE 469
Cdd:cd03266 85 DSTGlydrlTARENLE-YFAGLYGLKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 39930335 470 PTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHLDTQRLHY 520
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRalgKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
619-793 |
3.40e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 69.69 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGY---EGQKPLFKNLDFGIDMDSRICIVGPNGVGKStlllllt------gkltptNG------------EMRKN 677
Cdd:COG1136 7 LRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllnilggldrptsgevliDGqdisslserelaRLRRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 678 HrlkIGF-FnQQY--------AEQLHMeetPTEYLQRSFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAE- 747
Cdd:COG1136 87 H---IGFvF-QFFnllpeltaLENVAL---PLLLAGVSRKERRERARELLERVGLGDRLDH-RPSQLSGGQQQRVAIARa 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 39930335 748 LACRePDVLILDEPTNNLDIES----IDALGEAINDYKGAVIVVSHDARL 793
Cdd:COG1136 159 LVNR-PKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPEL 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
619-794 |
5.60e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.93 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltptngemrknhrLKIgffnqqyaeqLHMEET 698
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTL--------------------LKL----------LYGEER 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 699 PTE-------------------YLQRSFNLPYQD------------------------------ARKCLGRFGLESHAHT 729
Cdd:COG2884 54 PTSgqvlvngqdlsrlkrreipYLRRRIGVVFQDfrllpdrtvyenvalplrvtgksrkeirrrVREVLDLVGLSDKAKA 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 730 --IQickLSGGQKARVVFAelacR----EPDVLILDEPTNNLDIES----IDALgEAINDYKGAVIVVSHDARLI 794
Cdd:COG2884 134 lpHE---LSGGEQQRVAIA----RalvnRPELLLADEPTGNLDPETsweiMELL-EEINRRGTTVLIATHDLELV 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
628-797 |
6.20e-13 |
|
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: 68.15 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRlKIGFFNQQYAEQLHM---------EET 698
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-PLAEQRDEPHENILYlghlpglkpELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 699 PTEYLQ--RSFNLPYQ-DARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGE 775
Cdd:TIGR01189 90 ALENLHfwAAIHGGAQrTIEDALAAVGLTGFEDLP-AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170 180
....*....|....*....|....*
gi 39930335 776 AINDY---KGAVIVVSHDARLITET 797
Cdd:TIGR01189 169 LLRAHlarGGIVLLTTHQDLGLVEA 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
624-813 |
6.36e-13 |
|
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: 68.86 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 624 FGYEGQKPLFK-NLDFGIDmDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRL---------------KIGFFNQ 687
Cdd:cd03297 4 VDIEKRLPDFTlKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 688 QYAEQLHME--ETPTEYLQRSFNLPYQD-ARKCLGRFGLES--HAHTIQickLSGGQKARVVFAELACREPDVLILDEPT 762
Cdd:cd03297 83 QYALFPHLNvrENLAFGLKRKRNREDRIsVDELLDLLGLDHllNRYPAQ---LSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 763 NNLDIES----IDALGEAINDYKGAVIVVSHD---ARLITETncqLWVVEEQGVSQID 813
Cdd:cd03297 160 SALDRALrlqlLPELKQIKKNLNIPVIFVTHDlseAEYLADR---IVVMEDGRLQYIG 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
298-593 |
7.87e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 298 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhianralsippnidvLLCEQevvadetpavqavLRADT 377
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLK---------------LMLGQ-------------LQADS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 378 krlrlleeerrlqGQLEQGddtaaEKLEKVY-----EELRATGAAAAEA-----------KARRILAGLG---FDPEMQN 438
Cdd:PRK11147 374 -------------GRIHCG-----TKLEVAYfdqhrAELDPEKTVMDNLaegkqevmvngRPRHVLGYLQdflFHPKRAM 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 439 RPTQKFSGGWRMRVSLARaLFMEPT-LLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTD-IIHLDTQ 516
Cdd:PRK11147 436 TPVKALSGGERNRLLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcWIFEGNG 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 517 RLHYYRGNYmtFKKMYQQKQKELLKQyekqekklkelkAGGKSTKQAEKQTKEVLTRKQQKCRRKNQDEESQEPPEL 593
Cdd:PRK11147 515 KIGRYVGGY--HDARQQQAQYLALKQ------------PAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEQLPQLL 577
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
619-818 |
7.98e-13 |
|
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: 71.71 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNH-----------RLKIGFFNQ 687
Cdd:COG4988 339 LEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswRRQIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 688 Q-Y------AEQLHM------EETPTEYLQRSfnlpyqdarkCLGRF------GLEShahtiQI----CKLSGGQKARVV 744
Cdd:COG4988 419 NpYlfagtiRENLRLgrpdasDEELEAALEAA----------GLDEFvaalpdGLDT-----PLgeggRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 745 FAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHDARLITETNcQLWVVEEQGVSQIdGDFDD 818
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALLAQAD-RILVLDDGRIVEQ-GTHEE 557
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
316-518 |
8.38e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 68.39 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 316 LYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLceqevvaDETPAVQ---AVLRADTkrlrlleeerrlqGQ 392
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLA--GLYKPTSGSVLL-------DGTDIRQldpADLRRNI-------------GY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 LEQ-------------------GDDtaaEKLEKVYEelratgaaaaeakarriLAGL---------GFDPEMQNRpTQKF 444
Cdd:cd03245 83 VPQdvtlfygtlrdnitlgaplADD---ERILRAAE-----------------LAGVtdfvnkhpnGLDLQIGER-GRGL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR--KTLLIVSHDQGFLdDVCTDIIHLDTQRL 518
Cdd:cd03245 142 SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLgdKTLIIITHRPSLL-DLVDRIIVMDSGRI 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
619-790 |
1.09e-12 |
|
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: 67.21 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMrknhrlkigFFNqqyAEQLHMEET 698
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI---------LID---GEDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 699 PTEYLQRSFNLPYQDarkclgrFGLESHAHTIQICK--LSGGQKARVVFAELACREPDVLILDEPTNNLDIE---SIDAL 773
Cdd:cd03229 70 ELPPLRRRIGMVFQD-------FALFPHLTVLENIAlgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrrEVRAL 142
|
170
....*....|....*...
gi 39930335 774 GEAINDYKG-AVIVVSHD 790
Cdd:cd03229 143 LKSLQAQLGiTVVLVTHD 160
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
622-808 |
1.32e-12 |
|
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: 68.41 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-----------KNHRLKIG------- 683
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGvvpqdtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 684 ------FFNQQY-------------AEQLHMEETPTeylqrsfNLPYQDARKcLGRFGLeshahtiqicKLSGGQKARVV 744
Cdd:cd03253 86 lfndtiGYNIRYgrpdatdeevieaAKAAQIHDKIM-------RFPDGYDTI-VGERGL----------KLSGGEKQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 745 FAELACREPDVLILDEPTNNLDIESIDALGEAIND-YKG-AVIVVSHdaRLITETNCQLWVVEEQG 808
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDvSKGrTTIVIAH--RLSTIVNADKIIVLKDG 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
616-790 |
1.42e-12 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 68.54 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKS---------------TLLLLLTGKLTPTNGEMRKnHRL 680
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKStllrclnglveptsgEILVDGQDVTALRGRALRR-LRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 681 KIGFFNQQYA--EQL---------HMEETPTeyLQRSFNLPYQD----ARKCLGRFGLESHAHtiQIC-KLSGGQKARVV 744
Cdd:COG3638 81 RIGMIFQQFNlvPRLsvltnvlagRLGRTST--WRSLLGLFPPEdrerALEALERVGLADKAY--QRAdQLSGGQQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 39930335 745 FAELACREPDVLILDEPTNNLDIES----IDALGEAINDYKGAVIVVSHD 790
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTarqvMDLLRRIAREDGITVVVNLHQ 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
277-499 |
1.75e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 70.85 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 277 SVSQAEVSSRQAMLENASDIKLEKFSISAH---GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnRALSiPPNID 353
Cdd:TIGR02868 314 AGPVAEGSAPAAGAVGLGKPTLELRDLSAGypgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA-GLLD-PLQGE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 354 VLL---CEQEVVADETPAVQAVLRADTKRLRLLEEERRLQGQLEQGDDTAAEKLEKVyeelratgaaaaeaKARRILAGL 430
Cdd:TIGR02868 392 VTLdgvPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERV--------------GLADWLRAL 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 431 --GFDPEMQNRpTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA----VIWLNNYLQGwrKTLLIVSHD 499
Cdd:TIGR02868 458 pdGLDTVLGEG-GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETadelLEDLLAALSG--RTVVLITHH 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
621-804 |
2.57e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 70.01 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 621 GVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLH------ 694
Cdd:TIGR02857 326 GVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAwvpqhp 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 695 --MEETPTEYLQrsFNLPYQDA--------RKCLGRF--GLESHAHTI---QICKLSGGQKARVVFAELACREPDVLILD 759
Cdd:TIGR02857 406 flFAGTIAENIR--LARPDASDaeirealeRAGLDEFvaALPQGLDTPigeGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 39930335 760 EPTNNLDIESIDALGEAINDYKG--AVIVVSHDARLITETNcQLWVV 804
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAALAD-RIVVL 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
621-794 |
3.25e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 621 GVTFGyegQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETPT 700
Cdd:PRK09544 11 SVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 701 EYLQRSFNLPYQDARKCLGRFgleSHAHTIQ--ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIN 778
Cdd:PRK09544 88 RFLRLRPGTKKEDILPALKRV---QAGHLIDapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170 180
....*....|....*....|
gi 39930335 779 DYKG----AVIVVSHDARLI 794
Cdd:PRK09544 165 QLRReldcAVLMVSHDLHLV 184
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
617-796 |
3.27e-12 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 67.21 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKST--------------LLLLLTGKLTPTNGEMRKNHRLKI 682
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTllrclnglveptsgSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 683 GFFNQQYA---EQLHME--------ETPTeyLQRSFNLPY----QDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAE 747
Cdd:cd03256 81 GMIFQQFNlieRLSVLEnvlsgrlgRRST--WRSLFGLFPkeekQRALAALERVGLLDKAYQ-RADQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 39930335 748 LACREPDVLILDEPTNNLDIES----IDALgEAINDYKG-AVIVVSHDARLITE 796
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASsrqvMDLL-KRINREEGiTVIVSLHQVDLARE 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
296-511 |
3.85e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 66.76 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNA----DLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVvadetpavqa 371
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILG--LLKPTSGSIIFDGKDL---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 372 vLRADTKRLRLLEEERRLQGQ--------------------LEQGDDTAAEKLEKVYEELratgaaaaeakarriLAGLG 431
Cdd:cd03257 70 -LKLSRRLRKIRRKEIQMVFQdpmsslnprmtigeqiaeplRIHGKLSKKEARKEAVLLL---------------LVGVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 432 FDPEMQNR-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHDQGFL 503
Cdd:cd03257 134 LPEEVLNRyPHE-LSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqaqiLDLLKKLQEELG---LTLLFITHDLGVV 209
|
....*...
gi 39930335 504 DDVCTDII 511
Cdd:cd03257 210 AKIADRVA 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
617-809 |
4.37e-12 |
|
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: 65.32 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEG-QKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHrlkigffnqQYAEQLHm 695
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG---------ADISQWD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 696 eetPTEYLQRSFNLPyQDARKCLGrfgleSHAHTIqickLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGE 775
Cdd:cd03246 71 ---PNELGDHVGYLP-QDDELFSG-----SIAENI----LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 39930335 776 AINDYKGA---VIVVSHDARLITEtnCQLWVVEEQGV 809
Cdd:cd03246 138 AIAALKAAgatRIVIAHRPETLAS--ADRILVLEDGR 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
296-518 |
7.96e-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: 65.99 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALsIPPNIDVLLCEQEVVADETPAVQAVLRA 375
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV--GL-LRPDSGEVLIDGEDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 DTkrlrlleeerrlqGQLEQG----DD-TAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQkFSGGWRM 450
Cdd:cd03261 78 RM-------------GMLFQSgalfDSlTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-LSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 451 RVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG---LTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
616-789 |
9.71e-12 |
|
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: 65.88 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYEGqKPLFKNLDFGIDMDSRICIVGPNGVGKStllllltgkltptNGEMRKNH----------------- 678
Cdd:COG1119 3 LLELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKStll-------sliTGDLPPTYgndvrlfgerrggedvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 679 --RLKIGFFNQQYAEQLHMEET------------------PTEyLQRsfnlpyQDARKCLGRFGLESHAHTiQICKLSGG 738
Cdd:COG1119 75 elRKRIGLVSPALQLRFPRDETvldvvlsgffdsiglyrePTD-EQR------ERARELLELLGLAHLADR-PFGTLSQG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 739 QKARVVFAelacR----EPDVLILDEPTNNLDIESIDALGEAINDYKG----AVIVVSH 789
Cdd:COG1119 147 EQRRVLIA----RalvkDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
619-829 |
1.07e-11 |
|
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: 68.71 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLlllltgkltptngemrknhrLKI--GF---------FN 686
Cdd:COG2274 476 LENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTL--------------------LKLllGLyeptsgrilID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 687 QQYAEQLHmeetPTEY-------LQRSF--------NL-------PYQDARKCLGRFGL----ESHA---HTiQI----C 733
Cdd:COG2274 536 GIDLRQID----PASLrrqigvvLQDVFlfsgtireNItlgdpdaTDEEIIEAARLAGLhdfiEALPmgyDT-VVgeggS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHdaRLITETNCQLWVVEEQGVSQ 811
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAH--RLSTIRLADRIIVLDKGRIV 688
|
250
....*....|....*...
gi 39930335 812 IDGDFDdykrEVLEALGE 829
Cdd:COG2274 689 EDGTHE----ELLARKGL 702
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
313-513 |
1.12e-11 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 65.20 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvADETPAVQAVLRADTkrlrlleeerrlQGQ 392
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILG--GLDRPTSGEVRVDGTDI-SKLSEKELAAFRRRH------------IGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 LEQ-----GDDTAAEKLEkVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLML 467
Cdd:cd03255 87 VFQsfnllPDLTALENVE-LPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE-LSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 39930335 468 DEPTNHLDL-NAVIWLN-----NYLQGwrKTLLIVSHDQgFLDDVCTDIIHL 513
Cdd:cd03255 165 DEPTGNLDSeTGKEVMEllrelNKEAG--TTIVVVTHDP-ELAEYADRIIEL 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
295-514 |
1.40e-11 |
|
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: 68.32 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 295 DIKLEK--FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA-------------NRALS-IPP-----NID 353
Cdd:COG2274 473 DIELENvsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLglyeptsgrilidGIDLRqIDPaslrrQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 354 VLLceQEVV------------ADETPAVQAVLRA--------DTKrlrlleeerrlqgQLEQGDDTaaekleKVYEElra 413
Cdd:COG2274 553 VVL--QDVFlfsgtirenitlGDPDATDEEIIEAarlaglhdFIE-------------ALPMGYDT------VVGEG--- 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 414 tgaaaaeakarrilaGLGFdpemqnrptqkfSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN--AVIW--LNNYLQGW 489
Cdd:COG2274 609 ---------------GSNL------------SGGQRQRLAIARALLRNPRILILDEATSALDAEteAIILenLRRLLKGR 661
|
250 260
....*....|....*....|....*
gi 39930335 490 rkTLLIVSHDQGFLDDvCTDIIHLD 514
Cdd:COG2274 662 --TVIIIAHRLSTIRL-ADRIIVLD 683
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
426-499 |
1.78e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 64.62 E-value: 1.78e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 426 ILAGLGFDPeMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHD 499
Cdd:cd03297 115 LLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLnipvIFVTHD 191
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
622-797 |
1.79e-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: 64.35 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRknhrlkigfFNQQYAEQLHMEETPte 701
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIR---------VNGQDVSDLRGRAIP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 702 YLQRSFNLPYQDAR------------------------------KCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACR 751
Cdd:cd03292 75 YLRRKIGVVFQDFRllpdrnvyenvafalevtgvppreirkrvpAALELVGLSHKHRALPA-ELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 39930335 752 EPDVLILDEPTNNLDIES---IDALGEAINDYKGAVIVVSHDARLITET 797
Cdd:cd03292 154 SPTILIADEPTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTT 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
296-520 |
2.59e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 63.75 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRrYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQAV--- 372
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILA--TLTPPSSGTIRIDGQDVLKQPQKLRRRIgyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 ---------LRADTKRLRLLEEERRLQGQLEQgddTAAEKLEKVyeelratgaaaaeakarrilaGLGfdpEMQNRPTQK 443
Cdd:cd03264 78 pqefgvypnFTVREFLDYIAWLKGIPSKEVKA---RVDEVLELV---------------------NLG---DRAKKKIGS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQ--GWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHY 520
Cdd:cd03264 131 LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSelGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
629-814 |
3.03e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 64.28 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 629 QKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM----------RKNHRLKIGF-FNQQyaEQLHMEE 697
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrRKKFLRRIGVvFGQK--TQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 698 TPTE---YLQRSFNLPYQDARKCLGRFG----LESHAHTiQICKLSGGQKARvvfAELAC---REPDVLILDEPTNNLDI 767
Cdd:cd03267 111 PVIDsfyLLAAIYDLPPARFKKRLDELSelldLEELLDT-PVRQLSLGQRMR---AEIAAallHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 39930335 768 ESIDALGEAINDY----KGAVIVVSHDARLItETNCQLWVVEEQGVSQIDG 814
Cdd:cd03267 187 VAQENIRNFLKEYnrerGTTVLLTSHYMKDI-EALARRVLVIDKGRLLYDG 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
582-794 |
3.09e-11 |
|
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: 66.71 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 582 NQDEESQEPPELLKRPKEYTVRFtfpdppplsppvlglHGVTFGYEGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLL 660
Cdd:COG4987 314 DAPPAVTEPAEPAPAPGGPSLEL---------------EDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 661 LLLTGKLTPTNGEMRKNH-----------RLKIGFFNQQ-------YAEQLHM------EETPTEYLQRsfnlpyqdARk 716
Cdd:COG4987 379 ALLLRFLDPQSGSITLGGvdlrdldeddlRRRIAVVPQRphlfdttLRENLRLarpdatDEELWAALER--------VG- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 717 cLGRF------GLES----HAHTiqickLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY-KG-AV 784
Cdd:COG4987 450 -LGDWlaalpdGLDTwlgeGGRR-----LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlAGrTV 523
|
250
....*....|
gi 39930335 785 IVVSHDARLI 794
Cdd:COG4987 524 LLITHRLAGL 533
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
622-826 |
4.21e-11 |
|
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: 64.05 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM-----------RKNHRLKIGFFNQQY 689
Cdd:COG1124 9 VSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 AEQLH----MEETPTEYLqRSFNLPYQDAR--KCLGRFGLESHA-----HtiqicKLSGGQKARVVFAELACREPDVLIL 758
Cdd:COG1124 89 YASLHprhtVDRILAEPL-RIHGLPDREERiaELLEQVGLPPSFldrypH-----QLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 759 DEPTNNLDI----ESIDALGEAINDYKGAVIVVSHDARLITETnC-------QLWVVEEQGVSQIDGDF-DDYKREVLEA 826
Cdd:COG1124 163 DEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHL-CdrvavmqNGRIVEELTVADLLAGPkHPYTRELLAA 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
265-518 |
4.24e-11 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 66.32 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 265 SLKAANAAEN-----DFSVSQAEVSSRQAMLENASDIKLEKFSISAH-GKELFVNADLYIVAGRRYGLVGPNGKGKTTLL 338
Cdd:COG4988 301 RANGIAAAEKifallDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 339 K-------------HIANRALS-IPP-----------------------NIdvLLCEQEvvADETpAVQAVLRA------ 375
Cdd:COG4988 381 NlllgflppysgsiLINGVDLSdLDPaswrrqiawvpqnpylfagtireNL--RLGRPD--ASDE-ELEAALEAagldef 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 -DtkrlrlleeerrlqgQLEQGDDTaaekleKVYEelratgaaaaeakarrilAGLGFdpemqnrptqkfSGGWRMRVSL 454
Cdd:COG4988 456 vA---------------ALPDGLDT------PLGE------------------GGRGL------------SGGQAQRLAL 484
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 455 ARALFMEPTLLMLDEPTNHLDLN--AVIW--LNNYLQGwrKTLLIVSHDQGFLDDvCTDIIHLDTQRL 518
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
617-789 |
4.30e-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: 63.07 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN-------HRLKIGFF---- 685
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgkpldiaARNRIGYLpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 ----NQQYAEQLhmeetptEYLQRSFNLPYQDARK----CLGRFGLESHAHtIQICKLSGGQKARVVFAELACREPDVLI 757
Cdd:cd03269 80 glypKMKVIDQL-------VYLAQLKGLKKEEARRrideWLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190
....*....|....*....|....*....|....*
gi 39930335 758 LDEPTNNLDIESIDALGEAINDYKGA---VIVVSH 789
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAgktVILSTH 186
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
280-518 |
4.88e-11 |
|
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: 66.33 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 280 QAEVSSRQAMLENASDIKLEK--FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnRALsiPP------- 350
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDvsFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL-RFL--DPqsgsitl 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 351 -NIDVLLCEQE-------VVADETPAVQAVLR---------ADtkrlrlleeerrlqgqleqgDDTAAEKLEKVY-EELr 412
Cdd:COG4987 395 gGVDLRDLDEDdlrrriaVVPQRPHLFDTTLRenlrlarpdAT--------------------DEELWAALERVGlGDW- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 413 atgaaaaeakarriLAGL--GFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-LNAVIWLNNYLQGW 489
Cdd:COG4987 454 --------------LAALpdGLDTWLGEGGRR-LSGGERRRLALARALLRDAPILLLDEPTEGLDaATEQALLADLLEAL 518
|
250 260 270
....*....|....*....|....*....|
gi 39930335 490 R-KTLLIVSHDQGFLDDVCTdIIHLDTQRL 518
Cdd:COG4987 519 AgRTVLLITHRLAGLERMDR-ILVLEDGRI 547
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
444-498 |
5.07e-11 |
|
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: 62.23 E-value: 5.07e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSH 498
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAagaTRIVIAH 154
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
628-790 |
7.33e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 62.55 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-------------KNHRLKIGFFNQQYAEQLH 694
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltddkkniNELRQKVGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 695 ME--ETPTEYLQRSFNLPYQDA----RKCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 768
Cdd:cd03262 91 LTvlENITLAPIKVKGMSKAEAeeraLELLEKVGLADKADAYPA-QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180
....*....|....*....|....*
gi 39930335 769 SIDALGEAIND--YKG-AVIVVSHD 790
Cdd:cd03262 170 LVGEVLDVMKDlaEEGmTMVVVTHE 194
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
298-511 |
9.33e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 298 LEKFSISAHGKE--LFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVvADETPAVQAVLRA 375
Cdd:COG2401 31 LEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-GREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 DTKrlrlleeerrlqgqleqgdDTAAEKLEKVyeelratgaaaaeakarrilaGLGfDPEMQNRPTQKFSGGWRMRVSLA 455
Cdd:COG2401 110 GDF-------------------KDAVELLNAV---------------------GLS-DAVLWLRRFKELSTGQKFRFRLA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 456 RALFMEPTLLMLDEPTNHLD-LNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDVCTDII 511
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDrQTAKRVARNLQKLARRagiTLVVATHHYDVIDDLQPDLL 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
294-518 |
9.73e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 9.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 294 SDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEVVADET-PAVQAV 372
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI--NLLEQPEAGTIRVGDITIDTARSlSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 LRAdtkrlrlleeERRLQGQLEQGDDTAAEK--LEKVYEE---LRATGAAAAEAKARRILAGLGFDPEMQNRPtQKFSGG 447
Cdd:PRK11264 80 IRQ----------LRQHVGFVFQNFNLFPHRtvLENIIEGpviVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 448 WRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGW---RKTLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
427-513 |
9.86e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.06 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 427 LAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFL 503
Cdd:PRK10619 136 LAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFA 215
|
90
....*....|
gi 39930335 504 DDVCTDIIHL 513
Cdd:PRK10619 216 RHVSSHVIFL 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
617-789 |
1.09e-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: 61.02 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTllllltgkltptngemrknhrlkigFFN------QQYA 690
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSS-------------------------LFRalaglwPWGS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 691 EQLHM-EETPTEYL-QRsfnlPYqdarkcLGRFGLEShahtiQIC-----KLSGGQKARVVFAELACREPDVLILDEPTN 763
Cdd:cd03223 56 GRIGMpEGEDLLFLpQR----PY------LPLGTLRE-----QLIypwddVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180
....*....|....*....|....*.
gi 39930335 764 NLDIESIDALGEAINDYKGAVIVVSH 789
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGH 146
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
619-794 |
1.52e-10 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 61.88 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR---------KNHRL-----KIGF 684
Cdd:TIGR02673 4 FHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRiagedvnrlRGRQLpllrrRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 685 FNQQYaeQLHMEETPTEYLQRSFNLPYQDARK-------CLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLI 757
Cdd:TIGR02673 84 VFQDF--RLLPDRTVYENVALPLEVRGKKEREiqrrvgaALRQVGLEHKADAFPE-QLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 39930335 758 LDEPTNNLD---IESIDALGEAINDYKGAVIVVSHDARLI 794
Cdd:TIGR02673 161 ADEPTGNLDpdlSERILDLLKRLNKRGTTVIVATHDLSLV 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
315-506 |
1.73e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 61.10 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 315 DLYIVAGRRYGLVGPNGKGKTTLLKHIA----------NRALSIPPnidVLLCEQEVVADETPA--VQAV---------- 372
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAgvlrptsgtvRRAGGARV---AYVPQRSEVPDSLPLtvRDLVamgrwarrgl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 LRADTKrlrlleeerrlqgqleqgDDTAA--EKLEKVYeelratgaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRM 450
Cdd:NF040873 89 WRRLTR------------------DDRAAvdDALERVG------------------LADLA------GRQLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 451 RVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDqgfLDDV 506
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHargATVVVVTHD---LELV 182
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
616-796 |
2.14e-10 |
|
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: 61.93 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKST--------------LLLLLTGKLTPTNGEMRKNHRLK 681
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTllrcinrlvepssgSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 682 IGFFNQQY---------AEQLHMEETPTEYLQRSFNL----PYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAEL 748
Cdd:TIGR02315 81 IGMIFQHYnlierltvlENVLHGRLGYKPTWRSLLGRfseeDKERALSALERVGLADKAYQ-RADQLSGGQQQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 39930335 749 ACREPDVLILDEPTNNLDIES----IDALGEaINDYKGAVIVVS-HDARLITE 796
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTskqvMDYLKR-INKEDGITVIINlHQVDLAKK 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
313-514 |
2.17e-10 |
|
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: 61.68 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPPNI-DVLLCEQEV---------------------------VAD 364
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF---LRPTSgSVLFDGEDItglppheiarlgigrtfqiprlfpeltVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 365 etpAVQAVLRADTKRLRLLEEERRLQGQLEqgdDTAAEKLEKVyeelratgaaaaeakarrilaGLGfdpEMQNRPTQKF 444
Cdd:cd03219 95 ---NVMVAAQARTGSGLLLARARREEREAR---ERAEELLERV---------------------GLA---DLADRPAGEL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPT---NHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLD 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
288-476 |
2.42e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 61.71 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 288 AMLEnASDIklekfSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNI-DVLLCEQEVvaD 364
Cdd:PRK13548 1 AMLE-ARNL-----SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLL-----RALSgeLSPDSgEVRLNGRPL--A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 365 ETPAVQ-----AVL-------------------RADtkrlrlleeerrLQGQLEQGDDTAAEKLEKVYeelratgaaaae 420
Cdd:PRK13548 68 DWSPAElarrrAVLpqhsslsfpftveevvamgRAP------------HGLSRAEDDALVAAALAQVD------------ 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 421 akarriLAGLGfdpemqNRPTQKFSGGWRMRVSLARAL------FMEPTLLMLDEPTNHLDL 476
Cdd:PRK13548 124 ------LAHLA------GRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
301-514 |
2.45e-10 |
|
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: 60.09 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 301 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVvADETPAVqavLRAdtkrl 380
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR--LYDPTSGEILIDGVDL-RDLDLES---LRK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 381 rlleeerrLQGQLEQG----DDTAAEKLekvyeelratgaaaaeakarrilaglgfdpemqnrptqkFSGGWRMRVSLAR 456
Cdd:cd03228 77 --------NIAYVPQDpflfSGTIRENI---------------------------------------LSGGQRQRIAIAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 457 ALFMEPTLLMLDEPTNHLD--LNAVIW--LNNYLQGwrKTLLIVSHDqgfLDDV--CTDIIHLD 514
Cdd:cd03228 110 ALLRDPPILILDEATSALDpeTEALILeaLRALAKG--KTVIVIAHR---LSTIrdADRIIVLD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
426-475 |
2.79e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.55 E-value: 2.79e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 39930335 426 ILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:COG4172 408 ALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
315-520 |
2.94e-10 |
|
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: 61.19 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 315 DLYIVAGRRYGLVGPNGKGKTTLLKHIAN---------RALSIPP---------NIDVLLCEQEVVADETPAVQ--AVLR 374
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGllqptsgevRVAGLVPwkrrkkflrRIGVVFGQKTQLWWDLPVIDsfYLLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 375 ADTkrlrlleeerrlqgQLEqgDDTAAEKLEKVYEELRATgaaaaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVSL 454
Cdd:cd03267 121 AIY--------------DLP--PARFKKRLDELSELLDLE--------------------ELLDTPVRQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 455 ARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQGFLDDVCTDIIHLDTQRLHY 520
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
315-519 |
3.21e-10 |
|
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: 60.91 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 315 DLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVA-DETPavQAVLRADtkrlrlleeerrLQG-- 391
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLA--GLDRPTSGTVRLAGQDLFAlDEDA--RARLRAR------------HVGfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 392 ----QL---------------EQGD----DTAAEKLEKVyeelratgaaaaeakarrilaGLGfdPEMQNRPTQkFSGGW 448
Cdd:COG4181 96 fqsfQLlptltalenvmlpleLAGRrdarARARALLERV---------------------GLG--HRLDHYPAQ-LSGGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 449 RMRVSLARALFMEPTLLMLDEPTNHLD-------------LNAViwlnnylQGwrKTLLIVSHDQGfLDDVCTDIIHLDT 515
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDaatgeqiidllfeLNRE-------RG--TTLVLVTHDPA-LAARCDRVLRLRA 221
|
....
gi 39930335 516 QRLH 519
Cdd:COG4181 222 GRLV 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
289-476 |
3.54e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 61.28 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 289 MLEnASDIklekfSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLkhianRALS--IPPNI-DVLLCEQEVvaDE 365
Cdd:COG4559 1 MLE-AENL-----SVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLL-----KLLTgeLTPSSgEVRLNGRPL--AA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 366 TPAVQ-----AVLRadtkrlrlleeerrlQ--------------------GQLEQGDDT--AAEKLEKVyeelratgaaa 418
Cdd:COG4559 68 WSPWElarrrAVLP---------------QhsslafpftveevvalgrapHGSSAAQDRqiVREALALV----------- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 419 aeakarrilaGLGfdpEMQNRPTQKFSGGWRMRVSLARAL-------FMEPTLLMLDEPTNHLDL 476
Cdd:COG4559 122 ----------GLA---HLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
437-525 |
4.28e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 437 QNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHL-DT 515
Cdd:PRK11819 439 QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFeGD 518
|
90
....*....|
gi 39930335 516 QRLHYYRGNY 525
Cdd:PRK11819 519 SQVEWFEGNF 528
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
306-515 |
4.47e-10 |
|
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: 59.96 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 306 HGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralsippnidvLLCEQ--EVVADETPAVQAVLRADTkrlrll 383
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAG-----------LIKESsgSILLNGKPIKAKERRKSI------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 384 eeerrlqGQLEQGDDTaaeKL--EKVYEELR--ATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRMRVSLARALF 459
Cdd:cd03226 74 -------GYVMQDVDY---QLftDSVREELLlgLKELDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 460 MEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDT 515
Cdd:cd03226 143 SGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
445-499 |
4.57e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 61.26 E-value: 4.57e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD------LNAviWLNNYLQGWRKTLLIVSHD 499
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDaltrerLQD--ELLRLWQETGKTVLFVTHD 198
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
617-790 |
4.64e-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: 63.15 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN-----------HRLKIGFF 685
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 NQqyaeQLHMEETPTeylqrSFNL-------PYQDARKCLGRFGLESH-------AHTI---QICKLSGGQKARVVFAEL 748
Cdd:TIGR02868 415 AQ----DAHLFDTTV-----RENLrlarpdaTDEELWAALERVGLADWlralpdgLDTVlgeGGARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 39930335 749 ACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHD 790
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
431-513 |
5.80e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 431 GFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD--LNAVI--WLNNYLQGWRKTLLIVSHDQGFLDDV 506
Cdd:PRK15134 413 GLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAQIlaLLKSLQQKHQLAYLFISHDLHVVRAL 492
|
....*..
gi 39930335 507 CTDIIHL 513
Cdd:PRK15134 493 CHQVIVL 499
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
734-808 |
6.28e-10 |
|
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: 60.32 E-value: 6.28e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIND-YKG-AVIVVSHdaRLITETNCQLWVVEEQG 808
Cdd:cd03251 138 KLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERlMKNrTTFVIAH--RLSTIENADRIVVLEDG 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
296-520 |
7.09e-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: 59.81 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHgkELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADEtPAVQAVlra 375
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIA--GFETPQSGRVLINGVDVTAAP-PADRPV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 dtkRLRLLEEERRLQGQLEQGDDTAAEKLEKVYEElratgaaaAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLA 455
Cdd:cd03298 73 ---SMLFQENNLFAHLTVEQNVGLGLSPGLKLTAE--------DRQAIEVALARVGLAGLEKRLPGE-LSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 456 RALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRK-TLLIVSHDQGFLDDVCTDIIHLDTQRLHY 520
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
438-500 |
7.34e-10 |
|
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: 60.04 E-value: 7.34e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQ 500
Cdd:cd03299 124 NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefgvTVLHVTHDF 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
438-499 |
9.10e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 9.10e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHD 499
Cdd:PRK09544 115 DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHD 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
296-514 |
1.04e-09 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 59.08 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETP-------- 367
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN--LLEEPDSGTIIIDGLKLTDDKKNinelrqkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 368 --------------AVQAVLRADTKRLRLLEeerrlqgqlEQGDDTAAEKLEKVyeelratgaaaaeakarrilaglGFD 433
Cdd:cd03262 79 gmvfqqfnlfphltVLENITLAPIKVKGMSK---------AEAEERALELLEKV-----------------------GLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 434 PEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDI 510
Cdd:cd03262 127 DKADAYPAQ-LSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRV 205
|
....
gi 39930335 511 IHLD 514
Cdd:cd03262 206 IFMD 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
735-794 |
1.09e-09 |
|
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: 59.44 E-value: 1.09e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 735 LSGGQKARVVFAE-LACrEPDVLILDEPTNNLDIES----IDALGEAINDYKGAVIVVSHDARLI 794
Cdd:cd03257 146 LSGGQRQRVAIARaLAL-NPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVV 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
426-513 |
1.12e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 59.29 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 426 ILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNnylQGWRKTLLIVSH 498
Cdd:COG1136 128 LLERVGLGDRLDHRPSQ-LSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeevLELLRELN---RELGTTIVMVTH 203
|
90
....*....|....*
gi 39930335 499 DQgFLDDVCTDIIHL 513
Cdd:COG1136 204 DP-ELAARADRVIRL 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
307-479 |
1.30e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 58.52 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 307 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQAVLRAdtkrlrlleee 386
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA--GLLRPDSGEVRWNGTPLAEQRDEPHENILYL----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 387 rrlqGQLE--QGDDTAAEKLEKVYEELRATGAAAAEAKARRILAGLgfdpemQNRPTQKFSGGWRMRVSLARALFMEPTL 464
Cdd:TIGR01189 79 ----GHLPglKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTGF------EDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170
....*....|....*
gi 39930335 465 LMLDEPTNHLDLNAV 479
Cdd:TIGR01189 149 WILDEPTTALDKAGV 163
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
296-513 |
1.33e-09 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 59.58 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVA------------ 363
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLElepderaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 364 ------DETPAVQAV--LRAdtkrlrlleeERRLQGQLEQGDDTAAEKLEKVYEELratgaaaaeakarriLAGLGFDPE 435
Cdd:TIGR01978 81 lafqypEEIPGVSNLefLRS----------ALNARRSARGEEPLDLLDFEKLLKEK---------------LALLDMDEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 436 MQNRPTQK-FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDII 511
Cdd:TIGR01978 136 FLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRepdRSFLIITHYQRLLNYIKPDYV 215
|
..
gi 39930335 512 HL 513
Cdd:TIGR01978 216 HV 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
622-806 |
1.58e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.82 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM--------RKNH---RLKIGFFNQQYA 690
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitKENIrevRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 691 EQLHmeeTPTEYLQRSF---NLPYQDA------RKCLGRFGLEsHAHTIQICKLSGGQKARVVFAELACREPDVLILDEP 761
Cdd:PRK13652 89 DQIF---SPTVEQDIAFgpiNLGLDEEtvahrvSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 39930335 762 TNNLDIESIDALGEAIND----YKGAVIVVSHDARLITETNCQLWVVEE 806
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDlpetYGMTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
735-794 |
2.00e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 2.00e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG---AVIVVSHDARLI 794
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLL 167
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
296-499 |
2.06e-09 |
|
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: 58.73 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRALSIPPNI----DVLLCEQEVVADETPAVQa 371
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPGApdegEVLLDGKDIYDLDVDVLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 372 vLRAdtkrlrlleeerrLQGQLEQ---------------GDDTAAEKLEKVYEELRATGaaaaeakarriLAGLGFDPEM 436
Cdd:cd03260 79 -LRR-------------RVGMVFQkpnpfpgsiydnvayGLRLHGIKLKEELDERVEEA-----------LRKAALWDEV 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 437 QNRPTQ-KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL-------NAVIWLNNylqgwRKTLLIVSHD 499
Cdd:cd03260 134 KDRLHAlGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPistakieELIAELKK-----EYTIVIVTHN 199
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
427-500 |
2.11e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 60.16 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 427 LAGLGfdpemqNR-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDlNAV-----IWLNNYLQGWRKTLLIVSHDQ 500
Cdd:COG1118 123 LEGLA------DRyPSQ-LSGGQRQRVALARALAVEPEVLLLDEPFGALD-AKVrkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
634-790 |
2.20e-09 |
|
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: 59.39 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 634 KNLDFGIDMDSRICIVGPNGVGKST--------------LLLLLTGKLTPTNGEMRKNHRLKIGF-FnqQYAE-QLhMEE 697
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTliqhlngllkptsgTVTIDGRDITAKKKKKLKDLRKKVGLvF--QFPEhQL-FEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 698 T--------PteylqRSFNLPYQDARKC----LGRFGLESHAHTIQICKLSGGQKARVVFAE-LACrEPDVLILDEPTNN 764
Cdd:TIGR04521 99 TvykdiafgP-----KNLGLSEEEAEERvkeaLELVGLDEEYLERSPFELSGGQMRRVAIAGvLAM-EPEVLILDEPTAG 172
|
170 180 190
....*....|....*....|....*....|
gi 39930335 765 LDIESIDALGEAIND----YKGAVIVVSHD 790
Cdd:TIGR04521 173 LDPKGRKEILDLFKRlhkeKGLTVILVTHS 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
628-789 |
2.24e-09 |
|
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: 58.00 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMrknhrlkigFFNQQYAEQLH--------MEETP 699
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---------TFDGKSYQKNIealrrigaLIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 700 T-----------EYLQRSFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 768
Cdd:cd03268 82 GfypnltarenlRLLARLLGIRKKRIDEVLDVVGLKDSAKK-KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180
....*....|....*....|....
gi 39930335 769 SIDALGEAI---NDYKGAVIVVSH 789
Cdd:cd03268 161 GIKELRELIlslRDQGITVLISSH 184
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
296-513 |
2.48e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.92 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLceqevvadetpavqavlra 375
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILF------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 dtkrlrlleeerrlqgqleQGDD-TAAEKLEKVyeelratgaaaaeakarriLAGLGFdpEMQNRPT------------- 441
Cdd:cd03217 62 -------------------KGEDiTDLPPEERA-------------------RLGIFL--AFQYPPEipgvknadflryv 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 442 -QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHDQGFLDDVCTDIIHL 513
Cdd:cd03217 102 nEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReegKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
735-827 |
2.64e-09 |
|
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: 60.53 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYK---GAVIVVSHDARLITETNcQLWVVEEqGVSQ 811
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargATVVVITHRPSLLAAVD-KLLVLRD-GRVQ 545
|
90
....*....|....*.
gi 39930335 812 IDGDfddyKREVLEAL 827
Cdd:COG4618 546 AFGP----RDEVLARL 557
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
313-499 |
2.78e-09 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 58.25 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLsIPPNIDVLLCEQEVVADETPAVQAVLradtkrlrlleeerrlqgQ 392
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAG--L-ERPTSGEVLVDGEPVTGPGPDRGYVF------------------Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 -----------------LEQGDDTAAEKLEKVYEELRatgaaaaeakarriLAGL-GFDpemQNRPTQkFSGGWRMRVSL 454
Cdd:cd03293 81 qdallpwltvldnvalgLELQGVPKAEARERAEELLE--------------LVGLsGFE---NAYPHQ-LSGGMRQRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 39930335 455 ARALFMEPTLLMLDEPTNHLDlnAVI------WLNNYLQGWRKTLLIVSHD 499
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALD--ALTreqlqeELLDIWRETGKTVLLVTHD 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
313-507 |
4.22e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPN---IDVLLCEQEVvaDET-PAVQAVLRAdtkrlrlleeeRR 388
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPTsgeVNVRVGDEWV--DMTkPGPDGRGRA-----------KR 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 389 LQGQLEQGDDTAAEK--LEKVYEELRATGAAAAEAKARRI-LAGLGFDPE----MQNRPTQKFSGGWRMRVSLARALFME 461
Cdd:TIGR03269 366 YIGILHQEYDLYPHRtvLDNLTEAIGLELPDELARMKAVItLKMVGFDEEkaeeILDKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 462 PTLLMLDEPTNHLD-----------LNAVIWLNnylqgwrKTLLIVSHDQGFLDDVC 507
Cdd:TIGR03269 446 PRIVILDEPTGTMDpitkvdvthsiLKAREEME-------QTFIIVSHDMDFVLDVC 495
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
628-789 |
4.45e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.12 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRlKIGFFNQQYAEQLHM---------EET 698
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRDSIARGLLYlghapgiktTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 699 PTEYLQrsFNLPYQDARKC---LGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGE 775
Cdd:cd03231 90 VLENLR--FWHADHSDEQVeeaLARVGLNGFEDRP-VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*..
gi 39930335 776 AINDY---KGAVIVVSH 789
Cdd:cd03231 167 AMAGHcarGGMVVLTTH 183
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
619-790 |
4.68e-09 |
|
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: 57.58 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKST-----LLLLLTGKLTPTNGEMR-------------KNHRL 680
Cdd:cd03260 3 LRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTllrllNRLNDLIPGAPDEGEVLldgkdiydldvdvLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 681 KIGFFNQQ-------------YAEQLHmEETPTEYLQRSfnlpyqdARKCLGRFGL------ESHAHtiqicKLSGGQKA 741
Cdd:cd03260 82 RVGMVFQKpnpfpgsiydnvaYGLRLH-GIKLKEELDER-------VEEALRKAALwdevkdRLHAL-----GLSGGQQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 39930335 742 RVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHD 790
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
617-768 |
4.70e-09 |
|
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: 57.20 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEGQKPLFK-NLDFGIDMdsrICIVGPNGVGKSTLLLLLTGKLTPTNG----------EMRKNHRLKIGFF 685
Cdd:cd03264 1 LQLENLTKRYGKKRALDGvSLTLGPGM---YGLLGPNGAGKTTLMRILATLTPPSSGtiridgqdvlKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 NQQ--YAEQLHMEETpTEYLQRSFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILD 759
Cdd:cd03264 78 PQEfgVYPNFTVREF-LDYIAWLKGIPSKEVKArvdeVLELVNLGDRAKK-KIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
....*....
gi 39930335 760 EPTNNLDIE 768
Cdd:cd03264 156 EPTAGLDPE 164
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
617-790 |
5.75e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 57.72 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQL--- 693
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 694 ---HMeeTP--------TEYlQRSFNLPYqdarkcLGRFGLESHAHTIQ--------------ICKLSGGQKARVVFAEL 748
Cdd:PRK11231 82 pqhHL--TPegitvrelVAY-GRSPWLSL------WGRLSAEDNARVNQameqtrinhladrrLTDLSGGQRQRAFLAMV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 39930335 749 ACREPDVLILDEPTNNLDI----ESIDALGEaINDYKGAVIVVSHD 790
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDInhqvELMRLMRE-LNTQGKTVVTVLHD 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
265-499 |
5.78e-09 |
|
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: 59.61 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 265 SLKAANAAENDFSV----SQAEVSSRQAMLENASDIKLEKFSISAHGKELFV-NADLYIVAGRRYGLVGPNGKGKTTLLK 339
Cdd:TIGR02857 287 RADGVAAAEALFAVldaaPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALrPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 340 HIANRalsIPPNIDVLLCEQEVVADETPAV----------QAVLRADTkrlrllEEERRLQGQLEQGDDTAAEKLEKVYe 409
Cdd:TIGR02857 367 LLLGF---VDPTEGSIAVNGVPLADADADSwrdqiawvpqHPFLFAGT------IAENIRLARPDASDAEIREALERAG- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 410 elratgaaaaeakARRILAGLgfdPEMQNRPTQK----FSGGWRMRVSLARALFMEPTLLMLDEPTNHLD--LNAVIW-- 481
Cdd:TIGR02857 437 -------------LDEFVAAL---PQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDaeTEAEVLea 500
|
250
....*....|....*...
gi 39930335 482 LNNYLQGwrKTLLIVSHD 499
Cdd:TIGR02857 501 LRALAQG--RTVLLVTHR 516
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
313-514 |
6.33e-09 |
|
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: 57.74 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLK--------------------------HIANRALS-------IPPNIDVLlceq 359
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNlitgfyrptsgrilfdgrditglpphRIARLGIArtfqnprLFPELTVL---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 360 EVVAdetpaVQAVLRADTKRLRLLEEERRLQGQLEQGDDTAAEKLEKVyeelratgaaaaeakarrilaGLGfdpEMQNR 439
Cdd:COG0411 98 ENVL-----VAAHARLGRGLLAALLRLPRARREEREARERAEELLERV---------------------GLA---DRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 440 PTQKFSGGWRMRVSLARALFMEPTLLMLDEPT---NH---LDLNAVI-WLNnylQGWRKTLLIVSHDQGFLDDVCTDIIH 512
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPeetEELAELIrRLR---DERGITILLIEHDMDLVMGLADRIVV 225
|
..
gi 39930335 513 LD 514
Cdd:COG0411 226 LD 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
622-817 |
6.74e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQ--KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM--------RKNHRL---KIGFFNQq 688
Cdd:TIGR00958 484 VSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvQYDHHYlhrQVALVGQ- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 yaEQLHMEETPTEYLqrSFNLPYQDARKCLGRfGLESHAHTIqICK---------------LSGGQKARVVFAELACREP 753
Cdd:TIGR00958 563 --EPVLFSGSVRENI--AYGLTDTPDEEIMAA-AKAANAHDF-IMEfpngydtevgekgsqLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 754 DVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHdaRLITETNCQLWVVEEQGVSQIDGDFD 817
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRSRASRTVLLIAH--RLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
619-768 |
7.69e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.33 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFkNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-KNH----------------RLK 681
Cdd:PRK11124 5 LNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiAGNhfdfsktpsdkairelRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 682 IGFFNQQYAEQLHME------ETPTEYLQRSFNLPYQDARKCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDV 755
Cdd:PRK11124 84 VGMVFQQYNLWPHLTvqqnliEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|...
gi 39930335 756 LILDEPTNNLDIE 768
Cdd:PRK11124 163 LLFDEPTAALDPE 175
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
616-792 |
8.02e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGyEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN-HRLKIGFFNQQYAEQLH 694
Cdd:PRK13543 11 LLAAHALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTATRGDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 695 MEETPTEyLQRSFNL----------PYQDARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNN 764
Cdd:PRK13543 90 LPGLKAD-LSTLENLhflcglhgrrAKQMPGSALAIVGLAGYEDTL-VRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180 190
....*....|....*....|....*....|.
gi 39930335 765 LDIESIDALGEAINDY---KGAVIVVSHDAR 792
Cdd:PRK13543 168 LDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
619-818 |
8.69e-09 |
|
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: 56.78 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQK--PLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGE-------MRKNH----RLKIGFF 685
Cdd:cd03249 3 FKNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEilldgvdIRDLNlrwlRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 NQQ-----------------YAEQLHMEETPTEYLQRSF--NLPYQ-DARkcLGRFGleshahtiqiCKLSGGQKARVVF 745
Cdd:cd03249 83 SQEpvlfdgtiaenirygkpDATDEEVEEAAKKANIHDFimSLPDGyDTL--VGERG----------SQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 746 AELACREPDVLILDEPTNNLDIESIDALGEAINDYKGA--VIVVSHdaRLITETNCQLWVVEEQGVSQIDGDFDD 818
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH--RLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
619-790 |
8.91e-09 |
|
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: 56.74 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM--------------RKNHRLKIGF 684
Cdd:cd03261 3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglseaeLYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 685 FNQQYA--EQLHMEETPTEYLQRSFNLPYQD----ARKCLGRFGLESHAH--TIQickLSGGQKARVVFAELACREPDVL 756
Cdd:cd03261 82 LFQSGAlfDSLTVFENVAFPLREHTRLSEEEireiVLEKLEAVGLRGAEDlyPAE---LSGGMKKRVALARALALDPELL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 39930335 757 ILDEPTNNLDIESIDALGEAINDYKGA----VIVVSHD 790
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVTHD 196
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
735-795 |
8.93e-09 |
|
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: 56.46 E-value: 8.93e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 735 LSGGQKA------RVVFAELACREPDVLILDEPTNNLDIESID-ALGEAINDYKGA----VIVVSHDARLIT 795
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELVD 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
617-766 |
9.18e-09 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 55.78 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM----------RKNHRLKIGFF 685
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 NQQyaeqlhmeetptEYLqrsFNlpyQDARKCLGRfgleshahtiqicKLSGGQKARVVFAELACREPDVLILDEPTNNL 765
Cdd:cd03247 81 NQR------------PYL---FD---TTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
.
gi 39930335 766 D 766
Cdd:cd03247 130 D 130
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
735-827 |
1.22e-08 |
|
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: 58.51 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYK---GAVIVVSHDARLITETNCQLwvVEEQGVSQ 811
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCVDKIL--VLQDGRIA 532
|
90
....*....|....*.
gi 39930335 812 IDGDfddyKREVLEAL 827
Cdd:TIGR01842 533 RFGE----RDEVLAKL 544
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
306-517 |
1.50e-08 |
|
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: 55.90 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 306 HGKELFV--NADLYIVAGRRYGLVGPNGKGKTTLLKHI-AN--------RALSIPPNIDVLLC-EQEVVA---DE----- 365
Cdd:COG4778 20 GGKRLPVldGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNylpdsgsiLVRHDGGWVDLAQAsPREILAlrrRTigyvs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 366 --------TPAVQAVLRAdtkrlrlleeerrlqgQLEQGDDtAAEKLEKVyEELratgaaaaeakarriLAGLGFDPEMQ 437
Cdd:COG4778 100 qflrviprVSALDVVAEP----------------LLERGVD-REEARARA-REL---------------LARLNLPERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 39930335 515 TQR 517
Cdd:COG4778 227 PFS 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
619-766 |
1.51e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 55.72 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLfKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRL---------KIGFFNQQY 689
Cdd:cd03301 3 LENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlppkdrDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 AEQLHMeetpTEYLQRSFNLPYQDARKCLGRFGLESHAHTIQICK--------LSGGQKARVVFAELACREPDVLILDEP 761
Cdd:cd03301 82 ALYPHM----TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHlldrkpkqLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
....*
gi 39930335 762 TNNLD 766
Cdd:cd03301 158 LSNLD 162
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
296-518 |
1.53e-08 |
|
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: 56.14 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALsIPPN---IDVLlcEQEVVADETPAVQAV 372
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII--GL-LRPDsgeILVD--GQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 --------------------------LRadtkrlrlleeerrlqgqlEQGDDTAAEKLEKVYEELRatgaaaaeakarri 426
Cdd:COG1127 81 rrrigmlfqggalfdsltvfenvafpLR-------------------EHTDLSEAEIRELVLEKLE-------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 427 LAGLgfdPEMQNR-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD------LNAVIwlnNYLQGWRK-TLLIVSH 498
Cdd:COG1127 128 LVGL---PGAADKmPSE-LSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDELI---RELRDELGlTSVVVTH 200
|
250 260
....*....|....*....|
gi 39930335 499 DQGFLDDVCTDIIHLDTQRL 518
Cdd:COG1127 201 DLDSAFAIADRVAVLADGKI 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
735-828 |
1.67e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.59 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIND----YKGAVIVVSHD----ARLITETncqlwVVEE 806
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSmedvAKLADRI-----IVMN 219
|
90 100
....*....|....*....|....
gi 39930335 807 QGVSQIDGDFDDYKREV--LEALG 828
Cdd:PRK13637 220 KGKCELQGTPREVFKEVetLESIG 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
714-796 |
2.00e-08 |
|
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: 55.91 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 714 ARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGE---AINDYKGAVIVVSHD 790
Cdd:cd03219 124 AEELLERVGLADLADRP-AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHD 202
|
....*.
gi 39930335 791 ARLITE 796
Cdd:cd03219 203 MDVVMS 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
296-477 |
2.12e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.16 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAVQAVLRA 375
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING---TLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 DTKRLRLLEEERRLQGQLEQGD-------DTAAEKLEKVYEElratgaaaaeakarrILAGLGFDpEMQNRPTQKFSGGW 448
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRtphrsrfDTWTETDRAAVER---------------AMERTGVA-QFADRPVTSLSGGE 144
|
170 180
....*....|....*....|....*....
gi 39930335 449 RMRVSLARALFMEPTLLMLDEPTNHLDLN 477
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDIN 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
426-499 |
2.15e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 426 ILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL-NAVIWLN-----NYLQGwrKTLLIVSHD 499
Cdd:PRK11629 129 MLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDArNADSIFQllgelNRLQG--TAFLVVTHD 205
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
619-827 |
2.24e-08 |
|
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: 57.95 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQK-PLFKNLDFGIDMDSRICIVGPNGVGKSTLLllltgkltptngemrknhRLKIGFFNQQY-------- 689
Cdd:TIGR03375 466 FRNVSFAYPGQEtPALDNVSLTIRPGEKVAIIGRIGSGKSTLL------------------KLLLGLYQPTEgsvlldgv 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 -AEQLHMEEtpteyLQRSFNLPYQDAR-----------------------KCLGRFGLE----SHAH--TIQI----CKL 735
Cdd:TIGR03375 528 dIRQIDPAD-----LRRNIGYVPQDPRlfygtlrdnialgapyaddeeilRAAELAGVTefvrRHPDglDMQIgergRSL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 736 SGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINDYkgAVIVVSHDA-------RLItetncqlwvV 804
Cdd:TIGR03375 603 SGGQRQAVALARALLRDPPILLLDEPTSAMDNRSeerfKDRLKRWLAGK--TLVLVTHRTslldlvdRII---------V 671
|
250 260
....*....|....*....|...
gi 39930335 805 EEQGVSQIDGDfddyKREVLEAL 827
Cdd:TIGR03375 672 MDNGRIVADGP----KDQVLEAL 690
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
313-518 |
2.60e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.48 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRALSIP-------------PNIDVLLCEQE-------------VVADET 366
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITsgdlivdglkvndPKVDERLIRQEagmvfqqfylfphLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 367 PAVQAV-LRADTKrlrlleeerrlqgqlEQGDDTAAEKLEKVyeelratgaaaaeakarrilaglGFDPEMQNRPTQkFS 445
Cdd:PRK09493 98 VMFGPLrVRGASK---------------EEAEKQARELLAKV-----------------------GLAERAHHYPSE-LS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 446 GGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:PRK09493 139 GGQQQRVAIARALAVKPKLMLFDEPTSALDpelRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
307-479 |
2.82e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.81 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 307 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLcEQEVVADETPAVQavlradtkrlrlleee 386
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILA--GLSPPLAGRVLL-NGGPLDFQRDSIA---------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 387 rrlQGQLEQGDDTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPeMQNRPTQKFSGGWRMRVSLARALFMEPTLLM 466
Cdd:cd03231 73 ---RGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170
....*....|...
gi 39930335 467 LDEPTNHLDLNAV 479
Cdd:cd03231 149 LDEPTTALDKAGV 161
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
619-790 |
2.92e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.40 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFkNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-KNH----------------RLK 681
Cdd:COG4161 5 LKNINCFYGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiAGHqfdfsqkpsekairllRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 682 IGFFNQQYAEQLHM--EETPTEYLQRSFNLPYQDAR----KCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDV 755
Cdd:COG4161 84 VGMVFQQYNLWPHLtvMENLIEAPCKVLGLSKEQARekamKLLARLRLTDKADRFPL-HLSGGQQQRVAIARALMMEPQV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 39930335 756 LILDEPTNNLDIESIDALGEAINDYKGAVI---VVSHD 790
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHE 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
296-498 |
2.98e-08 |
|
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: 55.48 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPP--NIDVLLCEQE------------- 360
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD---LPPtyGNDVRLFGERrggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 361 -VVadeTPAVQAVLRADtkrlrlleeerrlqgqleqgddtaaeklEKVYE----------ELRATGAAAAEAKARRILAG 429
Cdd:COG1119 81 gLV---SPALQLRFPRD----------------------------ETVLDvvlsgffdsiGLYREPTDEQRERARELLEL 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 430 LGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSH 498
Cdd:COG1119 130 LGLA-HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
395-499 |
3.24e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.28 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 395 QGDDTAAEKLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHL 474
Cdd:COG4608 125 HGLASKAERRERVAE----------------LLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
90 100 110
....*....|....*....|....*....|..
gi 39930335 475 DLN--A-VIwlnNYLQGWRK----TLLIVSHD 499
Cdd:COG4608 189 DVSiqAqVL---NLLEDLQDelglTYLFISHD 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
712-801 |
3.42e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 712 QDARKCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDA----LGEaINDYKG-AVIV 786
Cdd:PRK11629 124 SRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSifqlLGE-LNRLQGtAFLV 201
|
90
....*....|....*
gi 39930335 787 VSHDARLITETNCQL 801
Cdd:PRK11629 202 VTHDLQLAKRMSRQL 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
445-519 |
3.83e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.67 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------------LNAViwlnnylqGwrKTLLIVSHDQGFLDDVCTDII 511
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLDpetsweimelleeINRR--------G--TTVLIATHDLELVDRMPKRVL 208
|
....*...
gi 39930335 512 HLDTQRLH 519
Cdd:COG2884 209 ELEDGRLV 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
313-500 |
4.06e-08 |
|
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: 55.04 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLcEQEVVADETPAVQAV-------------------- 372
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIA--GLERPDSGTILF-GGEDATDVPVQERNVgfvfqhyalfrhmtvfdnva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 --LRADTKRLRLleeerrlqgqleqgddTAAEKLEKVYEELRATGaaaaeakarriLAGLGfdpemqNRPTQKFSGGWRM 450
Cdd:cd03296 97 fgLRVKPRSERP----------------PEAEIRAKVHELLKLVQ-----------LDWLA------DRYPAQLSGGQRQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 451 RVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLqgwRK-------TLLIVSHDQ 500
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWL---RRlhdelhvTTVFVTHDQ 197
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
426-543 |
4.26e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 426 ILAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGF 502
Cdd:COG4161 125 LLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQVIVTHEVEF 203
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 39930335 503 LDDVCTDIIHLDTQRLHYYrGNYMTFkkmyQQKQKELLKQY 543
Cdd:COG4161 204 ARKVASQVVYMEKGRIIEQ-GDASHF----TQPQTEAFAHY 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
294-499 |
4.34e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 55.02 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 294 SDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLK---------------------HIANRALS----- 347
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKcfarlltpqsgtvflgdkpisMLSSRQLArrlal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 348 ------IPPNIDVllceQEVVA-DETPAVqavlradtkrlrlleeerRLQGQLEQGD----DTAAEKLEKVyeelratga 416
Cdd:PRK11231 81 lpqhhlTPEGITV----RELVAyGRSPWL------------------SLWGRLSAEDnarvNQAMEQTRIN--------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 417 aaaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTL 493
Cdd:PRK11231 130 ------------------HLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtqgKTV 191
|
....*.
gi 39930335 494 LIVSHD 499
Cdd:PRK11231 192 VTVLHD 197
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
445-506 |
4.50e-08 |
|
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: 56.68 E-value: 4.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDDV 506
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArgaTVVVITHRPSLLAAV 533
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
735-790 |
4.74e-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: 53.59 E-value: 4.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 735 LSGG--QKarVVFA-ELAcREPDVLILDEPTNNLDIESIDALGEAINDYK---GAVIVVSHD 790
Cdd:cd03215 105 LSGGnqQK--VVLArWLA-RDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSE 163
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
622-808 |
5.08e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.40 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQ--KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQLHMEETP 699
Cdd:cd03248 17 VTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 700 TEYLQRSF--NLPYQDARKCLGRF---GLESHAHT-IQI-------------CKLSGGQKARVVFAELACREPDVLILDE 760
Cdd:cd03248 97 PVLFARSLqdNIAYGLQSCSFECVkeaAQKAHAHSfISElasgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 39930335 761 PTNNLDIESIDALGEAINDY--KGAVIVVSHdaRLITETNCQLWVVEEQG 808
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWpeRRTVLVIAH--RLSTVERADQILVLDGG 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
435-500 |
5.15e-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: 54.55 E-value: 5.15e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQ 500
Cdd:cd03300 122 GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQ 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
445-514 |
5.26e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 5.26e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
298-499 |
5.29e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.68 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 298 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPnidvllcEQEVVADETPAVQAvlRADT 377
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA--GLETPS-------AGELLAGTAPLAEA--REDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 378 KRLRLleeerrlqgqleqgdDTAAEKLEKVYEELRATGAAAAEAKARRILAGLGFDPEMQNRPTqKFSGGWRMRVSLARA 457
Cdd:PRK11247 84 RLMFQ---------------DARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPA-ALSGGQKQRVALARA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 39930335 458 LFMEPTLLMLDEPTNHLDLNAVIWLNNYLQG-WRK---TLLIVSHD 499
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESlWQQhgfTVLLVTHD 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
690-790 |
5.64e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 AEQLHMEETPTEYLQRS-FNLpyqdarkclgrfgleshahtiqicklSGGQKARVVFAELACREPDVLILDEPTNNLD-- 766
Cdd:PRK13651 146 AKYIELVGLDESYLQRSpFEL--------------------------SGGQKRRVALAGILAMEPDFLVFDEPTAGLDpq 199
|
90 100
....*....|....*....|....*.
gi 39930335 767 --IESIDALGEaINDYKGAVIVVSHD 790
Cdd:PRK13651 200 gvKEILEIFDN-LNKQGKTIILVTHD 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
629-796 |
6.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 629 QKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR---------------KNHRLKIGFFNQQYAEQL 693
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 694 hMEET---PTEYLQRSFNLPYQDAR----KCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:PRK13641 99 -FENTvlkDVEFGPKNFGFSEDEAKekalKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190
....*....|....*....|....*....|...
gi 39930335 767 IESIDALGEAINDYKGA---VIVVSHDARLITE 796
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAghtVILVTHNMDDVAE 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
622-808 |
6.85e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 54.15 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM-----------RKNHRLKIGFFNQqya 690
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVLQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 691 EQLHMEETPTEYLqrSFNLPYQDARKCLgRFGLESHAHTIqICK---------------LSGGQKARVVFAELACREPDV 755
Cdd:cd03254 85 DTFLFSGTIMENI--RLGRPNATDEEVI-EAAKEAGAHDF-IMKlpngydtvlgenggnLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 756 LILDEPTNNLDIESIDALGEAI-NDYKG-AVIVVSHdaRLITETNCQLWVVEEQG 808
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALeKLMKGrTSIIIAH--RLSTIKNADKILVLDDG 213
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
313-497 |
6.95e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 54.20 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIP-PNIDVLLCEQEVVADETPavqavlradtkrlrlleeerRLQG 391
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGtTSGQILFNGQPRKPDQFQ--------------------KCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 392 QLEQgDDTAAEKLeKVYEEL----------RATGAAAAEAKARRILAGLGfDPEMQNRPTQKFSGGWRMRVSLARALFME 461
Cdd:cd03234 85 YVRQ-DDILLPGL-TVRETLtytailrlprKSSDAIRKKRVEDVLLRDLA-LTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 39930335 462 PTLLMLDEPTNHLD----LNAVIWLNNYLQgwRKTLLIVS 497
Cdd:cd03234 162 PKVLILDEPTSGLDsftaLNLVSTLSQLAR--RNRIVILT 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
426-499 |
7.31e-08 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 55.50 E-value: 7.31e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 426 ILAGLGFDPEMQnRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVI-WLNNYLQGWRKTLLIVSHD 499
Cdd:TIGR02142 115 VIELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHS 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
687-794 |
7.72e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.30 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 687 QQYAEQLHMEEtptEYLQRSFNLpyqdarkclgrfgleshahtiqicKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:COG0396 120 KEKMKELGLDE---DFLDRYVNE------------------------GFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
90 100 110
....*....|....*....|....*....|.
gi 39930335 767 IESIDALGEAINDYKG---AVIVVSHDARLI 794
Cdd:COG0396 173 IDALRIVAEGVNKLRSpdrGILIITHYQRIL 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
734-793 |
8.04e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 55.94 E-value: 8.04e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY-KGA-VIVVSHdaRL 793
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmKGRtTIVIAH--RL 535
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
622-797 |
8.50e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.37 E-value: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQKPL-FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMrknhrlkigFFNQQYAEQLHMEEtpt 700
Cdd:PRK13648 13 VSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITDDNFEK--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 701 eyLQRSFNLPYQDA-RKCLGR-------FGLESHA------HTI--QICK--------------LSGGQKARVVFAELAC 750
Cdd:PRK13648 81 --LRKHIGIVFQNPdNQFVGSivkydvaFGLENHAvpydemHRRvsEALKqvdmleradyepnaLSGGQKQRVAIAGVLA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 39930335 751 REPDVLILDEPTNNLDIESIDALGEAINDYKG----AVIVVSHDarlITET 797
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD---LSEA 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
306-498 |
8.51e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.81 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 306 HGKELFVNA-DLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvadETPAVQAVLRAdtkrlrlle 384
Cdd:PRK13537 17 YGDKLVVDGlSFHVQRGECFGLLGPNGAGKTTTLRMLL--GLTHPDAGSISLCGEPV---PSRARHARQRV--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 385 eerrlqGQLEQGDD-----TAAEKLeKVYEELRATGAAAAEAKARRILAglgFdPEMQNR---PTQKFSGGWRMRVSLAR 456
Cdd:PRK13537 83 ------GVVPQFDNldpdfTVRENL-LVFGRYFGLSAAAARALVPPLLE---F-AKLENKadaKVGELSGGMKRRLTLAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 39930335 457 ALFMEPTLLMLDEPTNHLDLNA--VIW--LNNYLQGwRKTLLIVSH 498
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTH 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
276-504 |
1.06e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 276 FSVSQAEVSSRQAMLENASDI--KLEKFSISAHGKELFVNADLyivagrryGLVGPNGKGKTTLLKHIANR----ALSIP 349
Cdd:PRK13409 326 FEERPPRDESERETLVEYPDLtkKLGDFSLEVEGGEIYEGEVI--------GIVGPNGIGKTTFAKLLAGVlkpdEGEVD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 350 PNIDVLLCEQEVVADETPAVQAVLRAdtkrlrlleeerrlqgqleqgddtAAEKLEKVYEElratgaaaaeakaRRILAG 429
Cdd:PRK13409 398 PELKISYKPQYIKPDYDGTVEDLLRS------------------------ITDDLGSSYYK-------------SEIIKP 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 430 LGFDPEMQnRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQGFLD 504
Cdd:PRK13409 441 LQLERLLD-KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMID 518
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
735-790 |
1.21e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.62 E-value: 1.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 735 LSGGQKARV----VFAELACREPD--VLILDEPTNNLDI----ESIDALGEAINDYKGAVIVVSHD 790
Cdd:PRK13548 135 LSGGEQQRVqlarVLAQLWEPDGPprWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
733-795 |
1.23e-07 |
|
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: 53.36 E-value: 1.23e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 733 CKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHDARLIT 795
Cdd:cd03245 139 RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
315-518 |
1.28e-07 |
|
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: 53.14 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 315 DLYIVAGRRYGLVGPNGKGKTT-------LLKHIANRAlsIPPNIDVLlCEQEVVADETPAVQAVLRADtkrlrlleeer 387
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRA--TVAGHDVV-REPREVRRRIGIVFQDLSVD----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 388 rlqGQLeqgddTAAEKLEkVYEELRATGAAAAEAKARRILAGLGFdPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLML 467
Cdd:cd03265 86 ---DEL-----TGWENLY-IHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 468 DEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEefgmTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
430-498 |
1.31e-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: 53.24 E-value: 1.31e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 430 LGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGW--RKTLLIVSH 498
Cdd:cd03248 138 SGYDTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
619-790 |
1.38e-07 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 52.91 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN---------HRLKIGFFNQQY 689
Cdd:cd03259 3 LKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvppERRNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 AEQLHM--EETpTEYLQRSFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTN 763
Cdd:cd03259 82 ALFPHLtvAEN-IAFGLKLRGVPKAEIRArvreLLELVGLEGLLNR-YPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190
....*....|....*....|....*....|.
gi 39930335 764 NLDIES----IDALGEAINDYKGAVIVVSHD 790
Cdd:cd03259 160 ALDAKLreelREELKELQRELGITTIYVTHD 190
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
430-500 |
1.40e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 53.03 E-value: 1.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 430 LGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQ 500
Cdd:cd03301 118 LQIEHLLDRKPKQ-LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
320-476 |
1.51e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.20 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 320 AGRRYGLVGPNGKGKTTLlkhiaNRALSI--PPNIDVLLCEQEVVADETPAVQAVLRADTkrlrlleeerrlQ------- 390
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTL-----ARLLTMieTPTGGELYYQGQDLLKADPEAQKLLRQKI------------Qivfqnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 391 ----------GQLEQ-----GDDTAAEKLEKVYEelratgaaaaeakarrILAGLGFDPEMQNRPTQKFSGGWRMRVSLA 455
Cdd:PRK11308 103 gslnprkkvgQILEEpllinTSLSAAERREKALA----------------MMAKVGLRPEHYDRYPHMFSGGQRQRIAIA 166
|
170 180
....*....|....*....|.
gi 39930335 456 RALFMEPTLLMLDEPTNHLDL 476
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDV 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
677-790 |
1.59e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 53.90 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 677 NHRLKIGffnQQYAE--QLHMEETPTEYLQRsfnlpyqdARKCLGRFGL---ESHA----HTiqickLSGGQKARVVFA- 746
Cdd:COG0444 100 NPVMTVG---DQIAEplRIHGGLSKAEARER--------AIELLERVGLpdpERRLdrypHE-----LSGGMRQRVMIAr 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 39930335 747 ELACrEPDVLILDEPTNNLDIeSIDA-----LGEAINDYKGAVIVVSHD 790
Cdd:COG0444 164 ALAL-EPKLLIADEPTTALDV-TIQAqilnlLKDLQRELGLAILFITHD 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
438-500 |
1.72e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.32 E-value: 1.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 438 NR-PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVI----WLNNYLQGWRKTLLIVSHDQ 500
Cdd:PRK10851 131 DRyPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
712-807 |
1.80e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 712 QDARKCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINDYKGAVIVV 787
Cdd:PRK10584 125 NGAKALLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILV 203
|
90 100
....*....|....*....|
gi 39930335 788 SHDARLITETNCQLWVVEEQ 807
Cdd:PRK10584 204 THDLQLAARCDRRLRLVNGQ 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
325-510 |
1.83e-07 |
|
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: 52.51 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 325 GLVGPNGKGKTTLLKHIANRalsIPPNI-DVLLCEQEVVADETPAVQAVlradtkrlrlleeerrlqGQLEQGDD----- 398
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGE---LRPTSgTAYINGYSIRTDRKAARQSL------------------GYCPQFDAlfdel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 399 TAAEKLEkVYEELRATGAAAAEAKARRILAGLGFDPEmQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA 478
Cdd:cd03263 91 TVREHLR-FYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 39930335 479 --VIWlnNYLQGWRK--TLLIVSHDQGFLDDVCTDI 510
Cdd:cd03263 169 rrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
297-475 |
1.94e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.48 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 297 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA-----------------NRALSIPP---NI---- 352
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgtlspafsasgevllngRRLTALPAeqrRIgilf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 353 -DVLLCEQEVVADE----TPAvqAVLRADTKrlrlleeerrlqgqleqgdDTAAEKLEKvyeelratgaaaaeakarril 427
Cdd:COG4136 83 qDDLLFPHLSVGENlafaLPP--TIGRAQRR-------------------ARVEQALEE--------------------- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 39930335 428 AGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:COG4136 121 AGLA---GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
279-498 |
2.17e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 279 SQAEVSSRQAMLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLlce 358
Cdd:PRK13536 25 GISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 359 qevvADETPAVQAVLRADTkrlrlleeerrlqGQLEQGDD-----TAAEKLeKVYEELRATGAAAAEAKARRILAGLGFD 433
Cdd:PRK13536 102 ----GVPVPARARLARARI-------------GVVPQFDNldlefTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 434 PEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA--VIW--LNNYL-QGwrKTLLIVSH 498
Cdd:PRK13536 164 SKADARVSD-LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLLaRG--KTILLTTH 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
304-475 |
2.40e-07 |
|
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: 51.78 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 304 SAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLceqevvaDETPAVQAVLRADTkrlrll 383
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLI-------NGRPLDKRSFRKII------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 384 eeerrlqGQLEQgDDTAAEKLeKVYEELRatgaaaaeakarrILAGLgfdpemqnrptQKFSGGWRMRVSLARALFMEPT 463
Cdd:cd03213 85 -------GYVPQ-DDILHPTL-TVRETLM-------------FAAKL-----------RGLSGGERKRVSIALELVSNPS 131
|
170
....*....|..
gi 39930335 464 LLMLDEPTNHLD 475
Cdd:cd03213 132 LLFLDEPTSGLD 143
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
617-790 |
2.43e-07 |
|
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: 52.47 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEGQKPLFKNLDfGIDMDSR----ICIVGPNGVGKS------TLLLLLTGKLTPTNGEMRKNHRLKIGFFN 686
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALE-DISLSVEegefVALVGPSGCGKStllriiAGLERPTSGEVLVDGEPVTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 687 QQYA-------EQ-----LHMEETPTEYLQRsfnlpyqDARKCLGRFGLESHAH--TIQickLSGGQKARVVFAE-LAcR 751
Cdd:cd03293 80 QQDAllpwltvLDnvalgLELQGVPKAEARE-------RAEELLELVGLSGFENayPHQ---LSGGMRQRVALARaLA-V 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 39930335 752 EPDVLILDEPTNNLDI---ESI-DALGEAINDYKGAVIVVSHD 790
Cdd:cd03293 149 DPDVLLLDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
439-500 |
2.65e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 53.56 E-value: 2.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 439 RPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA----VIWLNNYLQGWRKTLLIVSHDQ 500
Cdd:COG3842 132 YPHQ-LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLreemREELRRLQRELGITFIYVTHDQ 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
275-511 |
2.82e-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: 54.02 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 275 DFSVSQAEVSSRQAMLENASDI--KLEKFSISAHGKELFVNADLyivagrryGLVGPNGKGKTTLLKHIANR----ALSI 348
Cdd:COG1245 326 EFEVHAPRREKEEETLVEYPDLtkSYGGFSLEVEGGEIREGEVL--------GIVGPNGIGKTTFAKILAGVlkpdEGEV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 349 PPNIDVLLCEQEVVADETPAVQAVLRadtkrlrlleeerrlqgqleqgdDTAAEKLEKVYEElratgaaaaeakaRRILA 428
Cdd:COG1245 398 DEDLKISYKPQYISPDYDGTVEEFLR-----------------------SANTDDFGSSYYK-------------TEIIK 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 429 GLGFDPEMQnRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQGFLD 504
Cdd:COG1245 442 PLGLEKLLD-KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLID 520
|
....*..
gi 39930335 505 DVCTDII 511
Cdd:COG1245 521 YISDRLM 527
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
714-793 |
3.26e-07 |
|
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: 52.05 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 714 ARKCLGRFGLES--HAHTIQickLSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALgEAINDYKGA-VIV 786
Cdd:COG4181 127 ARALLERVGLGHrlDHYPAQ---LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLL-FELNRERGTtLVL 202
|
....*..
gi 39930335 787 VSHDARL 793
Cdd:COG4181 203 VTHDPAL 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
289-513 |
3.35e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.02 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 289 MLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPPNIDVLLCEQEVVADETPa 368
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL---ISPTSGTLLFEGEDISTLKP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 369 vqavlradtkrlrlleeeRRLQGQLEQGDDTAAEKLEKVYEEL----RATGAAAAEAKARRILAGLGFDPEMQNRPTQKF 444
Cdd:PRK10247 77 ------------------EIYRQQVSYCAQTPTLFGDTVYDNLifpwQIRNQQPDPAIFLDDLERFALPDTILTKNIAEL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD------LNAVIwlNNYLQGWRKTLLIVSHDQgflDDV--CTDIIHL 513
Cdd:PRK10247 139 SGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEII--HRYVREQNIAVLWVTHDK---DEInhADKVITL 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
307-479 |
3.79e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.41 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 307 GKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETP----------AVQAVLrad 376
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIA--GLLPPAAGTIKLDGGDIDDPDVAeachylghrnAMKPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 377 tkrlrlleeerrlqgqleqgddTAAEKLE---KVY--EELRATGAaaaeakarriLAGLGFDPeMQNRPTQKFSGGWRMR 451
Cdd:PRK13539 89 ----------------------TVAENLEfwaAFLggEELDIAAA----------LEAVGLAP-LAHLPFGYLSAGQKRR 135
|
170 180
....*....|....*....|....*...
gi 39930335 452 VSLARALFMEPTLLMLDEPTNHLDLNAV 479
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
622-815 |
3.94e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.43 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGY-EGQKPLfKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-----------KNHRLKIGFFNQQY 689
Cdd:PRK13647 10 LHFRYkDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevnaeneKWVRSKVGLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 AEQL--------------HMEETPTEYLQRSfnlpyQDARKCLGRFGLESHA--HtiqickLSGGQKARVVFAELACREP 753
Cdd:PRK13647 89 DDQVfsstvwddvafgpvNMGLDKDEVERRV-----EEALKAVRMWDFRDKPpyH------LSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 754 DVLILDEPTNNLDIESIDALGEAINDYKGA---VIVVSHDARLITETNCQLWVVEEqGVSQIDGD 815
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQgktVIVATHDVDLAAEWADQVIVLKE-GRVLAEGD 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
735-830 |
4.13e-07 |
|
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: 53.65 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESI----DALGEAINDYKGAVIVVSHDARLITE-TNCQLWVveEQGV 809
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWL--ENGE 246
|
90 100
....*....|....*....|.
gi 39930335 810 SQIDGDFDDYKREVLEALGEV 830
Cdd:TIGR03269 247 IKEEGTPDEVVAVFMEGVSEV 267
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
431-506 |
4.28e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 431 GFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAV-----IWLNNYLQGwrKTLLIVSHDqgfLDD 505
Cdd:PRK13651 153 GLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkeileIFDNLNKQG--KTIILVTHD---LDN 227
|
.
gi 39930335 506 V 506
Cdd:PRK13651 228 V 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
622-789 |
4.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.43 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQKPLFKNLDFGIDMD----SRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR---------------KNHRLKI 682
Cdd:PRK13643 7 VNYTYQPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkeiKPVRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 683 GFFNQQYAEQLhMEET---PTEYLQRSFNLPYQDARKC----LGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDV 755
Cdd:PRK13643 87 GVVFQFPESQL-FEETvlkDVAFGPQNFGIPKEKAEKIaaekLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 39930335 756 LILDEPTNNLDIES---IDALGEAINDYKGAVIVVSH 789
Cdd:PRK13643 166 LVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
628-768 |
5.15e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.63 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-------------KNHRLKIGFFNQQYAEQLH 694
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvndpkvdeRLIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 695 MEET------PTEYLQRSFNLPYQDARKCLGRFGLESHAHTIQiCKLSGGQKARVVFAE-LACRePDVLILDEPTNNLDI 767
Cdd:PRK09493 92 LTALenvmfgPLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARaLAVK-PKLMLFDEPTSALDP 169
|
.
gi 39930335 768 E 768
Cdd:PRK09493 170 E 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
617-790 |
5.62e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.19 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGY---EGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGE------------------MR 675
Cdd:PRK10535 5 LELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvatldadalaqLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 676 KNHrlkIGFFNQQYAEQLHME-----ETPTEYLQRSFNLPYQDARKCLGRFGLESHAHtIQICKLSGGQKARVVFAELAC 750
Cdd:PRK10535 85 REH---FGFIFQRYHLLSHLTaaqnvEVPAVYAGLERKQRLLRAQELLQRLGLEDRVE-YQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 39930335 751 REPDVLILDEPTNNLDIES---IDALGEAINDYKGAVIVVSHD 790
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
426-518 |
6.16e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.61 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 426 ILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN---AVIWLNNYLQGWRKT-LLIVSHDQG 501
Cdd:PRK10419 134 MLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlqaGVIRLLKKLQQQFGTaCLFITHDLR 213
|
90
....*....|....*..
gi 39930335 502 FLDDVCTDIIHLDTQRL 518
Cdd:PRK10419 214 LVERFCQRVMVMDNGQI 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
445-513 |
6.18e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 51.73 E-value: 6.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHL 513
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDpelVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFL 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
313-518 |
6.95e-07 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 51.73 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLRLLEEERRLQGQ 392
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLL--GLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 LEQgddTAAEKLEkvyeELRATGAAAAEAKARRILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTN 472
Cdd:TIGR02769 107 VRQ---IIGEPLR----HLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 39930335 473 HLD--LNAVI--WLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:TIGR02769 180 NLDmvLQAVIleLLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
616-766 |
6.98e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.11 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR----------KNHRLKIGFF 685
Cdd:PRK13537 7 PIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 NQqyAEQLHMEETPTEYLQ---RSFNLPYQDARKC---LGRFG-LESHAHTiQICKLSGGQKARVVFAELACREPDVLIL 758
Cdd:PRK13537 86 PQ--FDNLDPDFTVRENLLvfgRYFGLSAAAARALvppLLEFAkLENKADA-KVGELSGGMKRRLTLARALVNDPDVLVL 162
|
....*...
gi 39930335 759 DEPTNNLD 766
Cdd:PRK13537 163 DEPTTGLD 170
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
712-789 |
7.49e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.77 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 712 QDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG---AVIVVS 788
Cdd:PRK13631 154 KLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVIT 233
|
.
gi 39930335 789 H 789
Cdd:PRK13631 234 H 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
735-794 |
7.70e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.50 E-value: 7.70e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIND--YKGAVIVVSHDARLI 794
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRSTLA 547
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
628-789 |
7.78e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRlkiGFFNQQYAEQLH-------MEETPT 700
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHylghrnaMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 701 -----EYLQRSFNLPYQDARKCLGRFGLeSHAHTIQICKLSGGQKARVVFAEL-ACREPdVLILDEPTNNLDIESIDALG 774
Cdd:PRK13539 90 vaenlEFWAAFLGGEELDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLlVSNRP-IWILDEPTAALDAAAVALFA 167
|
170
....*....|....*...
gi 39930335 775 EAINDYK---GAVIVVSH 789
Cdd:PRK13539 168 ELIRAHLaqgGIVIAATH 185
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
734-825 |
8.66e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG----AVIVVSHDARLITETNcQLWVV---EE 806
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrITIIIAHRLSTIRYAN-TIFVLsnrER 657
|
90
....*....|....*....
gi 39930335 807 QGVSQIDGDFDDYKREVLE 825
Cdd:PTZ00265 658 GSTVDVDIIGEDPTKDNKE 676
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
296-475 |
8.98e-07 |
|
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: 51.03 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRaLSIPPNIDVLLCEQEVVADETPAVQAVlR 374
Cdd:cd03256 1 IEVENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL-NG-LVEPTSGSVLIDGTDINKLKGKALRQL-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 375 ADTkrlrlleeerrlqGQLEQ-----GDDTAAE-----KLEKV--YEELRATGAAAAEAKARRILAGLGFDpEMQNRPTQ 442
Cdd:cd03256 78 RQI-------------GMIFQqfnliERLSVLEnvlsgRLGRRstWRSLFGLFPKEEKQRALAALERVGLL-DKAYQRAD 143
|
170 180 190
....*....|....*....|....*....|...
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
426-499 |
9.61e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 9.61e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 426 ILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHD 499
Cdd:PRK15079 144 MMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemglSLIFIAHD 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
325-499 |
9.77e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 50.87 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 325 GLVGPNGKGKTTLLKHIANR-----ALSIPPNIDVLLCEQEVVADETPAVQAVLRadtkrlrlleeerrlqgqleqgddt 399
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVlkpdeGDIEIELDTVSYKPQYIKADYEGTVRDLLS------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 400 aaEKLEKVYEElratgaaaaEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---- 475
Cdd:cd03237 84 --SITKDFYTH---------PYFKTEIAKPLQIEQILDREVPE-LSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqr 151
|
170 180
....*....|....*....|....
gi 39930335 476 LNAVIWLNNYLQGWRKTLLIVSHD 499
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHD 175
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
628-790 |
1.06e-06 |
|
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: 50.58 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM----------RKNHRLKIGF---FNQQYaEQLh 694
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYcpqFDALF-DEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 695 meeTPTEYLQ---RSFNLPYQDARKC----LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI 767
Cdd:cd03263 91 ---TVREHLRfyaRLKGLPKSEIKEEvellLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180
....*....|....*....|....*
gi 39930335 768 ESIDALGEAINDYKG--AVIVVSHD 790
Cdd:cd03263 167 ASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
619-766 |
1.09e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.76 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR----------KNHRLKIGFFNQq 688
Cdd:PRK13536 44 LAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 yAEQLHMEETPTEYL---QRSFNLPYQDARKC---LGRFG-LESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEP 761
Cdd:PRK13536 122 -FDNLDLEFTVRENLlvfGRYFGMSTREIEAVipsLLEFArLESKADA-RVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
....*
gi 39930335 762 TNNLD 766
Cdd:PRK13536 200 TTGLD 204
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
619-790 |
1.10e-06 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 50.86 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGY---EGQKPLFKNLDFGIDMDSRICIVGPNGVGKStlllll------tgkltPTNGEMRKNHRLKIGF-FnQQ 688
Cdd:COG1116 10 LRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKStllrliaglekptsgevLVDGKPVTGPGPDRGVvF-QE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 YA-------EQ---LHME---ETPTEYLQRsfnlpyqdARKCLGRFGLESHAHtiqicK----LSGGQKARVVFAE-LAc 750
Cdd:COG1116 89 PAllpwltvLDnvaLGLElrgVPKAERRER--------ARELLELVGLAGFED-----AyphqLSGGMRQRVAIARaLA- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 39930335 751 REPDVLILDEPTNNLDIESIDALGEAI----NDYKGAVIVVSHD 790
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
628-768 |
1.16e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 50.38 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKS---------------------TLLLLLTGkltptngEMRKnHRLKIGFFN 686
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKStllrcinlleepdsgtitvdgEDLTDSKK-------DINK-LRRKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 687 QQYaeQL--HM------EETPTEYLQRSFNLPYQDARKCLGRFGLESHAHT--IQickLSGGQKARVVFAELACREPDVL 756
Cdd:COG1126 84 QQF--NLfpHLtvlenvTLAPIKVKKMSKAEAEERAMELLERVGLADKADAypAQ---LSGGQQQRVAIARALAMEPKVM 158
|
170
....*....|..
gi 39930335 757 ILDEPTNNLDIE 768
Cdd:COG1126 159 LFDEPTSALDPE 170
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
434-507 |
1.23e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.26 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 434 PEMQNRPT---QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD--LNAVIW--LNNYLQGWRKTLLIVSHDQGFLDDV 506
Cdd:PRK09473 149 PEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtVQAQIMtlLNELKREFNTAIIMITHDLGVVAGI 228
|
.
gi 39930335 507 C 507
Cdd:PRK09473 229 C 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
316-499 |
1.25e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.89 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 316 LYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEVvadeTPAVQAVLRA---------DTKRLRLLEEE 386
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHL--NGIYLPQRGRVKVMGREV----NAENEKWVRSkvglvfqdpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 387 RRLQGQLEQGDDtAAEKLEKVYEELRATGAAaaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLM 466
Cdd:PRK13647 100 DVAFGPVNMGLD-KDEVERRVEEALKAVRMW-----------------DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 39930335 467 LDEPTNHLD------LNAVIW-LNNylQGwrKTLLIVSHD 499
Cdd:PRK13647 162 LDEPMAYLDprgqetLMEILDrLHN--QG--KTVIVATHD 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
443-498 |
1.30e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 52.09 E-value: 1.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAviwLNNYLQGwrKTLLIVSH 498
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMKG--RTTIVIAH 533
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
735-789 |
1.83e-06 |
|
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: 48.58 E-value: 1.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG---AVIVVSH 789
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
718-798 |
1.84e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 718 LGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLILDEPTNNLD---IESIDALGEAINDYKGAVIVVSHDARLI 794
Cdd:PRK10908 122 LDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
....
gi 39930335 795 TETN 798
Cdd:PRK10908 201 SRRS 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
296-513 |
1.85e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFV-----NADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNI---DVLLCEQEVVADETP 367
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 368 AVQAV----------LRADTKRLRLLEEERRLQGQLEQGDDTAAEKLEKVyeelratgaaaaeakarrilaglGFDPEMQ 437
Cdd:PRK13643 82 VRKKVgvvfqfpesqLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----------------------GLADEFW 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR---KTLLIVSHdqgFLDDVC--TDIIH 512
Cdd:PRK13643 139 EKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTH---LMDDVAdyADYVY 215
|
.
gi 39930335 513 L 513
Cdd:PRK13643 216 L 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
445-514 |
1.90e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 49.99 E-value: 1.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNylQGWrkTLLIVSHDQGFLDDVCTDIIHLD 514
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevLDVMRDLAK--EGM--TMVVVTHEMGFAREVADRVVFMD 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
438-506 |
2.25e-06 |
|
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: 50.48 E-value: 2.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIwlnNYLQGWRKTL----LIVSHDqgfLDDV 506
Cdd:COG4148 128 DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkAEIL---PYLERLRDELdipiLYVSHS---LDEV 197
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
325-471 |
2.30e-06 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 49.35 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 325 GLVGPNGKGKTTLLKHIANralSIPP----------NIDVLLCEQ-------------EVVADETpaVQAVLRAdtkrlr 381
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMG---LLPPrsgsirfdgrDITGLPPHEraragigyvpegrRIFPELT--VEENLLL------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 382 lleeerrlqGQLEQGDDTAAEKLEKVYEELRatgaaaaeakarrILAglgfdpEMQNRPTQKFSGGWRMRVSLARALFME 461
Cdd:cd03224 99 ---------GAYARRRAKRKARLERVYELFP-------------RLK------ERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170
....*....|
gi 39930335 462 PTLLMLDEPT 471
Cdd:cd03224 151 PKLLLLDEPS 160
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
445-790 |
2.34e-06 |
|
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: 50.96 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDQGFLDDVCTDIIHLDtqrlhy 520
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasgiSMVLTSHWPEVIEDLSDKAIWLE------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 521 yrgnymtfkkmyqqkqkellkqyekqekklkelkaggKSTKQAEKQTKEVLTRKQQKCRRKNQDEESQEPPELLKRpKEY 600
Cdd:TIGR03269 244 -------------------------------------NGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKV-RNV 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 601 TVRFTfpdpPPLSPPVLGLHGVTFG-YEGQKplfknldFGIdmdsriciVGPNGVGKSTLLLLLTGKLTPTNGE------ 673
Cdd:TIGR03269 286 SKRYI----SVDRGVVKAVDNVSLEvKEGEI-------FGI--------VGTSGAGKTTLSKIIAGVLEPTSGEvnvrvg 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 674 -----MRK-----NHRLK--IGFFNQQYAEQLHME--ETPTEYLqrSFNLPYQDARK----CLGRFGL-ESHAHTI---Q 731
Cdd:TIGR03269 347 dewvdMTKpgpdgRGRAKryIGILHQEYDLYPHRTvlDNLTEAI--GLELPDELARMkaviTLKMVGFdEEKAEEIldkY 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 732 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLD-------IESIDALGEAINDykgAVIVVSHD 790
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAREEMEQ---TFIIVSHD 487
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
444-508 |
3.08e-06 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 48.93 E-value: 3.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN---AVIWLNNYLQGWRKTLLIVSHDQGFLDDVCT 508
Cdd:TIGR02324 150 FSGGEQQRVNIARGFIADYPILLLDEPTASLDAAnrqVVVELIAEAKARGAALIGIFHDEEVRELVAD 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
734-789 |
3.30e-06 |
|
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: 48.90 E-value: 3.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG---AVIVVSH 789
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTH 194
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
735-806 |
3.94e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 50.40 E-value: 3.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHdaRLIT-ETNCQLWVVEE 806
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH--RLSTiEKADEILVVED 553
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
647-794 |
4.43e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 647 CIVGPNGVGKSTLLLLltgkltptngemrknhrLKIGFFNQQYAEQLHMEETPTEYLqrsfnlPYQDARKCLGRFGLesh 726
Cdd:cd03227 25 IITGPNGSGKSTILDA-----------------IGLALGGAQSATRRRSGVKAGCIV------AAVSAELIFTRLQL--- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 727 ahtiqicklSGGQKARV----VFAELACREPDVLILDEPTNNLDIESIDALGEAINDY--KGA-VIVVSHDARLI 794
Cdd:cd03227 79 ---------SGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHLPELA 144
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
296-499 |
5.12e-06 |
|
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: 48.84 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSIS-AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIaNRALSiPPNIDVLLCEQEVVadETPAVQavLR 374
Cdd:cd03295 1 IEFENVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRLIE-PTSGEIFIDGEDIR--EQDPVE--LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 375 ADTkrlrlleeerrlqGQLEQG-----DDTAAE------KLEKVYEElratgaaAAEAKARRILAGLGFDP-EMQNRPTQ 442
Cdd:cd03295 75 RKI-------------GYVIQQiglfpHMTVEEnialvpKLLKWPKE-------KIRERADELLALVGLDPaEFADRYPH 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLqgwRKTLLIVSHD 499
Cdd:cd03295 135 ELSGGQQQRVGVARALAADPPLLLMDEPFGALDpitrdqlQEEFKRLQQEL---GKTIVFVTHD 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
734-808 |
5.56e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.91 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAE-LACrEPDVLILDEPTNNLDI----ESIDALGEAINDYKGAVIVVSHDARLItETNCQLWVVEEQG 808
Cdd:PRK10419 151 QLSGGQLQRVCLARaLAV-EPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLV-ERFCQRVMVMDNG 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
634-794 |
5.66e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.92 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 634 KNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM----------RK---NHRLKIGFFNQQYAEQLHmeeTPT 700
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepikydKKsllEVRKTVGIVFQNPDDQLF---APT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 701 EYLQRSF---NLPY---------QDARKCLGRFGLESHA-HtiqicKLSGGQKARVVFAELACREPDVLILDEPTNNLD- 766
Cdd:PRK13639 96 VEEDVAFgplNLGLskeevekrvKEALKAVGMEGFENKPpH-----HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDp 170
|
170 180 190
....*....|....*....|....*....|.
gi 39930335 767 --IESIDALGEAINDyKGAVIVVS-HDARLI 794
Cdd:PRK13639 171 mgASQIMKLLYDLNK-EGITIIIStHDVDLV 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
296-506 |
6.13e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 48.21 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELfvNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNI-DVLLCEQEVvADETPAVQAV-- 372
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAG---FLPPDSgRILWNGQDL-TALPPAERPVsm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 373 --------------------LRADTKRlrlleeerrlqgqleqgddTAAEKlEKVyeelratgaaaaeakaRRILAGLGF 432
Cdd:COG3840 76 lfqennlfphltvaqniglgLRPGLKL-------------------TAEQR-AQV----------------EQALERVGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 433 DPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHDqgfLDD 505
Cdd:COG3840 120 AGLLDRLPGQ-LSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqemLDLVDELCRERG---LTVLMVTHD---PED 192
|
.
gi 39930335 506 V 506
Cdd:COG3840 193 A 193
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
309-475 |
6.17e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.37 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 309 ELFVNADLYIVAGRRYGLVGPNGKGKTTLLKhIANRALSIPPNI----DVLLCEQEV----VADETPAVQAVLRADTKRL 380
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEArvsgEVYLDGQDIfkmdVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 381 RLLEEERRLQG-QLEQGDDTAAEKLEKVYEELRATGAAAaeakarrilaglgfdpEMQNR---PTQKFSGGWRMRVSLAR 456
Cdd:PRK14247 96 NLSIFENVALGlKLNRLVKSKKELQERVRWALEKAQLWD----------------EVKDRldaPAGKLSGGQQQRLCIAR 159
|
170
....*....|....*....
gi 39930335 457 ALFMEPTLLMLDEPTNHLD 475
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLD 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
735-788 |
6.25e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.63 E-value: 6.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 735 LSGG--QKarVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY--KG-AVIVVS 788
Cdd:COG1129 395 LSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaaEGkAVIVIS 451
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
718-790 |
6.43e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.54 E-value: 6.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 718 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI----ESIDALGEAINDYKGAVIVVSHD 790
Cdd:COG4604 120 IAYLDLEDLADR-YLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
619-790 |
6.61e-06 |
|
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: 48.45 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNH-----------RLKIGFFNQ 687
Cdd:cd03295 3 FENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 688 QYAEQLHM------------EETPTEYLQRSfnlpyqdARKCLGRFGLES------HAHtiqicKLSGGQKARVVFAELA 749
Cdd:cd03295 83 QIGLFPHMtveenialvpklLKWPKEKIRER-------ADELLALVGLDPaefadrYPH-----ELSGGQQQRVGVARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 39930335 750 CREPDVLILDEPTNNLDIESIDALGEAINDYK---GAVIV-VSHD 790
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQqelGKTIVfVTHD 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
634-823 |
6.71e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.93 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 634 KNLDFGIDMDSRICIVGPNGVGKStlllllt------gkltptNG----EMRKNHRLKIGF-FNQQyaEQLHMEETPTE- 701
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSttikmltgilvptsgevrvLGyvpfKRRKEFARRIGVvFGQR--SQLWWDLPAIDs 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 702 --YLQRSFNLPYQDARKCLGRF----GLESHAHTiQICKLSGGQKARvvfAELAC---REPDVLILDEPTNNLDIESIDA 772
Cdd:COG4586 117 frLLKAIYRIPDAEYKKRLDELvellDLGELLDT-PVRQLSLGQRMR---CELAAallHRPKILFLDEPTIGLDVVSKEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 773 LGEAINDY---KGA-VIVVSHDARLITETnCQLWVVEEQGVSQIDGDFDDYKREV 823
Cdd:COG4586 193 IREFLKEYnreRGTtILLTSHDMDDIEAL-CDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
616-790 |
6.75e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.86 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYEGQ-KPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNH-----------RLKIG 683
Cdd:PRK13635 5 IIRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 684 FFNQQYAEQ-------------LHMEETPTEYLQRSFnlpyQDArkcLGRFGLESHAHTiQICKLSGGQKARVVFAELAC 750
Cdd:PRK13635 85 MVFQNPDNQfvgatvqddvafgLENIGVPREEMVERV----DQA---LRQVGMEDFLNR-EPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 39930335 751 REPDVLILDEPTNNLD----IESIDALGEaINDYKGA-VIVVSHD 790
Cdd:PRK13635 157 LQPDIIILDEATSMLDprgrREVLETVRQ-LKEQKGItVLSITHD 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
436-500 |
6.86e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.95 E-value: 6.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 436 MQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNaviwLNNYL--------QGWRKTLLIVSHDQ 500
Cdd:PRK11432 129 FEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN----LRRSMrekirelqQQFNITSLYVTHDQ 197
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
619-790 |
7.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.44 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM------------RKNHRLKIGFFN 686
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfskLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 687 QQYAEQL--HMEETPTEYLQRSFNLPYQDARK----CLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDE 760
Cdd:PRK13644 84 QNPETQFvgRTVEEDLAFGPENLCLPPIEIRKrvdrALAEIGLEKYRHR-SPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 39930335 761 PTNNLDIESIDALGEAINDY--KGAVIV-VSHD 790
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLheKGKTIVyITHN 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
734-834 |
7.45e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 48.93 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NDYKGAVIVVSHDARLITETNCQLwVVEEQGV 809
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRV-VVMSQGN 214
|
90 100 110
....*....|....*....|....*....|
gi 39930335 810 SQIDGDFDDYKRE-----VLEALGEvmVNR 834
Cdd:PRK10851 215 IEQAGTPDQVWREpatrfVLEFMGE--VNR 242
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
445-505 |
7.82e-06 |
|
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: 47.79 E-value: 7.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFLDD 505
Cdd:cd03292 138 SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDT 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
301-498 |
8.16e-06 |
|
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: 46.92 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 301 FSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnRALSiPPNIDVLLCEQEVVADETPAVQAVlradtkrl 380
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT-GDLK-PQQGEITLDGVPVSDLEKALSSLI-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 381 rlleeerrlqGQLEQgddtaaekleKVYEelratgaaaaeakarrilaglgFDPEMQNRPTQKFSGGWRMRVSLARALFM 460
Cdd:cd03247 78 ----------SVLNQ----------RPYL----------------------FDTTLRNNLGRRFSGGERQRLALARILLQ 115
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 39930335 461 EPTLLMLDEPTNHLD-LNAVIWLNNYLQGWR-KTLLIVSH 498
Cdd:cd03247 116 DAPIVLLDEPTVGLDpITERQLLSLIFEVLKdKTLIWITH 155
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
318-499 |
8.48e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 318 IVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQeVVADETPAVQAVLRAdtkrlrlleeeRRLQGQ----- 392
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAG---LLPGSGSIQFAGQ-PLEAWSAAELARHRA-----------YLSQQQtppfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 --------LEQGDDTAAEKLEKVYEELRATgaaaaeakarrilagLGFDPEMqNRPTQKFSGGWRMRVSLA-------RA 457
Cdd:PRK03695 84 mpvfqyltLHQPDKTRTEAVASALNEVAEA---------------LGLDDKL-GRSVNQLSGGEWQRVRLAavvlqvwPD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 39930335 458 LFMEPTLLMLDEPTNHLDLNAVIWLNNYL-----QGwrKTLLIVSHD 499
Cdd:PRK03695 148 INPAGQLLLLDEPMNSLDVAQQAALDRLLselcqQG--IAVVMSSHD 192
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
617-790 |
8.48e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.14 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLllltgkltptngemrknhRLKIGfFNQQYAEQLHME 696
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL------------------RLLAG-LETPSAGELLAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 697 ETPTEYLQRSFNLPYQDAR------------------------KCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACRE 752
Cdd:PRK11247 73 TAPLAEAREDTRLMFQDARllpwkkvidnvglglkgqwrdaalQALAAVGLADRANEWP-AALSGGQKQRVALARALIHR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 39930335 753 PDVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSHD 790
Cdd:PRK11247 152 PGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
648-794 |
8.68e-06 |
|
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: 49.40 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 648 IVGPNGVGKSTLLLLLTGKLTPTNGEMRKNhrLKIGfFNQQYAEQlHMEETPTEYLQRSFNLPYQDAR---KCLGRFGLE 724
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDED--LKIS-YKPQYISP-DYDGTVEEFLRSANTDDFGSSYyktEIIKPLGLE 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 725 sHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY----KGAVIVVSHDARLI 794
Cdd:COG1245 447 -KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLI 519
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
426-499 |
9.49e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.31 E-value: 9.49e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 426 ILAGLGFDPeMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVI----WLNNYLQGWRKTLLIVSHD 499
Cdd:PRK13636 125 ALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLTIIIATHD 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
313-500 |
9.78e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 48.68 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVvaDETPAVQAVLRADTKRLRLLEEERRLQG- 391
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLA--GFEQPTAGQIMLDGVDL--SHVPPYQRPINMMFQSYALFPHMTVEQNi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 392 --QLEQGDDTAAEKLEKVYEELratgaaaaeakarrilaGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDE 469
Cdd:PRK11607 113 afGLKQDKLPKAEIASRVNEML-----------------GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 39930335 470 PTNHLD--LNAVIWLN--NYLQGWRKTLLIVSHDQ 500
Cdd:PRK11607 176 PMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
278-478 |
1.01e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.04 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 278 VSQAEVSSRQAMLENASDIKLEKFSI-SAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIA------NRALSIPP 350
Cdd:COG4178 345 ADALPEAASRIETSEDGALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygSGRIARPA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 351 NIDVLLCEQEvvadetPAV------QAVLRADTkrlrlleeerrlqgQLEQGDDTAAEKLEKVYeelratgaaaaeakar 424
Cdd:COG4178 425 GARVLFLPQR------PYLplgtlrEALLYPAT--------------AEAFSDAELREALEAVG---------------- 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 39930335 425 riLAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA 478
Cdd:COG4178 469 --LGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
734-790 |
1.09e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.19 E-value: 1.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSHD 790
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
626-792 |
1.12e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 626 YEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHrlKIGFFNQQYAE-----------QLH 694
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQidaiklrkevgMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 695 MEETPTEYLQRSFNLPY-------QDARK-------CLGRFGLESHAH---TIQICKLSGGQKARVVFAELACREPDVLI 757
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYplkshgiKEKREikkiveeCLRKVGLWKEVYdrlNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 39930335 758 LDEPTNNLDIESIDALGEAINDYKG--AVIVVSHDAR 792
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQ 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
289-513 |
1.12e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.06 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 289 MLENASDIKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLLCEQEVvadETPA 368
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSR--LMTPAHGHVWLDGEHI---QHYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 369 VQAVLRadtkrlrllEEERRLQGQLEQGDDTAAEKLEK---VYEELRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFS 445
Cdd:PRK10253 76 SKEVAR---------RIGLLAQNATTPGDITVQELVARgryPHQPLFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 446 GGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYL------QGWrkTLLIVSHDqgfLDDVCTDIIHL 513
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnreKGY--TLAAVLHD---LNQACRYASHL 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
691-836 |
1.14e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.08 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 691 EQLHMEETPTEYLQRSfnlPYQdarkclgrfgleshahtiqickLSGGQKARVVFAELACREPDVLILDEPTNNLDI--- 767
Cdd:PRK13645 132 ELLKLVQLPEDYVKRS---PFE----------------------LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkge 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 768 ESIDALGEAIN-DYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDYKREvlEALGEVMVNRPR 836
Cdd:PRK13645 187 EDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQ--ELLTKIEIDPPK 254
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
735-789 |
1.31e-05 |
|
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: 47.19 E-value: 1.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAE-LACrEPDVLILDEPTNNLDIE---SIDALGEAINDYKG-AVIVVSH 789
Cdd:cd03258 141 LSGGQKQRVGIARaLAN-NPKVLLCDEATSALDPEttqSILALLRDINRELGlTIVLITH 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
714-766 |
1.38e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 48.17 E-value: 1.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 39930335 714 ARKCLGRFGLESHAHTiQICKLSGGQKARVVFAE-LACrEPDVLILDEPTNNLD 766
Cdd:COG3842 116 VAELLELVGLEGLADR-YPHQLSGGQQQRVALARaLAP-EPRVLLLDEPLSALD 167
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
299-507 |
1.43e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.20 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 299 EKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQE---VVADETPAVQAV--L 373
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG---IVPRDAGNIIIDDEdisLLPLHARARRGIgyL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 374 RADTKRLRLLEEERRLQGQLEQGDDTAAEKLEKVYEELRATGAAAaeakarrilaglgfdpEMQNRPTQKFSGGWRMRVS 453
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE----------------HLRDSMGQSLSGGERRRVE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 454 LARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKT---LLIVSHDQGFLDDVC 507
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSglgVLITDHNVRETLAVC 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
427-499 |
1.46e-05 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 47.08 E-value: 1.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 427 LAGLGfdpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL----NAVIWLNNYLQGWRKTLLIVSHD 499
Cdd:TIGR01184 101 LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQEELMQIWEEHRVTVLMVTHD 174
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
616-790 |
1.46e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.54 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM----------RK---NHRLKI 682
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 683 GFFNQQYAEQLHmeeTPTEYLQRSF-----NLPYQDARK----CLGRFGLESHAHTIQICkLSGGQKARVVFAELACREP 753
Cdd:PRK13636 85 GMVFQDPDNQLF---SASVYQDVSFgavnlKLPEDEVRKrvdnALKRTGIEHLKDKPTHC-LSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 39930335 754 DVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSHD 790
Cdd:PRK13636 161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
619-766 |
1.62e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.10 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM-----RKNH----RLKIGFFNQQY 689
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekRMNDvppaERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 AEQLHMeetpTEYLQRSFNLPYQDARKCLGRFGLESHAHTIQICKL--------SGGQKARVVFAELACREPDVLILDEP 761
Cdd:PRK11000 85 ALYPHL----SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLldrkpkalSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
....*
gi 39930335 762 TNNLD 766
Cdd:PRK11000 161 LSNLD 165
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
438-514 |
1.68e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.77 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA--VIW--LNNYLQGWRKTLLIVSHDqgfLDDV---CTDI 510
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeAIRefLKEYNRERGTTILLTSHD---MDDIealCDRV 225
|
....
gi 39930335 511 IHLD 514
Cdd:COG4586 226 IVID 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
718-796 |
1.79e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 718 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEaINDYKGAVIVVSHDARL 793
Cdd:PRK15056 127 LARVDMVEFRHR-QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTeariISLLRE-LRDEGKTMLVSTHNLGS 204
|
...
gi 39930335 794 ITE 796
Cdd:PRK15056 205 VTE 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
712-790 |
1.90e-05 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 47.83 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 712 QDARKCLGRFGLESHAHTI--QickLSGGQKARVVFAE-LAcREPDVLILDEPTNNLDIESIDA----LGEAINDYKGAV 784
Cdd:COG1118 112 ARVEELLELVQLEGLADRYpsQ---LSGGQRQRVALARaLA-VEPEVLLLDEPFGALDAKVRKElrrwLRRLHDELGGTT 187
|
....*.
gi 39930335 785 IVVSHD 790
Cdd:COG1118 188 VFVTHD 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
445-539 |
2.06e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 47.92 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDL---NAVIW-LNNYLQGwrKTLLIVSHDQGFLDDVctDIIHLDTQRLHY 520
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAhseQLVMQaLNAASRR--QTTLMVTHQLEDLAQW--DQIWVMQDGQIV 562
|
90 100
....*....|....*....|....*.
gi 39930335 521 YRGNYMT-------FKKMYQQKQKEL 539
Cdd:PRK11174 563 QQGDYAElsqagglFATLLAHRQEEI 588
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
296-523 |
2.20e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.93 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsippnidvllceqeVVADETPAVQAVLRA 375
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL----------------ITGDKSAGSHIELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 DTkrlrlleeeRRLQGQLEQGDDTAAEKLEKVYEELraTGAAAAEAKARRILAGLG-----------FDPEMQNRPTQ-- 442
Cdd:PRK09984 69 RT---------VQREGRLARDIRKSRANTGYIFQQF--NLVNRLSVLENVLIGALGstpfwrtcfswFTREQKQRALQal 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 443 --------------KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------------------LNAVIWLNNYLQGW 489
Cdd:PRK09984 138 trvgmvhfahqrvsTLSGGQQQRVAIARALMQQAKVILADEPIASLDpesarivmdtlrdinqndgITVVVTLHQVDYAL 217
|
250 260 270
....*....|....*....|....*....|....*..
gi 39930335 490 RKTLLIVSHDQG--FLDDVCTdiiHLDTQRL-HYYRG 523
Cdd:PRK09984 218 RYCERIVALRQGhvFYDGSSQ---QFDNERFdHLYRS 251
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
646-766 |
2.28e-05 |
|
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: 46.50 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 646 ICIVGPNGVGKS---------TLLLLLTGKLTPTNGEMRKNHRLK--IGFFNQQ--YAEQLHMEET-------PTEYLQR 705
Cdd:cd03234 36 MAILGSSGSGKTtlldaisgrVEGGGTTSGQILFNGQPRKPDQFQkcVAYVRQDdiLLPGLTVRETltytailRLPRKSS 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 706 SFNLPYQDARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:cd03234 116 DAIRKKRVEDVLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
646-795 |
2.36e-05 |
|
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: 46.63 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 646 ICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNhRLKIGFFNQQY-------AEQLHMEETPTEYLQRSFNlpyQDARKCL 718
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIkadyegtVRDLLSSITKDFYTHPYFK---TEIAKPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 719 GRFGLESHahtiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY----KGAVIVVSHDARLI 794
Cdd:cd03237 104 QIEQILDR----EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMI 179
|
.
gi 39930335 795 T 795
Cdd:cd03237 180 D 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
735-766 |
2.51e-05 |
|
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: 47.76 E-value: 2.51e-05
10 20 30
....*....|....*....|....*....|...
gi 39930335 735 LSGGQKARVVFA-ELACrEPDVLILDEPTNNLD 766
Cdd:COG4172 157 LSGGQRQRVMIAmALAN-EPDLLIADEPTTALD 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
321-512 |
2.65e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.59 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 321 GRRYGLVGPNGKGKTTLLKHIANRalsIPPNidvlLCEQevvaDETPAVQAVLRADTKRLRLLEEERRLQGQLE------ 394
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGK---LKPN----LGKF----DDPPDWDEILDEFRGSELQNYFTKLLEGDVKvivkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 395 -------QGDDTAAEKLEKVYEelratgaaaaEAKARRILAGLGFDPEMqNRPTQKFSGGWRMRVSLARALFMEPTLLML 467
Cdd:cd03236 95 yvdlipkAVKGKVGELLKKKDE----------RGKLDELVDQLELRHVL-DRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 39930335 468 DEPTNHLD----LNAVIWLNNYLQGwRKTLLIVSHDQGFLdDVCTDIIH 512
Cdd:cd03236 164 DEPSSYLDikqrLNAARLIRELAED-DNYVLVVEHDLAVL-DYLSDYIH 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
714-766 |
2.66e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.78 E-value: 2.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 39930335 714 ARKCLGRFGLEsHAHTIQICKLSGGQKARVVFAE-LACrEPDVLILDEPTNNLD 766
Cdd:COG4525 115 AEELLALVGLA-DFARRRIWQLSGGMRQRVGIARaLAA-DPRFLLMDEPFGALD 166
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
735-789 |
2.69e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG----AVIVVSH 789
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1417
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
634-781 |
2.74e-05 |
|
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: 46.21 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 634 KNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR----------KNHRLKIGFFNQQYAeqLHMEETPTEYL 703
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRRRIGIVFQDLS--VDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 704 Q---RSFNLPYQDARK----CLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEA 776
Cdd:cd03265 95 YihaRLYGVPGAERRErideLLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
....*
gi 39930335 777 INDYK 781
Cdd:cd03265 174 IEKLK 178
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
714-768 |
2.77e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 46.72 E-value: 2.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 714 ARKCLGRFGLES--HAHTIQickLSGGQKARVVFAELACREPDVLILDEPTNNLDIE 768
Cdd:COG4598 135 AEALLAKVGLADkrDAYPAH---LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE 188
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
619-808 |
2.90e-05 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 46.33 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGYEGQKPL-FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM-----------RKNHRLKIGF-- 684
Cdd:cd03252 3 FEHVRFRYKPDGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGVvl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 685 -----FNQQYAEQLHMEET--PTEYLQRSFNLPYQDARKCLGRFGLEshahTI---QICKLSGGQKARVVFAELACREPD 754
Cdd:cd03252 83 qenvlFNRSIRDNIALADPgmSMERVIEAAKLAGAHDFISELPEGYD----TIvgeQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 755 VLILDEPTNNLDIESIDALGEAINDY-KG-AVIVVSHdaRLITETNCQLWVVEEQG 808
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIcAGrTVIIIAH--RLSTVKNADRIIVMEKG 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
297-512 |
3.18e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.21 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 297 KLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRALSIPPNIDVLLCEQEVVADET---------- 366
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDILELSPderaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 367 -----PAVQAV-----LRADTkrlrlleeerrlqGQLEQGDDTAAEKLEKVYEELRAtgaaaaeakarrilagLGFDPEM 436
Cdd:COG0396 82 afqypVEIPGVsvsnfLRTAL-------------NARRGEELSAREFLKLLKEKMKE----------------LGLDEDF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 437 QNRP-TQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD---LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVCTDIIH 512
Cdd:COG0396 133 LDRYvNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidaLRIVAEGVNKLRSPDRGILIITHYQRILDYIKPDFVH 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-499 |
3.60e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.19 E-value: 3.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK--TLLIVSHD 499
Cdd:PRK14246 148 NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
437-499 |
3.76e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.22 E-value: 3.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 437 QNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHD 499
Cdd:PRK13639 131 ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
431-498 |
3.77e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.41 E-value: 3.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 431 GFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAviwlNNYLQGWRK----TLLIVSH 498
Cdd:TIGR00958 606 GYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSrasrTVLLIAH 672
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
313-518 |
4.04e-05 |
|
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: 45.65 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLkhianRALSippnidvLLceqevvadETPAVQAVLRADTKRLRLLEEERRLQ-- 390
Cdd:cd03258 23 DVSLSVPKGEIFGIIGRSGAGKSTLI-----RCIN-------GL--------ERPTSGSVLVDGTDLTLLSGKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 391 --GQLEQGDDTAAEKleKVYE------ELRATGAAAAEAKARRILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEP 462
Cdd:cd03258 83 riGMIFQHFNLLSSR--TVFEnvalplEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ-LSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 463 TLLMLDEPTNHLD-------LNAVIWLNNYLqgwRKTLLIVSHDQGFLDDVCTDIIHLDTQRL 518
Cdd:cd03258 160 KVLLCDEATSALDpettqsiLALLRDINREL---GLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
616-795 |
4.05e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.86 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYEGQKPLfKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMrknhrlkigFFN--------- 686
Cdd:PRK10247 7 LLQLQNVGYLAGDAKIL-NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL---------LFEgedistlkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 687 QQYAEQL-HMEETPT---EYLQRSFNLPYQDARKC---------LGRFGLESHAHTIQICKLSGGQKARVVFAELACREP 753
Cdd:PRK10247 77 EIYRQQVsYCAQTPTlfgDTVYDNLIFPWQIRNQQpdpaiflddLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 39930335 754 DVLILDEPTNNLDIESIDALGEAINDY----KGAVIVVSHDARLIT 795
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDKDEIN 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
426-499 |
4.09e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.93 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 426 ILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNnylQGWRKTLLIVSH 498
Cdd:PRK10584 130 LLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtgdkiADLLFSLN---REHGTTLILVTH 205
|
.
gi 39930335 499 D 499
Cdd:PRK10584 206 D 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
445-499 |
4.14e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.01 E-value: 4.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD---------LNAVIWlnnylQGWRKTLLIVSHD 499
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDaltreqmqeLLLDVW-----QRTGKGVFLITHS 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
296-499 |
4.31e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.85 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 296 IKLEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETPAVQAVLRA 375
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAG---FVPYQHGSITLDGKPVEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 376 DTKRLRLLEEERRLQG-QL-----EQGDDTAAEKLEKVYeelratgaaaaeakarriLAGLGfdpemqNRPTQKFSGGWR 449
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGlQLagvekMQRLEIAHQMLKKVG------------------LEGAE------KRYIWQLSGGQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 450 MRVSLARALFMEPTLLMLDEPTNHLD---------LNAVIWlnnylQGWRKTLLIVSHD 499
Cdd:PRK11248 135 QRVGIARALAANPQLLLLDEPFGALDaftreqmqtLLLKLW-----QETGKQVLLITHD 188
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
735-795 |
4.44e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.52 E-value: 4.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDI----ESIDALGEAINDYKGAVIVVSH---DARLIT 795
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqEMLDLVDELCRERGLTVLMVTHdpeDAARIA 197
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
714-790 |
4.77e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 45.90 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 714 ARKCLGRFGLESHAHTIQIcKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIdalGEAIN------DYKGAVIVV 787
Cdd:PRK11264 125 ARELLAKVGLAGKETSYPR-RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV---GEVLNtirqlaQEKRTMVIV 200
|
...
gi 39930335 788 SHD 790
Cdd:PRK11264 201 THE 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
443-475 |
4.78e-05 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 45.68 E-value: 4.78e-05
10 20 30
....*....|....*....|....*....|...
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:cd03251 138 KLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
627-766 |
4.81e-05 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 45.23 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 627 EGQKPLFKNLDFGIDMDSRICIVGPNGVGKS--------TLLLLLTGKLTPTNGEMRKNHRLK--IGFFNQQyaEQLHME 696
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKStllnalagRRTGLGVSGEVLINGRPLDKRSFRkiIGYVPQD--DILHPT 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 697 ETPTEYLQRSFNLpyqdaRkclgrfgleshahtiqicKLSGGQKARVVFA-ELACRePDVLILDEPTNNLD 766
Cdd:cd03213 97 LTVRETLMFAAKL-----R------------------GLSGGERKRVSIAlELVSN-PSLLFLDEPTSGLD 143
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
735-790 |
5.00e-05 |
|
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: 45.40 E-value: 5.00e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINDYKGAVIVVSHD 790
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
444-475 |
5.14e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 46.20 E-value: 5.14e-05
10 20 30
....*....|....*....|....*....|..
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
736-816 |
5.23e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 736 SGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAIN---DYKGAVIVVSHDARLITETNCQLWVVEEQGVSQI 812
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNslrDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
....
gi 39930335 813 DGDF 816
Cdd:PRK09580 227 SGDF 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
631-813 |
5.42e-05 |
|
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: 45.10 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 631 PLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGemrknhRLKIgffnqqyaEQLHMEETPTEYLQRSFNLP 710
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG------KIEI--------DGIDISTIPLEDLRSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 711 YQDA-------RKCLGRFGLESHAHTIQICK-------LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEA 776
Cdd:cd03369 88 PQDPtlfsgtiRSNLDPFDEYSDEEIYGALRvsegglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 39930335 777 IND-YKGA-VIVVSHdaRLITETNCQLWVVEEQG-VSQID 813
Cdd:cd03369 168 IREeFTNStILTIAH--RLRTIIDYDKILVMDAGeVKEYD 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
712-766 |
5.91e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.78 E-value: 5.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 712 QDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:PRK13634 123 QKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
713-790 |
5.94e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 713 DARKclgRFGLESHahtiqicKLSGGQKARVVFA-ELACRePDVLILDEPTNNLDIeSIDA-----LGEAINDYKGAVIV 786
Cdd:PRK09473 150 EARK---RMKMYPH-------EFSGGMRQRVMIAmALLCR-PKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIM 217
|
....
gi 39930335 787 VSHD 790
Cdd:PRK09473 218 ITHD 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
426-499 |
6.35e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.64 E-value: 6.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 426 ILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA---VIWLNNYLQGWRKTLLIVSHD 499
Cdd:PRK10535 128 LLQRLGLEDRVEYQPSQ-LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
628-768 |
7.53e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.35 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNH------RLKIGFFNQQYAEQLHMEETPTE 701
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvRDKDGQLKVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 702 YLQRSFNL-------------PYQ-------DAR----KCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLI 757
Cdd:PRK10619 96 MVFQHFNLwshmtvlenvmeaPIQvlglskqEAReravKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170
....*....|.
gi 39930335 758 LDEPTNNLDIE 768
Cdd:PRK10619 176 FDEPTSALDPE 186
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
435-500 |
7.61e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.71 E-value: 7.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLI----VSHDQ 500
Cdd:PRK09452 136 EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGItfvfVTHDQ 205
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
443-513 |
8.29e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 8.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQGFLDDVcTDIIHL 513
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYL-SDRIHV 144
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
430-500 |
8.44e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 45.83 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 430 LGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-----------------LNAviwlnnylqgwrkT 492
Cdd:COG3839 121 LGLEDLLDRKPKQ-LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrvemraeikrlhrrLGT-------------T 186
|
....*...
gi 39930335 493 LLIVSHDQ 500
Cdd:COG3839 187 TIYVTHDQ 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
734-836 |
9.37e-05 |
|
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: 45.18 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDI---ESIDALGEAINDYKG-AVIVVSHDARLItETNCQLWVVEEQG- 808
Cdd:TIGR02769 150 QLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQAFGtAYLFITHDLRLV-QSFCQRVAVMDKGq 228
|
90 100 110
....*....|....*....|....*....|.
gi 39930335 809 -VSQID-GDFDDYKREVLEALGE-VMVNRPR 836
Cdd:TIGR02769 229 iVEECDvAQLLSFKHPAGRNLQSaVLPEHPV 259
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
736-818 |
9.37e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 736 SGGQKARVVFAELACREPDVLILDEptnnldiesidALG-----------EAINDYK---GAVIVVSHDARLItETNCQ- 800
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDE-----------VLAvgdaafqkkclARIRELResgRTVIFVSHSMGAV-RRLCDr 215
|
90
....*....|....*....
gi 39930335 801 -LWVveEQGVSQIDGDFDD 818
Cdd:COG1134 216 aIWL--EKGRLVMDGDPEE 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
319-475 |
9.78e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.18 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 319 VAGR--RYGLVGPNGKGKTTLLKHIaNRALSiPPNIDVLLCEQEVVADETPAVQAVL-----RADTKRLRLLEEERRLQG 391
Cdd:PRK13652 26 IAPRnsRIAVIGPNGAGKSTLFRHF-NGILK-PTSGSVLIRGEPITKENIREVRKFVglvfqNPDDQIFSPTVEQDIAFG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 392 QLEQGDDTAAEKlEKVYEELRAtgaaaaeakarrilagLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPT 471
Cdd:PRK13652 104 PINLGLDEETVA-HRVSSALHM----------------LGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
....
gi 39930335 472 NHLD 475
Cdd:PRK13652 166 AGLD 169
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
734-789 |
1.01e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.90 E-value: 1.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSH 789
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
627-794 |
1.04e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.90 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 627 EGQKpLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQ-------YAEQLHMEETP 699
Cdd:TIGR00954 463 NGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtLRDQIIYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 700 TEYLQRSFNlpYQDARKCLGRFGLEshaHTIQ-------ICK----LSGGQKARVVFAELACREPDVLILDEPTNNLDIE 768
Cdd:TIGR00954 542 EDMKRRGLS--DKDLEQILDNVQLT---HILEreggwsaVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180
....*....|....*....|....*.
gi 39930335 769 SIDALGEAINDYKGAVIVVSHDARLI 794
Cdd:TIGR00954 617 VEGYMYRLCREFGITLFSVSHRKSLW 642
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
735-789 |
1.14e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLD------IESIdaLGEAINDYkgAVIVVSH 789
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgtakIEEL--LFELKKEY--TIVLVTH 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
444-499 |
1.19e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 44.64 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWR----KTLLIVSHD 499
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
442-478 |
1.20e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....*..
gi 39930335 442 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA 478
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
445-470 |
1.27e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.25 E-value: 1.27e-04
10 20
....*....|....*....|....*.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEP 470
Cdd:COG1137 138 SGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
646-794 |
1.28e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 646 ICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNhrLKIGfFNQQY--AEQlhmEETPTEYLQR---SFNLPYQDArKCLGR 720
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--LKIS-YKPQYikPDY---DGTVEDLLRSitdDLGSSYYKS-EIIKP 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 721 FGLEsHAHTIQICKLSGGQKARVVFAelAC--REPDVLILDEPTNNLDIESIDALGEAINDY----KGAVIVVSHDARLI 794
Cdd:PRK13409 441 LQLE-RLLDKNVKDLSGGELQRVAIA--AClsRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHDIYMI 517
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
734-789 |
1.34e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 44.64 E-value: 1.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 734 KLSGGQKARVVFAelacR----EPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSH 789
Cdd:COG1117 154 GLSGGQQQRLCIA----RalavEPEVLLMDEPTSALDPISTAKIEELILELKKdyTIVIVTH 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
321-513 |
1.35e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 321 GRRYGLVGPNGKGKTTLLKhianrALS--IPPNidvlLCEQEvvadETPAVQAVLRADTKRLRLLEEERRLQGQL----- 393
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVK-----ILSgeLIPN----LGDYE----EEPSWDEVLKRFRGTELQNYFKKLYNGEIkvvhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 394 --------EQGDDTAAEKLEKVYEElratgaaaaeAKARRILAGLGFDPEMqNRPTQKFSGGWRMRVSLARALFMEPTLL 465
Cdd:PRK13409 166 pqyvdlipKVFKGKVRELLKKVDER----------GKLDEVVERLGLENIL-DRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 39930335 466 MLDEPTNHLD----LNAVIWLNNYLQGwrKTLLIVSHDQGFLDDVcTDIIHL 513
Cdd:PRK13409 235 FFDEPTSYLDirqrLNVARLIRELAEG--KYVLVVEHDLAVLDYL-ADNVHI 283
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
636-827 |
1.40e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.62 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 636 LDFGIDMDSRICIVGPNGVGKSTLLL--------------------LLTGKLTPTNGEMRKNhRLKIGFFNQQY--AEQL 693
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRhlsglitgdksagshiellgRTVQREGRLARDIRKS-RANTGYIFQQFnlVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 694 HMEET-------PTEYLQRSFN----LPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPT 762
Cdd:PRK09984 102 SVLENvligalgSTPFWRTCFSwftrEQKQRALQALTRVGMVHFAHQ-RVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 763 NNLDIES----IDALGEaINDYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDYKREVLEAL 827
Cdd:PRK09984 181 ASLDPESarivMDTLRD-INQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHL 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
711-789 |
1.41e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 711 YQDARKCLGRFGLESHAHTIqICKLSGGQK-----ARVVFaelacREPDVLILDEPTNNLDIESIDALGEAINDYKG--- 782
Cdd:COG1129 118 RRRARELLARLGLDIDPDTP-VGDLSVAQQqlveiARALS-----RDARVLILDEPTASLTEREVERLFRIIRRLKAqgv 191
|
....*..
gi 39930335 783 AVIVVSH 789
Cdd:COG1129 192 AIIYISH 198
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
431-498 |
1.42e-04 |
|
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: 44.07 E-value: 1.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 431 GFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN--AVIW--LNNYLQGwrKTLLIVSH 498
Cdd:cd03249 128 GYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSALDAEseKLVQeaLDRAMKG--RTTIVIAH 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
628-789 |
1.49e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 43.64 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGI---DMdsrICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRlKIGFFNQQYAEQL----HM----- 695
Cdd:PRK13538 12 DERILFSGLSFTLnagEL---VQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-PIRRQRDEYHQDLlylgHQpgikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 696 EETPTEYLQrsFNLP---YQDARKC---LGRFGL----ESHAHTiqickLSGGQKARVVFAELACREPDVLILDEPTNNL 765
Cdd:PRK13538 88 ELTALENLR--FYQRlhgPGDDEALweaLAQVGLagfeDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 39930335 766 DIESIDALGEAINDY---KGAVIVVSH 789
Cdd:PRK13538 161 DKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
435-471 |
1.51e-04 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 44.20 E-value: 1.51e-04
10 20 30
....*....|....*....|....*....|....*..
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPT 471
Cdd:COG0410 128 ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
736-825 |
1.53e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 736 SGGQKARVVFAELACREPDVLILDEPTNNLD---IESIDALGEAI-NDYKGAVIVVSHDARLITETNCQLWV-----VEE 806
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVlrqgeVVE 506
|
90 100
....*....|....*....|.
gi 39930335 807 QGVSQ--IDGDFDDYKREVLE 825
Cdd:PRK15134 507 QGDCErvFAAPQQEYTRQLLA 527
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
718-766 |
1.58e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.42 E-value: 1.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 39930335 718 LGRFGLESHAHTI-----QICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:TIGR00955 145 LQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
679-790 |
1.60e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.39 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 679 RLKIGFFNQQYAEQLHME--ETPTEYLQRSFNLPYQ----DARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACRE 752
Cdd:PRK13646 84 RKRIGMVFQFPESQLFEDtvEREIIFGPKNFKMNLDevknYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 39930335 753 PDVLILDEPTNNLDIESIDALGEAINDYK----GAVIVVSHD 790
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
619-790 |
1.65e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 44.21 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 619 LHGVTFGY-EGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR-----------KNHRLKIGFF- 685
Cdd:PRK13632 10 VENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenlKEIRKKIGIIf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 ----NQ-----------------------------QYAEQLHMEetptEYLQRsfnlpyqdarkclgrfglESHahtiqi 732
Cdd:PRK13632 90 qnpdNQfigatveddiafglenkkvppkkmkdiidDLAKKVGME----DYLDK------------------EPQ------ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930335 733 cKLSGGQKARVVFAELACREPDVLILDEPTNNLD------IESIdaLGEAINDYKGAVIVVSHD 790
Cdd:PRK13632 142 -NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreIKKI--MVDLRKTRKKTLISITHD 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
622-790 |
1.69e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.21 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYeGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM-----------RKNHRLKIGFFNQQYA 690
Cdd:PRK10253 13 LTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 691 --------EQLHMEETPTEYLQRSFNLPYQDARKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPT 762
Cdd:PRK10253 92 tpgditvqELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190
....*....|....*....|....*....|..
gi 39930335 763 NNLDI-ESIDALG--EAINDYKGAVI-VVSHD 790
Cdd:PRK10253 172 TWLDIsHQIDLLEllSELNREKGYTLaAVLHD 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
735-766 |
1.77e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 44.35 E-value: 1.77e-04
10 20 30
....*....|....*....|....*....|..
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
734-809 |
1.78e-04 |
|
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: 45.09 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINDYKGavIVVSHdaRLITETNCQLWVVEEQGV 809
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGRTT--LVIAH--RLSTIEKADRIVVMDDGR 544
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
734-796 |
1.83e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 1.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 734 KLSGGQKARVVFA-ELACRePDVLILDEPTNNLDI----ESIDALGEAINDYKGAVIVVSHDARLITE 796
Cdd:PRK11022 153 QLSGGMSQRVMIAmAIACR-PKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAE 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
312-342 |
1.88e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.92 E-value: 1.88e-04
10 20 30
....*....|....*....|....*....|.
gi 39930335 312 VNADLYivAGRRYGLVGPNGKGKTTLLKHIA 342
Cdd:COG1134 45 VSFEVE--RGESVGIIGRNGAGKSTLLKLIA 73
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
436-499 |
1.99e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.15 E-value: 1.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 436 MQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHD 499
Cdd:PRK11701 145 IDDLPTT-FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglavVIVTHD 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
427-506 |
2.00e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 44.27 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 427 LAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNnylQGWRKTLLIVSHD 499
Cdd:PRK13637 129 IVGLDYE-DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELH---KEYNMTIILVSHS 204
|
....*..
gi 39930335 500 qgfLDDV 506
Cdd:PRK13637 205 ---MEDV 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
616-766 |
2.10e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.41 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGyEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRknHRLKIGFFNQQYA--EQL 693
Cdd:COG2401 30 VLEAFGVELR-VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC--VDVPDNQFGREASliDAI 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 694 HMEETPTEYLQRSFNLPYQDARKCLGRFGleshahtiqicKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:COG2401 107 GRKGDFKDAVELLNAVGLSDAVLWLRRFK-----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
427-500 |
2.20e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 2.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 427 LAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-LNAVI---WLNNYLQGWRKTLLIVSHDQ 500
Cdd:PRK10938 385 LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDpLNRQLvrrFVDVLISEGETQLLFVSHHA 462
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
426-505 |
2.27e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.42 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 426 ILAGLGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD--LNAVI--WLNNYLQGWRKTLLIVSHDqg 501
Cdd:PRK10771 113 IARQMGIEDLLARLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQEMltLVSQVCQERQLTLLMVSHS-- 189
|
....
gi 39930335 502 fLDD 505
Cdd:PRK10771 190 -LED 192
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
628-766 |
2.33e-04 |
|
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: 43.38 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKN---------HRLKIGFFNQQYAEQLHMEET 698
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlppHKRPVNTVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 699 -----PTEYLQRSFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:cd03300 91 eniafGLRLKKLPKAEIKERVAEALDLVQLEGYANR-KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
735-790 |
2.33e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.63 E-value: 2.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 735 LSGG--QKarVVFA-ELAcREPDVLILDEPTNNLDIESIDALGEAINDY--KG-AVIVVSHD 790
Cdd:COG3845 403 LSGGnqQK--VILArELS-RDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGaAVLLISED 461
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
445-482 |
2.39e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 2.39e-04
10 20 30
....*....|....*....|....*....|....*...
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWL 482
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
313-521 |
2.40e-04 |
|
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: 43.29 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIA------------NRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRl 380
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAgiyppdsgtvtvRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKE- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 381 rlleeerrlqgqleqgddtAAEKLEKVYEelratgaaaaeakarriLAGLGfdpEMQNRPTQKFSGGWRMRVSLARALFM 460
Cdd:cd03220 119 -------------------IDEKIDEIIE-----------------FSELG---DFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 461 EPTLLMLDEPTNHLDLN----AVIWLNNYLQGwRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHYY 521
Cdd:cd03220 160 EPDILLIDEVLAVGDAAfqekCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
438-500 |
2.42e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.25 E-value: 2.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD----LNAVIWLNNYLQGWRKTLLIVSHDQ 500
Cdd:PRK11000 128 DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
318-513 |
2.47e-04 |
|
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: 43.04 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 318 IVAGRRYGLVGPNGKGKTTLLKHIANralSIPPNIDVLLCEQEVVADETpavqavlradtkrlrlleeeRRLQGQL--EQ 395
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILG---IILPDSGEVLFDGKPLDIAA--------------------RNRIGYLpeER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 396 G---DDTAAEKLekVY-EELRATGAAAAEAKARRILAGLGFDpEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPT 471
Cdd:cd03269 80 GlypKMKVIDQL--VYlAQLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 39930335 472 NHLD-LNAVIWLN--NYLQGWRKTLLIVSHDQGFLDDVCTDIIHL 513
Cdd:cd03269 157 SGLDpVNVELLKDviRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
427-475 |
2.48e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.96 E-value: 2.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 39930335 427 LAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:PRK13649 129 LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
431-475 |
2.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.86 E-value: 2.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 39930335 431 GFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:PRK13634 133 GLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
731-807 |
2.68e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 731 QICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY----KGAVIVVSHDARLITETNCQLWVVEE 806
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
.
gi 39930335 807 Q 807
Cdd:cd03222 148 E 148
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
616-790 |
2.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.54 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVTFGYEGQKPL--FKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNG-----------EMRKNHRLKI 682
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgelltaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 683 GFFNQQYAEQL--HMEETPTEYLQRSFNLPYQDARKCLGRFGLESHA---HTIQICKLSGGQKARVVFAELACREPDVLI 757
Cdd:PRK13642 84 GMVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMldfKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 39930335 758 LDEPTNNLD----IESIDALGEAINDYKGAVIVVSHD 790
Cdd:PRK13642 164 LDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
445-498 |
2.89e-04 |
|
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: 42.03 E-value: 2.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYL-----QGwrKTLLIVSH 498
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrlraQG--VAVIFISH 140
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
445-498 |
2.95e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.43 E-value: 2.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAviwLNNYLQGwrKTLLIVSH 498
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDaeterqiLEL---LAEHAQN--KTVLMITH 532
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
310-482 |
3.03e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.87 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 310 LFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEVVADET------------PAVQAVLRADt 377
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILA--GLARPDAGEVLWQGEPIRRQRDeyhqdllylghqPGIKTELTAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 378 krlrlLEEERRLQGQLEQGDDTAAEKLEKV----YEELratgaaaaeakarrilaglgfdpemqnrPTQKFSGGWRMRVS 453
Cdd:PRK13538 93 -----ENLRFYQRLHGPGDDEALWEALAQVglagFEDV----------------------------PVRQLSAGQQRRVA 139
|
170 180
....*....|....*....|....*....
gi 39930335 454 LARALFMEPTLLMLDEPTNHLDLNAVIWL 482
Cdd:PRK13538 140 LARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
718-790 |
3.15e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.24 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 718 LGRFGLESHAHTIQ--------------ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI-ESID--ALGEAINDY 780
Cdd:PRK10575 117 LGRFGAADREKVEEaislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDvlALVHRLSQE 196
|
90
....*....|.
gi 39930335 781 KG-AVIVVSHD 790
Cdd:PRK10575 197 RGlTVIAVLHD 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
718-829 |
3.20e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 43.44 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 718 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NDYKGAVIVVSHDARL 793
Cdd:PRK11300 138 LERVGLLEHANR-QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKL 216
|
90 100 110
....*....|....*....|....*....|....*....
gi 39930335 794 ITETNCQLWVVeEQGVSQIDGDFDDYK--REVLEA-LGE 829
Cdd:PRK11300 217 VMGISDRIYVV-NQGTPLANGTPEEIRnnPDVIKAyLGE 254
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
430-498 |
3.20e-04 |
|
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: 44.35 E-value: 3.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 430 LGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-LNAVIWLNNYLQGWRKTLLIVSH 498
Cdd:TIGR01193 599 LGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
732-790 |
3.29e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 3.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 732 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY---KGAVIVVSHD 790
Cdd:COG1245 210 ISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaeeGKYVLVVEHD 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
732-790 |
3.31e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 732 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI-ESIDAlGEAINDY--KGAVIVVSHD 790
Cdd:PRK13409 210 ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrQRLNV-ARLIRELaeGKYVLVVEHD 270
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
735-790 |
3.32e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 43.64 E-value: 3.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIES----IDALGEAINDYKGAVIVVSHD 790
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
735-794 |
3.42e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.31 E-value: 3.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 735 LSGGQKARVVFA-ELACR-EPDVLILDEPTNNLDIESIDALGEAIN---DYKGAVIVVSHDARLI 794
Cdd:cd03238 88 LSGGELQRVKLAsELFSEpPGTLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVL 152
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
718-795 |
3.46e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.64 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 718 LGRFGLESHAHTIQiCKLSGGQKARVVFAE-LACRePDVLILDEPTNNLDIE---SIDALGEAINDYKGAVIVvshdarL 793
Cdd:PRK11153 125 LELVGLSDKADRYP-AQLSGGQKQRVAIARaLASN-PKVLLCDEATSALDPAttrSILELLKDINRELGLTIV------L 196
|
..
gi 39930335 794 IT 795
Cdd:PRK11153 197 IT 198
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
735-791 |
3.53e-04 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 42.85 E-value: 3.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARV--VFAELAcrEPDVLILDEPTNNLD-----------IESIDALGeaindykGAVIVVSHDA 791
Cdd:COG4136 134 LSGGQRARValLRALLA--EPRALLLDEPFSKLDaalraqfrefvFEQIRQRG-------IPALLVTHDE 194
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
622-767 |
3.58e-04 |
|
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: 44.35 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 622 VTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNH-----------RLKIGFFNQQ-- 688
Cdd:TIGR01193 479 VSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslkdidrhtlRQFINYLPQEpy 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 -----YAEQLHM---EETPTEYLQRSFNLPY--QDARKCLGRFG--LESHAHTIqicklSGGQKARVVFAELACREPDVL 756
Cdd:TIGR01193 559 ifsgsILENLLLgakENVSQDEIWAACEIAEikDDIENMPLGYQteLSEEGSSI-----SGGQKQRIALARALLTDSKVL 633
|
170
....*....|.
gi 39930335 757 ILDEPTNNLDI 767
Cdd:TIGR01193 634 ILDESTSNLDT 644
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
732-790 |
3.65e-04 |
|
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: 43.12 E-value: 3.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 732 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIE---SIDALGEAINDYKGAVIVVSHD 790
Cdd:cd03236 137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
325-470 |
3.73e-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: 42.92 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 325 GLVGPNGKGKTTLLKHIAnrALSIPPNIDVLLCEQEV---------------------------VADETPAVqavlradt 377
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIV--GLVKPDSGKILLDGQDItklpmhkrarlgigylpqeasifrkltVEENILAV-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 378 krlrlleeerrlqgqLEQGDDTAAEKLEKVyEELratgaaaaeakarriLAGLGFDPeMQNRPTQKFSGGWRMRVSLARA 457
Cdd:cd03218 100 ---------------LEIRGLSKKEREEKL-EEL---------------LEEFHITH-LRKSKASSLSGGERRRVEIARA 147
|
170
....*....|...
gi 39930335 458 LFMEPTLLMLDEP 470
Cdd:cd03218 148 LATNPKFLLLDEP 160
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
443-498 |
3.76e-04 |
|
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: 42.99 E-value: 3.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAviwLNNYLQGwrKTLLIVSH 498
Cdd:cd03253 137 KLSGGEKQRVAIARAILKNPPILLLDEATSALDthtereiQAA---LRDVSKG--RTTIVIAH 194
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
646-798 |
3.85e-04 |
|
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: 41.59 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 646 ICIVGPNGVGKSTLlllltgkltptngemrknhrlkigffnqqyAEQLHMEETPTEYLQRSFNLpyqDARKCLGRFGLES 725
Cdd:smart00382 5 ILIVGPPGSGKTTL------------------------------ARALARELGPPGGGVIYIDG---EDILEEVLDQLLL 51
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 726 HAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGAVIVVSHDARLITETN 798
Cdd:smart00382 52 IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTN 124
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
445-513 |
3.87e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.71 E-value: 3.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHDqgfLDdvctDIIHL 513
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREInipiLYVSHS---LD----EILRL 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
648-790 |
4.36e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 43.17 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 648 IVGPNGVGKStlllllt------gkltptNGE-MRKNHRLKIGFF--------NQQYAEQLhmeetptEYLQRSFNLPYQ 712
Cdd:COG4152 32 LLGPNGAGKTttiriilgilapdsgevlwDGEpLDPEDRRRIGYLpeerglypKMKVGEQL-------VYLARLKGLSKA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 713 DARK----CLGRFGLESHA-HTIQicKLSGGQKARVVF-AELACrEPDVLILDEPTNNLDIESIDALGEAINDYK--GA- 783
Cdd:COG4152 105 EAKRradeWLERLGLGDRAnKKVE--ELSKGNQQKVQLiAALLH-DPELLILDEPFSGLDPVNVELLKDVIRELAakGTt 181
|
....*..
gi 39930335 784 VIVVSHD 790
Cdd:COG4152 182 VIFSSHQ 188
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
722-790 |
4.47e-04 |
|
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: 42.45 E-value: 4.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 722 GLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NDYKGAVIVVSHD 790
Cdd:TIGR01184 103 GLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
712-822 |
4.49e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 712 QDARKCLGrfgLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES---IDALGEAINDYKGAVIVVS 788
Cdd:PRK09700 390 ENQRELLA---LKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAkaeIYKVMRQLADDGKVILMVS 466
|
90 100 110
....*....|....*....|....*....|....
gi 39930335 789 HDARLITETNCQLWVVEEQGVSQIDGDFDDYKRE 822
Cdd:PRK09700 467 SELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
444-534 |
4.58e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLN---NYLQGWRKTLLIVSHDQGFLDDVCTDIIHLDTQRLHY 520
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIV 225
|
90
....*....|....
gi 39930335 521 YRGNYMTFKKMYQQ 534
Cdd:PRK09580 226 KSGDFTLVKQLEEQ 239
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
732-793 |
4.72e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 43.29 E-value: 4.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 732 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI----ESIDALGEAINDYKGAVIVVsHDARL 793
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDInhqvRTLELVRRLVDDGKTAVAAI-HDLDL 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
321-505 |
4.79e-04 |
|
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: 41.20 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 321 GRRYGLVGPNGKGKTTLLKHIANraLSIPPNIDVLlceqeVVADETpavqavLRADTKRLRLLEEERRLQGQLEQGDdta 400
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR--ELGPPGGGVI-----YIDGED------ILEEVLDQLLLIIVGGKKASGSGEL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 401 aeklekvyeelratgaaaaeakarrilaglgfdpemqnrptqkfsggwRMRVSLARALFMEPTLLMLDEPTNHLD----- 475
Cdd:smart00382 66 ------------------------------------------------RLRLALALARKLKPDVLILDEITSLLDaeqea 97
|
170 180 190
....*....|....*....|....*....|....
gi 39930335 476 ----LNAVIWLNNYLQGWRKTLLIVSHDQGFLDD 505
Cdd:smart00382 98 llllLEELRLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
671-790 |
5.39e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 671 NGEMRKNHRLKIGFFNQQYAEQLHMEETP-TEYLQRSFNLPYQDARK----CLGRFGLESHAHTIQIcKLSGGQKARVVF 745
Cdd:PRK10070 97 DAELREVRRKKIAMVFQSFALMPHMTVLDnTAFGMELAGINAEERREkaldALRQVGLENYAHSYPD-ELSGGMRQRVGL 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 39930335 746 AELACREPDVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSHD 790
Cdd:PRK10070 176 ARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
444-503 |
5.58e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 42.32 E-value: 5.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNN-----YLQGWRKTLLIVSHDQGFL 503
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYL 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
445-498 |
5.77e-04 |
|
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: 42.47 E-value: 5.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA--VIWLNNYLQGWRKTLLIVSH 498
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESehAIMRNMHDICAGRTVIIIAH 195
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
735-818 |
6.03e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 43.29 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKGA--VIVVSHdaRLITETNC-QLWVVEE-QGVS 810
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTH--QLEDLAQWdQIWVMQDgQIVQ 563
|
....*...
gi 39930335 811 QidGDFDD 818
Cdd:PRK11174 564 Q--GDYAE 569
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
426-499 |
6.32e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 6.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 426 ILAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTL----LIVSHD 499
Cdd:PRK10261 446 LLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHD 523
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
718-790 |
6.72e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 42.41 E-value: 6.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 718 LGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHD 790
Cdd:COG4674 136 LETIGLTDKADR-LAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGkhSVVVVEHD 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
731-790 |
6.93e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 6.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 731 QICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG---AVIVVSHD 790
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSE 454
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
435-475 |
7.01e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 7.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 39930335 435 EMQNR----PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:PRK14267 138 EVKDRlndyPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
445-498 |
7.17e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.07 E-value: 7.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK--TLLIVSH 498
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
435-507 |
7.34e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.18 E-value: 7.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNA---VIWLNNYLQGWRKTLLIVSHDQGFLDDVC 507
Cdd:PRK15056 134 EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
712-766 |
7.62e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.99 E-value: 7.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 712 QDARKCLGRFGLEShAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:PRK11248 107 EIAHQMLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
734-767 |
7.69e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 7.69e-04
10 20 30
....*....|....*....|....*....|....
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDI 767
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
435-506 |
8.80e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.03 E-value: 8.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHDqgfLDDV 506
Cdd:PRK13650 132 DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyqmTVISITHD---LDEV 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
722-795 |
8.94e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.37 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 722 GLESHAHTI--QickLSGGQKARVVFAE-LACRePDVLILDEPTNNLDIE---SIDALGEAINDYKGAVIVvshdarLIT 795
Cdd:COG1135 129 GLSDKADAYpsQ---LSGGQKQRVGIARaLANN-PKVLLCDEATSALDPEttrSILDLLKDINRELGLTIV------LIT 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
435-499 |
9.06e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 9.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK----TLLIVSHD 499
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehnvTVLLIEHD 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
442-514 |
9.44e-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: 40.60 E-value: 9.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930335 442 QKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRKTLLIVSHDQGfLDDVCTDIIHLD 514
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPS-LWKFHDRVLDLD 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
735-789 |
9.82e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.68 E-value: 9.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAI----NDYkgAVIVVSH 789
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTR 205
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
736-794 |
1.03e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.55 E-value: 1.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 736 SGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG---AVIVVSHDARLI 794
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsenSIILITHYQRLL 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
445-475 |
1.06e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.99 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
443-475 |
1.12e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|...
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
735-789 |
1.21e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 41.61 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSH 789
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
617-766 |
1.23e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.49 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEGQKPLFknlDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMR---KNHR--------LKIGF- 684
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngQDHTttppsrrpVSMLFq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 685 ----FNQQYAEQ-----LHMEETPTEYlQRsfnlpyQDARKCLGRFGLESHAHTIQiCKLSGGQKARVVFAELACREPDV 755
Cdd:PRK10771 79 ennlFSHLTVAQniglgLNPGLKLNAA-QR------EKLHAIARQMGIEDLLARLP-GQLSGGQRQRVALARCLVREQPI 150
|
170
....*....|.
gi 39930335 756 LILDEPTNNLD 766
Cdd:PRK10771 151 LLLDEPFSALD 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
735-794 |
1.32e-03 |
|
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: 40.94 E-value: 1.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSH---DARLI 794
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHqpeDAKRL 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
734-821 |
1.34e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.62 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY--KGAVIVVSH----------------DARLIT 795
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHnlaqaarisdraalffDGRLVE 242
|
90 100 110
....*....|....*....|....*....|..
gi 39930335 796 ETNC-QLWVVEEQG-----VSQIDGDFDDYKR 821
Cdd:PRK14271 243 EGPTeQLFSSPKHAetaryVAGLSGDVKDAKR 274
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
444-476 |
1.34e-03 |
|
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: 42.59 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|...
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLDL 476
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
445-499 |
1.39e-03 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 41.48 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQgwrKTLLIVSHD 499
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALDplirremQDELLRLQAELQ---KTIVFITHD 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
435-475 |
1.44e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
313-506 |
1.48e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.30 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 313 NADLYIVAGRRYGLVGPNGKGKTTLLKHIanRALSIPPNIDVLLCEQEVVADETPAVQAVLRADTKRLRLLEEERRLQGQ 392
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNI--NALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 393 LEQ----GDDTAAEKLEKVYEElratgaaaaeakARRILAGLGFDPE-MQNRPTQkFSGGWRMRVSLARALFMEPTLLML 467
Cdd:PRK13646 103 VEReiifGPKNFKMNLDEVKNY------------AHRLLMDLGFSRDvMSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 39930335 468 DEPTNHLDLNA---VIWLNNYLQ-GWRKTLLIVSHDqgfLDDV 506
Cdd:PRK13646 170 DEPTAGLDPQSkrqVMRLLKSLQtDENKTIILVSHD---MNEV 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
735-814 |
1.53e-03 |
|
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: 40.98 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIE----SIDALGEAINDYKgAVIVVSHDARLITEtNCQLWVVEEQGVS 810
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQGK-TVILVSHDPSSIKR-LCDRALVLEKGKI 220
|
....
gi 39930335 811 QIDG 814
Cdd:cd03220 221 RFDG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
735-766 |
1.60e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 41.60 E-value: 1.60e-03
10 20 30
....*....|....*....|....*....|....*...
gi 39930335 735 LSGGQKARV------VfaelacREPDVLILDEPTNNLD 766
Cdd:COG3839 134 LSGGQRQRValgralV------REPKVFLLDEPLSNLD 165
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
298-476 |
1.69e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 41.31 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 298 LEKFSISAHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalSIPPNIDVLLCEQEVVADETPAV-------- 369
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH--QPPSEGEILLDAQPLESWSSKAFarkvaylp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 370 QAVLRAD--TKRLRLLEEERRLQGQLEQgddTAAEKLEKVYEElratgaaaaeakarriLAGLGFDPeMQNRPTQKFSGG 447
Cdd:PRK10575 92 QQLPAAEgmTVRELVAIGRYPWHGALGR---FGAADREKVEEA----------------ISLVGLKP-LAHRLVDSLSGG 151
|
170 180
....*....|....*....|....*....
gi 39930335 448 WRMRVSLARALFMEPTLLMLDEPTNHLDL 476
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
443-499 |
1.82e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 1.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGW--RKTLLIVSHD 499
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
305-475 |
1.92e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 40.32 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 305 AHGKELFVNADLYIVAGRRYGLVGPNGKGKTTLLKHIANRalsIPPNIDVllcEQEVVADETPAVQAVLRAdtkrlrlle 384
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSV---EGDIHYNGIPYKEFAEKY--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 385 eerrlQGQL---EQGDD-----TAAEKLEkvyeelratgaaaaeakarrilaglgFDPEMQ-NRPTQKFSGGWRMRVSLA 455
Cdd:cd03233 82 -----PGEIiyvSEEDVhfptlTVRETLD--------------------------FALRCKgNEFVRGISGGERKRVSIA 130
|
170 180
....*....|....*....|
gi 39930335 456 RALFMEPTLLMLDEPTNHLD 475
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLD 150
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
445-498 |
1.93e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.87 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDLNAVIWLNNYLQGWRK--TLLIVSH 498
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKgrTTFIIAH 528
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
734-812 |
2.07e-03 |
|
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: 40.61 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINDYKGAVIVVSH---DARLITEtncQLWVVEE 806
Cdd:TIGR01277 128 QLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHhlsDARAIAS---QIAVVSQ 204
|
....*.
gi 39930335 807 QGVSQI 812
Cdd:TIGR01277 205 GKIKVV 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
620-818 |
2.10e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.49 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 620 HGVTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM-----------RKNHRLKIG----- 683
Cdd:PRK13657 338 DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdirtvtRASLRRNIAvvfqd 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 684 --FFNQQYAEQLHM------EETPTEYLQRSFNLPYQDARKclgrFGLESHAHTiQICKLSGGQKARVVFAELACREPDV 755
Cdd:PRK13657 418 agLFNRSIEDNIRVgrpdatDEEMRAAAERAQAHDFIERKP----DGYDTVVGE-RGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 756 LILDEPTNNLDIESIDALGEAINDY-KG-AVIVVSHdaRLITETNCQLWVVEEQGVSQIDGDFDD 818
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELmKGrTTFIIAH--RLSTVRNADRILVFDNGRVVESGSFDE 555
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
616-796 |
2.50e-03 |
|
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: 40.41 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHGVT--FGyeGQKPLfKNLDFGIDMDSRICIVGPNGVGKSTllllltgkltptngemrknhrlkigFFNQ---QY- 689
Cdd:COG0411 4 LLEVRGLTkrFG--GLVAV-DDVSLEVERGEIVGLIGPNGAGKTT-------------------------LFNLitgFYr 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 690 -----------------------------------------------AEQLHMEETPTEYLQRSFNLPYQD------ARK 716
Cdd:COG0411 56 ptsgrilfdgrditglpphriarlgiartfqnprlfpeltvlenvlvAAHARLGRGLLAALLRLPRARREErearerAEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 717 CLGRFGLESHAHTiQICKLSGGQKARVvfaELA---CREPDVLILDEPTNNLDIESIDALGE---AINDYKG-AVIVVSH 789
Cdd:COG0411 136 LLERVGLADRADE-PAGNLSYGQQRRL---EIAralATEPKLLLLDEPAAGLNPEETEELAElirRLRDERGiTILLIEH 211
|
....*..
gi 39930335 790 DARLITE 796
Cdd:COG0411 212 DMDLVMG 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
429-504 |
2.62e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 429 GLGFDPemQNRPTQKFSGGWRMRVSLARALFMEP--TLLMLDEPTNHLDLNAVIWLNNYLQGWRK---TLLIVSHDQGFL 503
Cdd:cd03238 75 GLGYLT--LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVILIEHNLDVL 152
|
.
gi 39930335 504 D 504
Cdd:cd03238 153 S 153
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
732-788 |
2.68e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 2.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 732 ICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY--KG-AVIVVS 788
Cdd:PRK13549 403 IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvqQGvAIIVIS 462
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
734-766 |
2.82e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.98 E-value: 2.82e-03
10 20 30
....*....|....*....|....*....|...
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:PRK11650 134 ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
326-475 |
2.98e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.19 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 326 LVGPNGKGKTTLLKHIANRalsIPPNI----DVLLCEQEVVADETPAVQAVLRAD-------TkrlrlLEEERRLQGQLE 394
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFR---SPKGVkgsgSVLLNGMPIDAKEMRAISAYVQQDdlfiptlT-----VREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 395 QGDDTAA-EKLEKVYEelratgaaaaeakarrILAGLGFDPEMQNR---PTQK--FSGGWRMRVSLARALFMEPTLLMLD 468
Cdd:TIGR00955 128 MPRRVTKkEKRERVDE----------------VLQALGLRKCANTRigvPGRVkgLSGGERKRLAFASELLTDPPLLFCD 191
|
....*..
gi 39930335 469 EPTNHLD 475
Cdd:TIGR00955 192 EPTSGLD 198
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
445-476 |
3.17e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 40.23 E-value: 3.17e-03
10 20 30
....*....|....*....|....*....|..
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLDL 476
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
736-790 |
3.35e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 40.33 E-value: 3.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930335 736 SGGQKARVVFAELACREPDVLILDEPTNNLDIeSIDAlgEAIN-------DYKGAVIVVSHD 790
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQA--QVLNlmmdlqqELGLSYVFISHD 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
735-808 |
3.41e-03 |
|
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: 39.78 E-value: 3.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY-KGA-VIVVSHdaRLITETNCQLWVVEEQG 808
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAfKDCtVLTIAH--RLDTIIDSDRILVLDKG 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
616-812 |
3.44e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 616 VLGLHG--VTFGYEGQK-PLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEM-------RKNHRLKIGFF 685
Cdd:PRK10261 12 VLAVENlnIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 686 NQQYAEQLHME--------ETPTEYLQRSFNLPYQ------------------DARKCLGRFGL-ESHA------Htiqi 732
Cdd:PRK10261 92 EQSAAQMRHVRgadmamifQEPMTSLNPVFTVGEQiaesirlhqgasreeamvEAKRMLDQVRIpEAQTilsrypH---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 733 cKLSGGQKARVVFA-ELACRePDVLILDEPTNNLDIESIDALGEAIN----DYKGAVIVVSHDARLITETNCQLWV---- 803
Cdd:PRK10261 168 -QLSGGMRQRVMIAmALSCR-PAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEIADRVLVmyqg 245
|
250
....*....|.
gi 39930335 804 --VEEQGVSQI 812
Cdd:PRK10261 246 eaVETGSVEQI 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
435-506 |
3.59e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 3.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 435 EMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLDLN---AVIWLNNYLQGWRKTLLI-VSHDQGFLDDV 506
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMGVIfITHDMGVVAEI 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
734-766 |
3.73e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 40.02 E-value: 3.73e-03
10 20 30
....*....|....*....|....*....|...
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
440-475 |
3.99e-03 |
|
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: 40.82 E-value: 3.99e-03
10 20 30
....*....|....*....|....*....|....*.
gi 39930335 440 PTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:COG4172 154 PHQ-LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
705-823 |
4.52e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 705 RSFNLPYQDAR----KCLGRFGLeSHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDY 780
Cdd:NF000106 112 R*LDLSRKDARaradELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM 190
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 39930335 781 --KGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGDFDDYKREV 823
Cdd:NF000106 191 vrDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKV 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
711-790 |
4.76e-03 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 39.93 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 711 YQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFAELACREPDVLILDEPTNNLD----IESIDALGEAINDYKGAVIV 786
Cdd:cd03294 138 EERAAEALELVGLEGWEHK-YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVF 216
|
....
gi 39930335 787 VSHD 790
Cdd:cd03294 217 ITHD 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
735-790 |
5.01e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.77 E-value: 5.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEAINDYKG--AVIVVSHD 790
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
688-815 |
5.26e-03 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 40.04 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 688 QYAEQLHMEETPTEYLQRSFNLPYQDAR-KCLGRFGLESHA---HTIQICKLSGGQKARVV----FAELACRepdvlILD 759
Cdd:cd05675 238 AYFAQMAELAGGEGGALMLTAVPVLDPAlAKLGPSAPLLNAmlrNTASPTMLDAGYATNVLpgraTAEVDCR-----ILP 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 760 EPTNNldiESIDALGEAINDYKGAVIVVSHDARLITETNCQLWVVEEQGVSQIDGD 815
Cdd:cd05675 313 GQSEE---EVLDTLDKLLGDPDVSVEAVHLEPATESPLDSPLVDAMEAAVQAVDPG 365
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
735-804 |
5.49e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 39.24 E-value: 5.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 735 LSGGQKARVVFAELACREPDVLILDEPTNNLDIESIDALGEA-----INDYKGAVIVVSHDARLITETNcqlWVV 804
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYLPHAD---WII 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
443-475 |
5.54e-03 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 40.09 E-value: 5.54e-03
10 20 30
....*....|....*....|....*....|...
gi 39930335 443 KFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
438-471 |
5.57e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.00 E-value: 5.57e-03
10 20 30
....*....|....*....|....*....|....
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPT 471
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
617-789 |
5.85e-03 |
|
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: 38.99 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 617 LGLHGVTFGYEG----QKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTgkltptnGEMRKNHrlkiGFFNQQ---- 688
Cdd:cd03250 1 ISVEDASFTWDSgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELEKLS----GSVSVPgsia 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 689 YAEQlhmeeTPteYLQRS-------FNLPYQDARK-------CLGRfGLESHAHTIQIC------KLSGGQKARVVFAEL 748
Cdd:cd03250 70 YVSQ-----EP--WIQNGtirenilFGKPFDEERYekvikacALEP-DLEILPDGDLTEigekgiNLSGGQKQRISLARA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 39930335 749 ACREPDVLILDEPTNNLDIE---SI--DALGEAINDYKgAVIVVSH 789
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHvgrHIfeNCILGLLLNNK-TRILVTH 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
715-788 |
5.90e-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: 40.19 E-value: 5.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930335 715 RKCLGRFGLESHAHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDIES---IDALGEAINDYKGAVIVVS 788
Cdd:TIGR02633 384 GSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVS 460
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
628-790 |
6.48e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 39.33 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 628 GQKPLFKNLDFGIDMDSRICIVGPNGVGKSTLLLLLTGKLTPTNGEMRKNHRLKIGFFNQQYAEQ-------------LH 694
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRravlpqhsslafpFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 695 MEE------TPteyLQRSFNLPYQDARKCLGRFGLESHAHTiQICKLSGGQKARVVFA-------ELACREPDVLILDEP 761
Cdd:COG4559 92 VEEvvalgrAP---HGSSAAQDRQIVREALALVGLAHLAGR-SYQTLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEP 167
|
170 180 190
....*....|....*....|....*....|..
gi 39930335 762 TNNLDIESIDALGEAINDY---KGAVIVVSHD 790
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLarrGGGVVAVLHD 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
711-834 |
6.48e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.99 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930335 711 YQDARKCLGRFGLESHAHTIqICKLSGGQKARVVFAELACREPDVLILDEPTNNL-DIESiDALGEAINDYK--GAVIV- 786
Cdd:PRK10762 119 YAEADKLLARLNLRFSSDKL-VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIRELKsqGRGIVy 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 39930335 787 VSHDARLITETNCQLWV------VEEQGVSQIDGDfddykrevleALGEVMVNR 834
Cdd:PRK10762 197 ISHRLKEIFEICDDVTVfrdgqfIAEREVADLTED----------SLIEMMVGR 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
427-475 |
6.48e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.45 E-value: 6.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 39930335 427 LAGLGFDPEMQNRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
734-766 |
6.91e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 39.70 E-value: 6.91e-03
10 20 30
....*....|....*....|....*....|...
gi 39930335 734 KLSGGQKARVVFAELACREPDVLILDEPTNNLD 766
Cdd:PRK11432 136 QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
727-788 |
7.00e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 7.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930335 727 AHTIQICKLSGGQKARVVFAELACREPDVLILDEPTNNLDI----ESIDALGEAINDYKGAVIVVS 788
Cdd:PRK10982 384 GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVgakfEIYQLIAELAKKDKGIIIISS 449
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
438-471 |
7.03e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 7.03e-03
10 20 30
....*....|....*....|....*....|....
gi 39930335 438 NRPTQKFSGGWRMRVSLARALFMEPTLLMLDEPT 471
Cdd:NF033858 131 DRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
444-511 |
7.25e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 40.31 E-value: 7.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930335 444 FSGGWRMRVSLARALFMEPTLLMLDEPTNHLD-------LNAVIWLNNYLQGwrKTLLIVSHDQGFLDDVctDII 511
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYLPQV--DVI 831
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
445-475 |
7.54e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.86 E-value: 7.54e-03
10 20 30
....*....|....*....|....*....|.
gi 39930335 445 SGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
622-657 |
7.88e-03 |
|
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: 39.80 E-value: 7.88e-03
10 20 30
....*....|....*....|....*....|....*.
gi 39930335 622 VTFGYEGQKPLFKNLDFGIDMDSRICIVGPNGVGKS 657
Cdd:COG5265 363 VSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKS 398
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
430-475 |
8.51e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.44 E-value: 8.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 39930335 430 LGFDPEMQNRPTQkFSGGWRMRVSLARALFMEPTLLMLDEPTNHLD 475
Cdd:PRK11650 122 LELEPLLDRKPRE-LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| |
