|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-1241 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 935.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 8 DRSKHLGEELQRYWDKELLRAKkdsrkPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPddsva 87
Cdd:PLN03130 267 DQTETLYRSFQKCWDEELKKPK-----PWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP----- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 88 LHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTI 167
Cdd:PLN03130 337 AWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 168 FLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYA 247
Cdd:PLN03130 417 QLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYA 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 248 WEKSFADLIANLRKKEISKILGSSYLRGMNMasfFIANKVILFVT---FTSYVLLGNEITASHVFVAMTLYGAVRLTvtL 324
Cdd:PLN03130 497 WENSFQSKVQTVRDDELSWFRKAQLLSAFNS---FILNSIPVLVTvvsFGVFTLLGGDLTPARAFTSLSLFAVLRFP--L 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 325 F-FPSAIERGSEAIVSIRRIKNFLLLDEL-----PQRKAHVPSdgkaiVHVQDFTAFWDKALDSPTLQGLSFIARPGELL 398
Cdd:PLN03130 572 FmLPNLITQAVNANVSLKRLEELLLAEERvllpnPPLEPGLPA-----ISIKNGYFSWDSKAERPTLSNINLDVPVGSLV 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 399 AVVGPVGAGKSSLLSAVLGELPPAS-GLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLL 477
Cdd:PLN03130 647 AIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLL 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 478 EDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAA 557
Cdd:PLN03130 727 PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 558 SHILILKDGEMVQKGTYTEFLKSGVDFGSLL----KKENEEAEPSTAPGTPTLRKRTfsEASIWSQQSSRPSLKDGAPEG 633
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEELSNNGPLFQKLMenagKMEEYVEENGEEEDDQTSSKPV--ANGNANNLKKDSSSKKKSKEG 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 634 QDAENTQavqpeESRSEGRIGFKAYKNYFSA-GASWFFIIfLVLLNMVGQVFYVLQDWWLSHWANkQGAlnntrnangni 712
Cdd:PLN03130 885 KSVLIKQ-----EERETGVVSWKVLERYKNAlGGAWVVMI-LFLCYVLTEVFRVSSSTWLSEWTD-QGT----------- 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 713 TETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDL 792
Cdd:PLN03130 947 PKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRN 1026
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 793 LPL---TFLDFIQTLLLVVSVIAVAAAVIPWILIPLVplsVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLW 869
Cdd:PLN03130 1027 VAVfvnMFLGQIFQLLSTFVLIGIVSTISLWAIMPLL---VLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLS 1103
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 870 TIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVA-FGSLVLAKTLN----AGQVGLALSYAL 944
Cdd:PLN03130 1104 TIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTAsFAVMQNGRAENqaafASTMGLLLSYAL 1183
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 945 TLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECK-KRPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIK 1023
Cdd:PLN03130 1184 NITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIEnNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEIS 1263
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1024 SREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEE 1102
Cdd:PLN03130 1264 PSEKVGIVGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDAD 1343
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1103 LWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ 1182
Cdd:PLN03130 1344 LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS 1423
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1183 CTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLFYKMVQQLGKGEAAAL 1241
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTGAANAQYL 1482
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-1234 |
0e+00 |
|
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: 920.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 33 RKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDsvalHTAYGYAAVLSMCTLILAILHHLY 112
Cdd:TIGR00957 303 RKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPD----WQGYFYTGLLFVCACLQTLILHQY 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 113 FYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGI 192
Cdd:TIGR00957 379 FHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 193 SCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSY 272
Cdd:TIGR00957 459 SVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAY 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 273 LRGMNMASFFIANKVILFVTFTSYVLL--GNEITASHVFVAMTLYGAVRLTVTLFfPSAIERGSEAIVSIRRIKNFLLLD 350
Cdd:TIGR00957 539 LHAVGTFTWVCTPFLVALITFAVYVTVdeNNILDAEKAFVSLALFNILRFPLNIL-PMVISSIVQASVSLKRLRIFLSHE 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 351 EL-PQ---RKAHVPSDGKAI-VHVQDFTafWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGL 425
Cdd:TIGR00957 618 ELePDsieRRTIKPGEGNSItVHNATFT--WARD-LPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 426 VSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARA 505
Cdd:TIGR00957 695 VHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARA 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 506 VYQDADIYLLDDPLSAVDAEVGKHLFQLCICQ--ALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVD 583
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGA 854
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 584 FGSLLKK--------------------ENEEAEP--STAPGTPTLRK---RTFSEASIWSQQSSR---PSLKDGAPEGQd 635
Cdd:TIGR00957 855 FAEFLRTyapdeqqghledswtalvsgEGKEAKLieNGMLVTDVVGKqlqRQLSASSSDSGDQSRhhgSSAELQKAEAK- 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 636 aENTQAVQPEESRSEGRIGFKAYKNYfsAGASWFFIIFLVLLNMVGQ-VFYVLQDWWLSHWANKqgALNNTRNANGNITe 714
Cdd:TIGR00957 934 -EETWKLMEADKAQTGQVELSVYWDY--MKAIGLFITFLSIFLFVCNhVSALASNYWLSLWTDD--PMVNGTQNNTSLR- 1007
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 715 tldlswyLGIYAGLtavtvlfGIARSLLVF-YIL------VNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIG 787
Cdd:TIGR00957 1008 -------LSVYGAL-------GILQGFAVFgYSMavsiggIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELD 1073
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 788 HMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQG 867
Cdd:TIGR00957 1074 TVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLG 1153
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 868 LWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLM 947
Cdd:TIGR00957 1154 VSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVT 1233
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 948 GMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECKK-RPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSRE 1026
Cdd:TIGR00957 1234 FYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEtAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGE 1313
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1027 KVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWR 1105
Cdd:TIGR00957 1314 KVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWW 1393
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1106 ALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTV 1185
Cdd:TIGR00957 1394 ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTV 1473
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*....
gi 255683324 1186 LTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNpESLFYKMVQQLG 1234
Cdd:TIGR00957 1474 LTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ-RGIFYSMAKDAG 1521
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-1242 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 856.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 8 DRSKHLGEELQRYWDKELLRAKkdsrkPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPddsva 87
Cdd:PLN03232 267 DQTETLIKRFQRCWTEESRRPK-----PWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP----- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 88 LHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTI 167
Cdd:PLN03232 337 AWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 168 FLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYA 247
Cdd:PLN03232 417 QLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYA 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 248 WEKSFADLIANLRKKEISKILGSSYLRGMNMasfFIANK---VILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTL 324
Cdd:PLN03232 497 WEKSFESRIQGIRNEELSWFRKAQLLSAFNS---FILNSipvVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNM 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 325 FfPSAIERGSEAIVSIRRIKNFLLLDE--LPQRKAHVPsdGKAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVG 402
Cdd:PLN03232 574 L-PNLLSQVVNANVSLQRIEELLLSEEriLAQNPPLQP--GAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVG 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 403 PVGAGKSSLLSAVLGELPPA-SGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGD 481
Cdd:PLN03232 651 GTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRD 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 482 LTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHIL 561
Cdd:PLN03232 731 LTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 562 ILKDGEMVQKGTYTEFLKSGVDFGSLLKKENE-EAEPSTAPGTPTLRKRTFSEASIWSQQSSrpslkdgAPEGQDAENTQ 640
Cdd:PLN03232 811 LVSEGMIKEEGTFAELSKSGSLFKKLMENAGKmDATQEVNTNDENILKLGPTVTIDVSERNL-------GSTKQGKRGRS 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 641 AVQPEESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNMVGQVFYVLQDWWLSHWANkQGALNNTRNAngnitetldlsW 720
Cdd:PLN03232 884 VLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTD-QSTPKSYSPG-----------F 951
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 721 YLGIYA--GLTAVTVLFgiARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMD----DLLP 794
Cdd:PLN03232 952 YIVVYAllGFGQVAVTF--TNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDrnvaNLMN 1029
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 795 LtFLDFIQTLLLVVSVIAVAAAVIPWILIPLVplsVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAY 874
Cdd:PLN03232 1030 M-FMNQLWQLLSTFALIGTVSTISLWAIMPLL---ILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY 1105
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 875 KAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVA-FGSLVLAKTLN----AGQVGLALSYALTLMGM 949
Cdd:PLN03232 1106 KAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTAtFAVLRNGNAENqagfASTMGLLLSYTLNITTL 1185
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 950 FQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECKK-RPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKV 1028
Cdd:PLN03232 1186 LSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENnRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKV 1265
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1029 GIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWRAL 1107
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEAL 1345
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1108 EEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLT 1187
Cdd:PLN03232 1346 ERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLV 1425
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1188 IAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLFYKMVQQLGKGEAAALT 1242
Cdd:PLN03232 1426 IAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYLS 1480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-1226 |
0e+00 |
|
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: 807.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 8 DRSKHLGEELQRYWDKELLRAKKdsrKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEyfeKYDPDDSVA 87
Cdd:TIGR01271 44 DSADNLSERLEREWDRELASAKK---NPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIA---SYDPFNAPE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 88 LHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTI 167
Cdd:TIGR01271 118 REIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 168 FLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYA 247
Cdd:TIGR01271 198 LAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYC 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 248 WEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTSYVLLgNEITASHVFVAMTLYGAVRLTVTLFFP 327
Cdd:TIGR01271 278 WEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI-KGIILRRIFTTISYCIVLRMTVTRQFP 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 328 SAIERGSEAIVSIRRIKNFLLLDELPQRKAHVPSDGKAIVHVqdfTAFWDKALD-------------------------- 381
Cdd:TIGR01271 357 GAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNV---TASWDEGIGelfekikqnnkarkqpngddglffsn 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 382 -----SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKY 456
Cdd:TIGR01271 434 fslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSY 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 457 EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCIC 536
Cdd:TIGR01271 514 DEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLC 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 537 QALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL---------------------------- 588
Cdd:TIGR01271 594 KLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerrnsiltetlrrvsid 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 589 ---------------------------------------KK--------------------------------ENEEAEP 597
Cdd:TIGR01271 674 gdstvfsgpetikqsfkqpppefaekrkqsiilnpiasaRKfsfvqmgpqkaqattiedavrepserkfslvpEDEQGEE 753
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 598 S-----------------------------TAPGTPTLRKRTFSEASIWSQQS---------SRPSLKDGAPEGQDAENT 639
Cdd:TIGR01271 754 SlprgnqyhhglqhqaqrrqsvlqlmthsnRGENRREQLQTSFRKKSSITQQNelaseldiySRRLSKDSVYEISEEINE 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 640 QAVQP----EESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNMVGQVF-YVLQDWWLSHWANKQGAL-NNTRNANGNIT 713
Cdd:TIGR01271 834 EDLKEcfadERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLAEVAaSLLGLWLITDNPSAPNYVdQQHANASSPDV 913
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 714 E-----TLDLSWYL-GIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIG 787
Cdd:TIGR01271 914 QkpviiTPTSAYYIfYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMA 993
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 788 HMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQG 867
Cdd:TIGR01271 994 IIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKG 1073
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 868 LWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVAFGSlVLAKTLNAGQVGLALSYALTLM 947
Cdd:TIGR01271 1074 LWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIA-IGTNQDGEGEVGIILTLAMNIL 1152
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 948 GMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPwECKKRPPPG----------------WPHEGVIVFDNVNFTYSLDG 1011
Cdd:TIGR01271 1153 STLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEP-RPSGGGGKYqlstvlvienphaqkcWPSGGQMDVQGLTAKYTEAG 1231
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1012 PLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKN 1091
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1092 LDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDEL 1171
Cdd:TIGR01271 1312 LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1172 IQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLqNPESLF 1226
Cdd:TIGR01271 1392 IRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLF 1445
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-1239 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 697.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 33 RKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLflgkIIEYFEKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLY 112
Cdd:PTZ00243 230 KRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPV----LLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 113 FYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGK--TTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEI 190
Cdd:PTZ00243 306 YYISIRCGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 191 GISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFadlIANLRKKEISKIlgs 270
Cdd:PTZ00243 386 GWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCF---VANIEDKRAREL--- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 271 SYLRGM---NMASFFIAN---KVILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFfPSAIERGSEAIVSIRRIK 344
Cdd:PTZ00243 460 RYLRDVqlaRVATSFVNNatpTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMI-PWVFTTVLQFLVSIKRIS 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 345 NFLLLDEL-------------PQRKAHVPSDGKAIVHVQDFTAFW-----------------------------DKALDS 382
Cdd:PTZ00243 539 TFLECDNAtcstvqdmeeywrEQREHSTACQLAAVLENVDVTAFVpvklprapkvktsllsralrmlcceqcrpTKRHPS 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PT-------------------------------------------------------LQGLSFIARPGELLAVVGPVGAG 407
Cdd:PTZ00243 619 PSvvvedtdygspssasrhiveggtgggheatptsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSG 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 408 KSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGD 487
Cdd:PTZ00243 699 KSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGE 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 488 RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGE 567
Cdd:PTZ00243 779 KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 568 MVQKGTYTEFLKSGV--DFGSLLK---------KENEEAEPSTAPGTPTLRKRtfseasiwsqqssRPSLKDGAPEGQDA 636
Cdd:PTZ00243 859 VEFSGSSADFMRTSLyaTLAAELKenkdskegdADAEVAEVDAAPGGAVDHEP-------------PVAKQEGNAEGGDG 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 637 ENTQAVQP----EESRSEGRIGFKAYKNYFSA--GASWffIIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNNTRNang 710
Cdd:PTZ00243 926 AALDAAAGrlmtREEKASGSVPWSTYVAYLRFcgGLHA--AGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAATY--- 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 711 nitetldLSWYLGIyagltavtVLFGIA----RSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDI 786
Cdd:PTZ00243 1001 -------LYVYLGI--------VLLGTFsvplRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDI 1065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 787 GHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQ 866
Cdd:PTZ00243 1066 DILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQ 1145
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 867 GLWTIRAY-KAEERCQELFdAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVAF----GSLVLAKTLNAGQVGLALS 941
Cdd:PTZ00243 1146 GSATITAYgKAHLVMQEAL-RRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALigviGTMLRATSQEIGLVSLSLT 1224
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 942 YALTLMGMFQWSVRQSAEVENMMISVERVIEYTD-LEKEAPWE-------CKKR-----------------PPPGWPH-- 994
Cdd:PTZ00243 1225 MAMQTTATLNWLVRQVATVEADMNSVERLLYYTDeVPHEDMPEldeevdaLERRtgmaadvtgtvviepasPTSAAPHpv 1304
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 995 -EGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRK 1072
Cdd:PTZ00243 1305 qAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRR 1384
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNN 1152
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1153 RILII-DEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLFYKMVQ 1231
Cdd:PTZ00243 1465 SGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVE 1544
|
....*...
gi 255683324 1232 QLGKGEAA 1239
Cdd:PTZ00243 1545 ALGRSEAK 1552
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
667-974 |
0e+00 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 547.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 667 SWFFIIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNNTRNANGNIT------ETLDLSWYLGIYAGLTAVTVLFGIARS 740
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENstnvdiEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 741 LLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPW 820
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 821 ILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLT 900
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 901 TSRWFAVRLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
51-343 |
6.60e-162 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 484.80 E-value: 6.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 51 ILGIFTLIEEGTRVVQPLFLGKIIEYFEkyDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 130
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFE--GNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 131 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 210
Cdd:cd18593 79 IYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 211 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 290
Cdd:cd18593 159 FGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 291 VTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFFPSAIERGSEAIVSIRRI 343
Cdd:cd18593 239 LTFLAYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
996-1215 |
6.08e-133 |
|
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: 405.72 E-value: 6.08e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 1074
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRI 1154
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1155 LIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEP 1215
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
51-343 |
5.34e-127 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 392.77 E-value: 5.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 51 ILGIFTLIEEGTRVVQPLFLGKIIEYFekyDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 130
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYF---VPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 131 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 210
Cdd:cd18594 78 IYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 211 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 290
Cdd:cd18594 158 LGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 291 VTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFFPSAIERGSEAIVSIRRI 343
Cdd:cd18594 238 ATFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
51-343 |
7.59e-114 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 357.57 E-value: 7.59e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 51 ILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 130
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEP---LSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 131 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 210
Cdd:cd18579 78 IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 211 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 290
Cdd:cd18579 158 LAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 291 VTFTSYVLLGNEITASHVFVAMTLYGAVRlTVTLFFPSAIERGSEAIVSIRRI 343
Cdd:cd18579 238 ATFATYVLLGNPLTAAKVFTALSLFNLLR-FPLLMLPQAISSLIEALVSLKRI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
668-1231 |
9.88e-114 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 368.34 E-value: 9.88e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 668 WFFIIFLVLLNMVGQVFYVLQDWWLSHWANkqgALNNTRNANGnitetldLSWYLGIYAGLTAVTVLFGIARSLLVFYIL 747
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIID---ALLAGGDLSA-------LLLLLLLLLGLALLRALLSYLQRYLLARLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 748 VNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVP 827
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 828 LSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAV 907
Cdd:COG1132 170 VLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 908 RLDAICAI-FVIVVAFGS-LVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECK 985
Cdd:COG1132 250 LMELLGNLgLALVLLVGGlLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 986 KRPPPgwPHEGVIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTE 1064
Cdd:COG1132 330 AVPLP--PVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGVDIRD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1065 IGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEH-TDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVC 1143
Cdd:COG1132 407 LTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1144 LARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvLLQ 1220
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEqgtHEE---LLA 563
|
570
....*....|.
gi 255683324 1221 NpESLFYKMVQ 1231
Cdd:COG1132 564 R-GGLYARLYR 573
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
671-974 |
5.13e-113 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 355.66 E-value: 5.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 671 IIFLVLLNMVGQVFYVLQDWWLSHWANkqgalNNTRNANgnitetLDLSWYLGIYAGLTAV-TVLFGIARSLLVFYILVN 749
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSS-----DWSSSPN------SSSGYYLGVYAALLVLaSVLLVLLRWLLFVLAGLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 750 ASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLS 829
Cdd:cd18580 70 ASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 830 VVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRL 909
Cdd:cd18580 150 VVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 910 DAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18580 230 DLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
367-567 |
1.31e-111 |
|
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: 347.92 E-value: 1.31e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKA--LDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSG 444
Cdd:cd03250 1 ISVEDASFTWDSGeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255683324 525 EVGKHLFQLCICQAL-HEKITILVTHQLQYLKAASHILILKDGE 567
Cdd:cd03250 161 HVGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
668-974 |
2.15e-91 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 297.55 E-value: 2.15e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 668 WFFIIFLVLLNMVGQVFyvlQDWWLSHWAnKQGALNNTRNAN------GNITETLDLSWYLGIYAGLTAVTVLFGIARSL 741
Cdd:cd18599 5 FLFVLLLFILSVGSTVF---SDWWLSYWL-KQGSGNTTNNVDnstvdsGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 742 LVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWI 821
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 822 LIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTT 901
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 902 SRWFAVRLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
668-974 |
2.31e-91 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 296.31 E-value: 2.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 668 WFFIIFLVLLNmvgQVFYVLQDWWLSHWANKQGALNNTRnangnitetldlswYLGIYAGLTAVTVLFGIARSLLVFYIL 747
Cdd:cd18606 1 LPLLLLLLILS---QFAQVFTNLWLSFWTEDFFGLSQGF--------------YIGIYAGLGVLQAIFLFLFGLLLAYLG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 748 VNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVP 827
Cdd:cd18606 64 IRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 828 LSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAV 907
Cdd:cd18606 144 LLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAI 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 908 RLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18606 224 RLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
710-1232 |
3.81e-89 |
|
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: 304.83 E-value: 3.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 710 GNITETLdlsWYLGI-YAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSkDIGH 788
Cdd:COG2274 189 NQDLSTL---WVLAIgLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVES 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 789 MDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWI-LIPLVpLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQG 867
Cdd:COG2274 265 IREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLaLVVLL-LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRG 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 868 LWTIRAYKAEERCQELFDAHQDLHSEA---WFLFLTTSRWFAVRLDAICAIFVIVVAfGSLVLAKTLNAGQ-------VG 937
Cdd:COG2274 344 IETIKALGAESRFRRRWENLLAKYLNArfkLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQliafnilSG 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 938 LALSYALTLMGMFQwsvrqsaEVENMMISVERVIEYTDLEKEAPWECKKRPPPgwPHEGVIVFDNVNFTYSLDGPLVLKH 1017
Cdd:COG2274 423 RFLAPVAQLIGLLQ-------RFQDAKIALERLDDILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDN 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1018 LTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFN 1096
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1097 EH-TDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQK 1175
Cdd:COG2274 574 PDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1176 IREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEyDEPYVLLQNPESLFYKMVQQ 1232
Cdd:COG2274 654 LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVE-DGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
671-974 |
7.12e-89 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 289.76 E-value: 7.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 671 IIFLVLLNMVGQVFYVLQDWWLSHWANkqgalNNTRNANGNITETldlSWYLGIYAGLTAVTVLFGIARSLLVFYILVNA 750
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSD-----DPALNGTQDTEQR---DYRLGVYGALGLGQAIFVFLGSLALALGCVRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 751 SQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSV 830
Cdd:cd18603 73 SRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 831 VFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLD 910
Cdd:cd18603 153 LYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 911 AICAifvIVVAFGSL--VLAK-TLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18603 233 FLGN---LIVLFAALfaVLSRdSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
668-974 |
7.65e-89 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 289.75 E-value: 7.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 668 WFFIIFLVLLnmvGQVFYVLQDWWLSHWANKQGALNNTRNANGNitetldLSWYLGIYAGLTAVTVLFGIARSLLVFYIL 747
Cdd:cd18604 1 WALLLLLFVL---SQLLSVGQSWWLGIWASAYETSSALPPSEVS------VLYYLGIYALISLLSVLLGTLRYLLFFFGS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 748 VNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVP 827
Cdd:cd18604 72 LRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 828 LSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAV 907
Cdd:cd18604 152 LAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 908 RLDAICAIFVIVVAFGsLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18604 232 RIDLLGALFSFATAAL-LVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
992-1215 |
5.49e-88 |
|
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: 283.92 E-value: 5.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 992 WPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL 1070
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWRALEevqlkeaiedlpgkmdteLAESGSNFSVGQRQLVCLARAILK 1150
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1151 NNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEP 1215
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
671-974 |
6.28e-83 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 273.71 E-value: 6.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 671 IIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNN-TRNANGNITETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVN 749
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASvVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 750 ASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLS 829
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 830 VVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRL 909
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 910 DAICAIFVIVVAFGSLV--LAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18602 241 DYLGAVIVFLAALSSLTaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
51-343 |
1.85e-79 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 263.18 E-value: 1.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 51 ILGIFTLIEEGTRVVQPLFLGKIIEYFEkydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 130
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVE----DPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 131 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 210
Cdd:cd18595 77 IYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 211 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 290
Cdd:cd18595 157 LARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 291 VTFTSYVLLG--NEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 343
Cdd:cd18595 237 ATFATYVLSDpdNVLDAEKAFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
53-343 |
6.82e-78 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 258.92 E-value: 6.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 53 GIFTLIEEGTRVVQPLFLGKIIEYFE-KYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMI 131
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEdAYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 132 YRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCI 211
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 212 GKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFV 291
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 292 TFTSYVLLGNEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 343
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
40-581 |
1.55e-75 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 262.41 E-value: 1.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 40 AIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKII-EYFEKYDpddsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQC 118
Cdd:COG1132 14 RYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD------LSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 119 AGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIAVTVLLWV---EIGISC 194
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVidwRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 195 LAGLAVLVILL-PLQSCIGKLFSSLRSKTAAFTdariRTMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISKILG 269
Cdd:COG1132 168 LLVLPLLLLVLrLFGRRLRKLFRRVQEALAELN----GRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 270 SSYLRGMNMASFFIAnkVILFVTFTSYVLLGNEITAShVFVAMTLYgavrlTVTLFFP-----SAIERGSEAIVSIRRIk 344
Cdd:COG1132 244 SALFFPLMELLGNLG--LALVLLVGGLLVLSGSLTVG-DLVAFILY-----LLRLFGPlrqlaNVLNQLQRALASAERI- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 345 nFLLLDELPQRK----AHVPSDGKAIVHVQDFTAFWDKalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP 420
Cdd:COG1132 315 -FELLDEPPEIPdppgAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 421 PASG-------------LVSVHGRIAYVSQQPWVFSGTVRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIG 486
Cdd:COG1132 392 PTSGrilidgvdirdltLESLRRQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 487 DRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCICQALHEKITILVTHQLQYLKAASHILILKDG 566
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
570
....*....|....*
gi 255683324 567 EMVQKGTYTEFLKSG 581
Cdd:COG1132 551 RIVEQGTHEELLARG 565
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
664-1221 |
7.32e-74 |
|
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: 256.99 E-value: 7.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 664 AGASWFFIIFLVLLNMVGQVFYVLQDWWLSHwankqgALNNTRNANGNITEtldLSWYLGIYAGLTAVTVLFGIARSLLV 743
Cdd:COG4988 12 ARGARRWLALAVLLGLLSGLLIIAQAWLLAS------LLAGLIIGGAPLSA---LLPLLGLLLAVLLLRALLAWLRERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 744 FYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDD-------------LLPLT------FLDFIQTL 804
Cdd:COG4988 83 FRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfarylpqlflaaLVPLLilvavfPLDWLSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 805 LLVvsviavaaavipwILIPLVPLSVVFL------VLRRYFLETSRdvkrlesttrspVFSHLSSSLQGLWTIRAYKAEE 878
Cdd:COG4988 163 ILL-------------VTAPLIPLFMILVgkgaakASRRQWRALAR------------LSGHFLDRLRGLTTLKLFGRAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 879 R-CQELFDAHQDLHSE-------AwflFLTTsrwfAVrLDAICAIFVIVVAfgsLVLAKTLNAGQVGLA-------LS-- 941
Cdd:COG4988 218 AeAERIAEASEDFRKRtmkvlrvA---FLSS----AV-LEFFASLSIALVA---VYIGFRLLGGSLTLFaalfvllLApe 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 942 -YA-LTLMGMFqWSVRQSAevenmMISVERVIEYTDLEKEAPWECKKRPPpgWPHEGVIVFDNVNFTYSlDGPLVLKHLT 1019
Cdd:COG4988 287 fFLpLRDLGSF-YHARANG-----IAAAEKIFALLDAPEPAAPAGTAPLP--AAGPPSIELEDVSFSYP-GGRPALDGLS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1020 ALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEH 1098
Cdd:COG4988 358 LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPySGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1099 -TDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIR 1177
Cdd:COG4988 438 aSDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALR 517
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 255683324 1178 EKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQN 1221
Cdd:COG4988 518 RLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
658-973 |
1.19e-70 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 239.70 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 658 YKNYFSAGASWFFIIFLVLLNMVGQVFYVLQDWWL---SHWANKQGALNNTRNANGNITETLDLSWYLGIYAGLTAVTVL 734
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 735 FGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVA 814
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 815 AAVIPWILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEA 894
Cdd:cd18600 166 SILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTAN 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 895 WFLFLTTSRWFAVRLDAICAIFVIVVAFGSlVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEY 973
Cdd:cd18600 246 WFLYLSTLRWFQMRIEMIFVIFFTAVTFIS-IGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIFKF 323
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
667-974 |
3.13e-70 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 237.43 E-value: 3.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 667 SWFFIIFLVLLnmvgQVFYVLQDWWLSHWANKQgalNNTRNANGNITETLdlswYLGIYAGLTAVTVLFGIARSLLVFYI 746
Cdd:cd18605 1 LILILLSLILM----QASRNLIDFWLSYWVSHS---NNSFFNFINDSFNF----FLTVYGFLAGLNSLFTLLRAFLFAYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 747 LVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLV 826
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 827 PLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFA 906
Cdd:cd18605 150 PLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 907 VRLDAICAIFVIVVAFGSLVLA---KTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEYT 974
Cdd:cd18605 230 IRLQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
996-1220 |
1.73e-69 |
|
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: 232.50 E-value: 1.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKM 1074
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTGTMRKNLDPFNEHTDEELW-RALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNR 1153
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1154 ILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQ 1220
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
996-1231 |
2.34e-69 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 233.26 E-value: 2.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 1074
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRI 1154
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1155 LIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLFYKMVQ 1231
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
49-343 |
1.91e-64 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 220.51 E-value: 1.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 49 YLILGIFTLIeegtrvVQPLFLGKIIEYFEKYDPDdsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 128
Cdd:cd18592 6 LLISLIFGFI------GPTILIRKLLEYLEDSDSS----VWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 129 HMIYRKALRLSNSamGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQ 208
Cdd:cd18592 76 GLLYKKILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 209 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVI 288
Cdd:cd18592 154 AFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 289 LFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 343
Cdd:cd18592 234 SVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLR-MLPYAVKALAEAKVALQRI 287
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
382-608 |
7.07e-63 |
|
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: 215.88 E-value: 7.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 382 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERY 461
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 462 EKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHE 541
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 542 KITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL----KKENEEAEPSTAPGTPTLRK 608
Cdd:cd03291 210 KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLmgydTFDQFSAERRNSILTETLRR 280
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
51-343 |
1.02e-62 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 215.49 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 51 ILGIFTLIEEGTRVVQPLFLGKIIEYFEkydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 130
Cdd:cd18598 1 PLGLLKLLADVLGFAGPLLLNKLVEFLE----DSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 131 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 210
Cdd:cd18598 77 VYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 211 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMnMASFFIANKVIL- 289
Cdd:cd18598 157 IAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATTPVLIs 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 290 FVTFTSYVLLGNEITASHVFVAMTLYGavRLTVTL-FFPSAIERGSEAIVSIRRI 343
Cdd:cd18598 236 ILTFATYVLMGNTLTAAKVFTSLALFN--MLIGPLnAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
51-343 |
1.13e-62 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 216.21 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 51 ILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDdsvALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 130
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDPGED---ATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 131 IYRKALRLSNSA-------------------MGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIG 191
Cdd:cd18596 78 IFEKALRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 192 ISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSS 271
Cdd:cd18596 158 WSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRF 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 272 YLRGMNMASFFIANKVILFVTFTSYVLL-GNEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 343
Cdd:cd18596 238 LLDLLLSLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
998-1208 |
1.34e-59 |
|
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: 201.84 E-value: 1.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1076
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTGTMRKNLdpfnehtdeelwraleevqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKNNRILI 1156
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1157 IDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGR 1208
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
998-1211 |
1.76e-59 |
|
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: 204.39 E-value: 1.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1076
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTGTMRKNL---DPfnEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNR 1153
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1154 ILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1211
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
996-1226 |
2.52e-59 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 205.47 E-value: 2.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMS 1075
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEPVLFTGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRIL 1155
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1156 IIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLqNPESLF 1226
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHF 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
998-1232 |
5.19e-57 |
|
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: 197.07 E-value: 5.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1076
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVsSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTGTMRKNLDPFNEH-TDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRIL 1155
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1156 IIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLqNPESLFYKMVQQ 1232
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKA 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
122-579 |
6.00e-57 |
|
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: 207.70 E-value: 6.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 122 RLRVAmchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVtiFLHFL---WAGPLQAIAVTVLLWV---EIGISCL 195
Cdd:COG4987 89 DLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVLlplLVALLVILAAVAFLAFfspALALVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 196 AGLAVLVILLPLqscigkLFSSL-----RSKTAAFTDARIRTMnEVITGMRIIKMY----AWEKSFADLIANLRKKE--I 264
Cdd:COG4987 163 LGLLLAGLLLPL------LAARLgrragRRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQrrL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 265 SKILGSSylRGMNMASFFIAnkVILFVTFTSYVLLGNEITASH----VFVAMTLYGAVrltVTLffPSAIERGSEAIVSI 340
Cdd:COG4987 236 ARLSALA--QALLQLAAGLA--VVAVLWLAAPLVAAGALSGPLlallVLAALALFEAL---APL--PAAAQHLGRVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 341 RRIKNflLLDELPQR---KAHVPSDGKAIVHVQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLG 417
Cdd:COG4987 307 RRLNE--LLDAPPAVtepAEPAPAPGGPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 418 ELPPASGLV-------------SVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKEryEKVIKACA---LKKDLQLLEDGD 481
Cdd:COG4987 384 FLDPQSGSItlggvdlrdldedDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD--EELWAALErvgLGDWLAALPDGL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 482 LTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQLQYLKAASHIL 561
Cdd:COG4987 462 DTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRIL 540
|
490
....*....|....*...
gi 255683324 562 ILKDGEMVQKGTYTEFLK 579
Cdd:COG4987 541 VLEDGRIVEQGTHEELLA 558
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-581 |
5.76e-56 |
|
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: 204.99 E-value: 5.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 18 QRYWDKELLRAKKDSRKPsltkaiikcywksYLILGIFTLIEEGTRVVQPLFLGKII-EYFEKYDPDDSVALHTayGYAA 96
Cdd:COG4988 1 QKPLDKRLKRLARGARRW-------------LALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPLSALLPLL--GLLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 97 VLSMCTLILAILHHLYFYHvqcAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFL-HFLwag 175
Cdd:COG4988 66 AVLLLRALLAWLRERAAFR---AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV---EALDGYFaRYL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 176 P--LQAIAVTVLLWVEI-GISCLAGLAVLV--ILLPL-QSCIGKlfsslrsKTAAFTDARIRTMN-------EVITGMRI 242
Cdd:COG4988 137 PqlFLAALVPLLILVAVfPLDWLSGLILLVtaPLIPLfMILVGK-------GAAKASRRQWRALArlsghflDRLRGLTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 243 IKMYAWEKSFADLIA----NLRKK--EISKI--LGSSYLRGMnmASFFIAnKVILFVTFTsyvLLGNEITASHVFVAMTL 314
Cdd:COG4988 210 LKLFGRAKAEAERIAeaseDFRKRtmKVLRVafLSSAVLEFF--ASLSIA-LVAVYIGFR---LLGGSLTLFAALFVLLL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 315 ----YGAVRLTVTLFFPSAiergsEAIVSIRRIKNFLLLDELPQRKAHV--PSDGKAIVHVQDFTAFWDKalDSPTLQGL 388
Cdd:COG4988 284 apefFLPLRDLGSFYHARA-----NGIAAAEKIFALLDAPEPAAPAGTAplPAAGPPSIELEDVSFSYPG--GRPALDGL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 389 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGK- 454
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRp 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 455 KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLc 534
Cdd:COG4988 437 DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA- 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 255683324 535 ICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:COG4988 516 LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-592 |
1.60e-55 |
|
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: 206.61 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 15 EELQRYWDKELL------RAKKDSRKPSLTKAI---IKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIeyfekydpdDS 85
Cdd:COG2274 115 EEFAESWTGVALlleptpEFDKRGEKPFGLRWFlrlLRRYRRLLLQVLLASLLINLLALATPLFTQVVI---------DR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 86 V----ALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLsNDVNK 161
Cdd:COG2274 186 VlpnqDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 162 FDQV--TIFLHFLWAGPLQAIAVTVLL-------WVEIGISCLAGLAVLVILLPLQSCIGKLFSsLRSKTAAFtdarirt 232
Cdd:COG2274 265 IREFltGSLLTALLDLLFVLIFLIVLFfyspplaLVVLLLIPLYVLLGLLFQPRLRRLSREESE-ASAKRQSL------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 233 MNEVITGMRIIKMYA--------WEKSFADLI-ANLRKKEISKILGssylrgmNMASFFIANKVILFVTFTSYVLLGNEI 303
Cdd:COG2274 337 LVETLRGIETIKALGaesrfrrrWENLLAKYLnARFKLRRLSNLLS-------TLSGLLQQLATVALLWLGAYLVIDGQL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 304 TASHVFVAMTLYGAVRLTVTLFFpSAIERGSEAIVSIRRIKNFLLL--DELPQRKAHVPSDGKAIVHVQDFTaFWDKALD 381
Cdd:COG2274 410 TLGQLIAFNILSGRFLAPVAQLI-GLLQRFQDAKIALERLDDILDLppEREEGRSKLSLPRLKGDIELENVS-FRYPGDS 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 382 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRS 448
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 527
Cdd:COG2274 568 NITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 528 KHLFQLcICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKEN 592
Cdd:COG2274 648 AIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
710-1211 |
4.30e-55 |
|
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: 202.64 E-value: 4.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 710 GNITETLDLSWYLGiyAGLTAVTVLFGIARSLLVFYILVNASQTLHN---RMFESILKAPVLFFDRNPIGRILNRFSKDI 786
Cdd:TIGR02203 44 GFGGRDRSVLWWVP--LVVIGLAVLRGICSFVSTYLLSWVSNKVVRDirvRMFEKLLGLPVSFFDRQPTGTLLSRITFDS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 787 GHMDDLLpltfLDFIQTLLLVVSVIAVAAAVIPWI-----LIPLVPLSVVFLVLRRY---FLETSRDVKRLESTTRSPVf 858
Cdd:TIGR02203 122 EQVASAA----TDAFIVLVRETLTVIGLFIVLLYYswqltLIVVVMLPVLSILMRRVskrLRRISKEIQNSMGQVTTVA- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 859 shlSSSLQGLWTIRAYKAEERCQELFDAHQDlhseawflfltTSRWFAVRLDAICAI------FVIVVAFGSLVLAKTLN 932
Cdd:TIGR02203 197 ---EETLQGYRVVKLFGGQAYETRRFDAVSN-----------RNRRLAMKMTSAGSIsspitqLIASLALAVVLFIALFQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 933 AG----QVGLALSYALTLMGMFQwSVRQSAEVENMM----ISVERVIEYTDLEKEApwECKKRPPPgwPHEGVIVFDNVN 1004
Cdd:TIGR02203 263 AQagslTAGDFTAFITAMIALIR-PLKSLTNVNAPMqrglAAAESLFTLLDSPPEK--DTGTRAIE--RARGDVEFRNVT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1005 FTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVL 1083
Cdd:TIGR02203 338 FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDVVL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1084 FTGTMRKNL---DPfNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEA 1160
Cdd:TIGR02203 418 FNDTIANNIaygRT-EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1161 TANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1211
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
53-343 |
1.78e-54 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 192.84 E-value: 1.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 53 GIFTLIEEGTRVVQPLFLGKIIEYFEK--YDPDDSVALHTAY----------GY--AAVLSMCTLILAILHHLYFYHVQC 118
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEEntYSSSNSTDKLSVSyvtveeffsnGYvlAVILFLALLLQATFSQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 119 AGMRLRVAMCHMIYRKALRLS--NSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLA 196
Cdd:cd18591 83 EGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 197 GLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGM 276
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 277 NMASFFIANKVILFVTFTSYVLLGNE-ITASHVFVAMTLYGavRLTVTLF-FPSAIERGSEAIVSIRRI 343
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFN--QLTVPLFiFPVVIPILINAVVSTRRL 309
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
722-1243 |
1.16e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 195.71 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 722 LGIYAGLTAVTVLFGI-------ARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLlp 794
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLlaaglhyAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDL-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 795 ltFLDFIQTLLLVVS---VIAVAAAVIPW--ILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTrSPVFSHLSSSLQGLW 869
Cdd:PRK10790 139 --YVTVVATVLRSAAligAMLVAMFSLDWrmALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYL-ADINDGFNEVINGMS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 870 TIRAYKAEERCQELFDAHQDLHSEAwflflttsRWFAVRLDA-----ICAIFVIVVAFGSLVLAKTLNAGQVGLALSYA- 943
Cdd:PRK10790 216 VIQQFRQQARFGERMGEASRSHYMA--------RMQTLRLDGfllrpLLSLFSALILCGLLMLFGFSASGTIEVGVLYAf 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 944 LTLMGMF---------QWSVRQSAEVenmmiSVERVIEYTDLEKEaPWECKKRPPPGwpheGVIVFDNVNFTYsLDGPLV 1014
Cdd:PRK10790 288 ISYLGRLneplielttQQSMLQQAVV-----AGERVFELMDGPRQ-QYGNDDRPLQS----GRIDIDNVSFAY-RDDNLV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1015 LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLD 1093
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLtEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1094 PFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQ 1173
Cdd:PRK10790 437 LGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1174 QKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNpESLFYKM--VQQLGKGEAAALTE 1243
Cdd:PRK10790 517 QALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMyqLQLAGEELAASVRE 587
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
998-1232 |
1.18e-52 |
|
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: 184.67 E-value: 1.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTY-SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS 1075
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPtSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEPVLFTGTMRKNL---DpfNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNN 1152
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygK--PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1153 RILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvLLQNPEsLFYKM 1229
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEqgtHDE---LMAQKG-VYAKL 234
|
...
gi 255683324 1230 VQQ 1232
Cdd:cd03249 235 VKA 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
720-1230 |
9.23e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 195.33 E-value: 9.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 720 WYLGIYAGLTAVTVLFGIArSLLVFYILVNASqtLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLD 799
Cdd:TIGR00958 205 FFMCLLSIASSVSAGLRGG-SFNYTMARINLR--IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 800 FIQTLLLVVSVIAVAAAVIPWI-LIPLVPLSVVFLVLRRY---FLETSRDVKrlESTTRSPVFSHlsSSLQGLWTIRAYK 875
Cdd:TIGR00958 282 LLRNLVMLLGLLGFMLWLSPRLtMVTLINLPLVFLAEKVFgkrYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 876 AEE-RCQELFDAHQDLHSEAW------FLFLTTSRWFAVrldaicAIFVIVVAFGS-LVLAKTLNAGQVglaLSYALTLM 947
Cdd:TIGR00958 358 AEEgEASRFKEALEETLQLNKrkalayAGYLWTTSVLGM------LIQVLVLYYGGqLVLTGKVSSGNL---VSFLLYQE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 948 GMFQwSVRQSAEVEN-MMISV---ERVIEYTDLEKEAPWECKKRPPPgwpHEGVIVFDNVNFTYSL--DGPlVLKHLTAL 1021
Cdd:TIGR00958 429 QLGE-AVRVLSYVYSgMMQAVgasEKVFEYLDRKPNIPLTGTLAPLN---LEGLIEFQDVSFSYPNrpDVP-VLKGLTFT 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLD-PFNEHT 1099
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPtGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTP 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1100 DEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKirEK 1179
Cdd:TIGR00958 584 DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RS 661
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1180 FAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPeSLFYKMV 1230
Cdd:TIGR00958 662 RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
369-566 |
3.08e-50 |
|
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: 177.14 E-value: 3.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 369 VQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV-----------------SVHGR 431
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 432 IAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDAD 511
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 512 IYLLDDPLSAVDAEVGKHLFQLCICQALHE--KITILVTHQLQYLKAASHILILKDG 566
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
911-1211 |
1.84e-48 |
|
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: 183.48 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 911 AICAIFVIVVAfGSLVLAKTLNAGQVGLALSYALTL------MGMFQWSVRQS-AEVENMMISVERVIEYTDlekeapwe 983
Cdd:COG5265 274 ALGLTAMMLMA-AQGVVAGTMTVGDFVLVNAYLIQLyiplnfLGFVYREIRQAlADMERMFDLLDQPPEVAD-------- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 984 cKKRPPPGWPHEGVIVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILT 1062
Cdd:COG5265 345 -APDAPPLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVtSGRILIDGQDI 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1063 TEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQR 1139
Cdd:COG5265 423 RDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEK 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1140 QLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1211
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
996-1209 |
3.55e-47 |
|
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: 168.54 E-value: 3.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 1074
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPtSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTGTMRKNLDPFN-EHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNR 1153
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 1154 ILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1209
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
998-1231 |
3.48e-46 |
|
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: 166.12 E-value: 3.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSI 1076
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEnGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTGTMRKNLDPFNEHTDEElwRALEEVQLKEA---IEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNR 1153
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1154 ILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvlLQNPESLFYKMV 1230
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEqgsHDE----LLAENGLYAYLY 234
|
.
gi 255683324 1231 Q 1231
Cdd:cd03252 235 Q 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
670-1204 |
1.76e-44 |
|
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: 169.77 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 670 FIIFLVLLNMVGQVFYVLQDWWLShwankqGALNNTRNANGNITEtldLSWYLGIYAGLTAVTVLFGIARSLLVFYILVN 749
Cdd:TIGR02857 4 ALALLALLGVLGALLIIAQAWLLA------RVVDGLISAGEPLAE---LLPALGALALVLLLRALLGWLQERAAARAAAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 750 ASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDD-------------LLPLTFL------DFIQTLLLVvsv 810
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGyfarylpqlvlavIVPLAILaavfpqDWISGLILL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 811 iavaaavipwILIPLVPlsvVFLVLRRYFLEtSRDVKRLESTTRspVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDL 890
Cdd:TIGR02857 152 ----------LTAPLIP---IFMILIGWAAQ-AAARKQWAALSR--LSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 891 HSEAWFLFLTTSRWFAVRLDAICAIFVIVVAfgsLVLAKTLNAGQVGLALS-YALTLMGMFQWSVRQ-------SAEVEN 962
Cdd:TIGR02857 216 YRERTMRVLRIAFLSSAVLELFATLSVALVA---VYIGFRLLAGDLDLATGlFVLLLAPEFYLPLRQlgaqyhaRADGVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 963 MMISVERVIEytdlekEAPWECKKRPPPGWPHEGVIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLI 1042
Cdd:TIGR02857 293 AAEALFAVLD------AAPRPLAGKAPVTAAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1043 SALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWRALEEVQLKEAIED 1118
Cdd:TIGR02857 366 NLLLGFVDPtEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP--DASDAEIREALERAGLDEFVAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1119 LPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDS 1198
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
....*.
gi 255683324 1199 DKIMVL 1204
Cdd:TIGR02857 524 DRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
825-1214 |
4.54e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 170.14 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 825 LVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAY-KAEERCQELFDAHQDLHSeAWFLFLTtsr 903
Cdd:PRK13657 162 LVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnRIEAETQALRDIADNLLA-AQMPVLS--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 904 WFAV-----RLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQwsvRQSAEVENMMISVERVIEYTDLEK 978
Cdd:PRK13657 238 WWALasvlnRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLD---QVVAFINQVFMAAPKLEEFFEVED 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 979 EAPwecKKRPPPGWPH----EGVIVFDNVNFTYSLDGPLVlKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-G 1053
Cdd:PRK13657 315 AVP---DVRDPPGAIDlgrvKGAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQsG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1054 KIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEH-TDEELWRALEEVQLKEAIEDLPGKMDTELAESGS 1132
Cdd:PRK13657 391 RILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGR 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1133 NFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE- 1211
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEs 550
|
....*
gi 255683324 1212 --YDE 1214
Cdd:PRK13657 551 gsFDE 555
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
233-1206 |
4.64e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 172.14 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 233 MNEVITGMRIIKMYAWEKSFadlianLRKKEISKILGSSYLRGMN-MASFFIA--NKVILfVTFTSYVLLGNEI---TAS 306
Cdd:PTZ00265 239 IEEALVGIRTVVSYCGEKTI------LKKFNLSEKLYSKYILKANfMESLHIGmiNGFIL-ASYAFGFWYGTRIiisDLS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 307 HVFVAMTLYGAVRLTV-----------TLFFPSAIE--RGSEAIVSIRRIKNfllldelpqRKAHVPS--DGKAI----- 366
Cdd:PTZ00265 312 NQQPNNDFHGGSVISIllgvlismfmlTIILPNITEymKSLEATNSLYEIIN---------RKPLVENndDGKKLkdikk 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH--------------GRI 432
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrSKI 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 433 AYVSQQPWVFSGTVRSNI---LFGKK---YEKERYEK--------------VIKACA-----------------LKKDLQ 475
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIkysLYSLKdleALSNYYNEdgndsqenknkrnsCRAKCAgdlndmsnttdsnelieMRKNYQ 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 476 LLEDGDL---------------------TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGKHLFQLC 534
Cdd:PTZ00265 543 TIKDSEVvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 535 I--CQALHEKITILVTHQLQYLKAASHILILKDGEmvqKGTYTEFLKSGVDFGSLLKKENEEAEPSTAPGTPTLRKRTFS 612
Cdd:PTZ00265 622 InnLKGNENRITIIIAHRLSTIRYANTIFVLSNRE---RGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKIN 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 613 EA----------------------------SIWSQQSS----------RPSLKDGAPEGQDAE--NTQAVQPEESRS--- 649
Cdd:PTZ00265 699 NAgsyiieqgthdalmknkngiyytminnqKVSSKKSSnndndkdsdmKSSAYKDSERGYDPDemNGNSKHENESASnkk 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 650 --------------EGRIGF---------KA-------YKNYFSAGASwFFIIFLVLLNMVG--QVFYVLqdwwlshWAN 697
Cdd:PTZ00265 779 sckmsdenasennaGGKLPFlrnlfkrkpKApnnlrivYREIFSYKKD-VTIIALSILVAGGlyPVFALL-------YAK 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 698 KQGALNNTRNANGNitetldlSWYLGIYAGLTAVTVLfgIARSLLVFY---ILVNASQTLHNRMFESILKAPVLFFDR-- 772
Cdd:PTZ00265 851 YVSTLFDFANLEAN-------SNKYSLYILVIAIAMF--ISETLKNYYnnvIGEKVEKTMKRRLFENILYQEISFFDQdk 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 773 NPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPwiLIPLVPLSVVFLVLR----RYFLETSRDVKR 848
Cdd:PTZ00265 922 HAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCP--IVAAVLTGTYFIFMRvfaiRARLTANKDVEK 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 849 LESTTRSPVFSH-------------LSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAW-FLFLTTSRWFAVRLDAICA 914
Cdd:PTZ00265 1000 KEINQPGTVFAYnsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQkRKTLVNSMLWGFSQSAQLF 1079
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 915 IFVIVVAFGSLVLAK-TLNAGQVGLAL-------SYALTLMGMfqwsvrqSAEVENMMISVERVieYTDLEKEAPWECKK 986
Cdd:PTZ00265 1080 INSFAYWFGSFLIRRgTILVDDFMKSLftflftgSYAGKLMSL-------KGDSENAKLSFEKY--YPLIIRKSNIDVRD 1150
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 987 ----RPPPGWPHEGVIVFDNVNFTY-SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFR-------------- 1047
Cdd:PTZ00265 1151 nggiRIKNKNDIKGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkn 1230
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1048 -----------------------------------------LSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTG 1086
Cdd:PTZ00265 1231 ehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNM 1310
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1087 TMRKNLDPFNEH-TDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVD 1165
Cdd:PTZ00265 1311 SIYENIKFGKEDaTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 255683324 1166 PRTDELIQQK---IREKfAQCTVLTIAHRLNTIIDSDKIMVLDS 1206
Cdd:PTZ00265 1391 SNSEKLIEKTivdIKDK-ADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
383-581 |
2.38e-41 |
|
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: 151.99 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASG-------------LVSVHGRIAYVSQQPWVFSGTVRSN 449
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdisRKSLRSMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGKKYEKEryEKVIKACALKKDLQL---LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:cd03254 97 IRLGRPNATD--EEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 527 GKhLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:cd03254 175 EK-LIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
122-551 |
3.13e-41 |
|
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: 160.22 E-value: 3.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 122 RLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVL----LWVEIGISCLAG 197
Cdd:TIGR02868 87 ALRVRV----YERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAaiavLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 198 LAVLVILLPLqscigklFSSLRSKTAAFTDARIRtmnevitGMRIIKMYAWEKSFADLIANLRKKEI---SKILGSSYLR 274
Cdd:TIGR02868 163 LLLAGFVAPL-------VSLRAARAAEQALARLR-------GELAAQLTDALDGAAELVASGALPAAlaqVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 275 GMNMASFFIA-----NKVILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLF-----FPSAIERGSEAIVSIRRIk 344
Cdd:TIGR02868 229 AERRAAAATAlgaalTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeafaaLPAAAQQLTRVRAAAERI- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 345 NFLLLDELPQRKAHVPSDG-----KAIVHVQDFTAFWDKalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGEL 419
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGavglgKPTLELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 420 PPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVI 485
Cdd:TIGR02868 386 DPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 486 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQL 551
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
720-1233 |
3.78e-41 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 162.82 E-value: 3.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 720 WYLGIYAGLTAVT-VLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFS--KDIGHM------D 790
Cdd:TIGR03797 176 VQIALALLAAAVGaAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMgiSQIRRIlsgstlT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 791 DLLPLTFLDFIQTLLLVVSVIAVAAAvipwILIPLVpLSVVFLVLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWT 870
Cdd:TIGR03797 256 TLLSGIFALLNLGLMFYYSWKLALVA----VALALV-AIAVTLVLGLLQVRKERRLLELSGK----ISGLTVQLINGISK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 871 IRAYKAEERCqelFDAHQDLHSEAWFLFLTTSRW--FAVRLDAICAIFVIVVAF---GSLVLAKTLNAGQVgLALSYALt 945
Cdd:TIGR03797 327 LRVAGAENRA---FARWAKLFSRQRKLELSAQRIenLLTVFNAVLPVLTSAALFaaaISLLGGAGLSLGSF-LAFNTAF- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 946 lmGMFQWSVRQSAeveNMMISVERVI---EYTDLEKEAPWECK-KRPPPGwPHEGVIVFDNVNFTYSLDGPLVLKHLTAL 1021
Cdd:TIGR03797 402 --GSFSGAVTQLS---NTLISILAVIplwERAKPILEALPEVDeAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTD 1100
Cdd:TIGR03797 476 IEPGEFVAIVGPSGSGKSTLLRLLLGFETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1101 EELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIrEKF 1180
Cdd:TIGR03797 556 DEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL-ERL 634
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1181 aQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvlLQNPESLFYKMVQ-QL 1233
Cdd:TIGR03797 635 -KVTRIVIAHRLSTIRNADRIYVLDAGRVVQqgtYDE----LMAREGLFAQLARrQL 686
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
723-1192 |
2.09e-40 |
|
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: 157.91 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 723 GIYAGLTAVTV-LFGIARSL------LVFYILVNASQT-LHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLP 794
Cdd:TIGR02868 49 VLYLSVAAVAVrAFGIGRAVfrylerLVGHDAALRSLGaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 795 LTFLDFIQTLLLVVSVIAVAAA-VIPWILIPLVPLSVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRA 873
Cdd:TIGR02868 129 RVIVPAGVALVVGAAAVAAIAVlSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 874 YKAEERCQ-ELFDAHQDLH----SEAWFLFLTTS-RWFAVRLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALS-----Y 942
Cdd:TIGR02868 209 SGALPAALaQVEEADRELTraerRAAAATALGAAlTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAafeafA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 943 ALTLMGMFQWSVRQSAEvenmmisveRVIEYTDLEKEAPWECKKRPPPGWPHEGVIVFDNVNFTYSlDGPLVLKHLTALI 1022
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAE---------RIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1023 KSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFN-EHTD 1100
Cdd:TIGR02868 359 PPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1101 EELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKF 1180
Cdd:TIGR02868 439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
490
....*....|..
gi 255683324 1181 AQCTVLTIAHRL 1192
Cdd:TIGR02868 519 SGRTVVLITHHL 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
383-567 |
4.24e-40 |
|
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: 146.37 E-value: 4.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSN 449
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 IlfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 529
Cdd:cd03228 96 I-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 255683324 530 LFQLcICQALHEKITILVTHQLQYLKAASHILILKDGE 567
Cdd:cd03228 135 ILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
671-948 |
5.07e-40 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 149.72 E-value: 5.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 671 IIFLVLLNMVGQVFYVLQDWWLSHWANKqgalnntrNANGNITETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNA 750
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDV--------LLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 751 SQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSV 830
Cdd:pfam00664 73 SRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 831 VFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLD 910
Cdd:pfam00664 153 LYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 255683324 911 AICAIFVIVVAF--GSLVLAKTLNAGQVGLALSYALTLMG 948
Cdd:pfam00664 233 FIGYLSYALALWfgAYLVISGELSVGDLVAFLSLFAQLFG 272
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
382-563 |
6.50e-39 |
|
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: 153.21 E-value: 6.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 382 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRS 448
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGKKYEKE-RYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 527
Cdd:TIGR02857 415 NIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 255683324 528 KHLFQ--LCICQAlheKITILVTHQLQYLKAASHILIL 563
Cdd:TIGR02857 495 AEVLEalRALAQG---RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1007-1232 |
6.64e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.23 E-value: 6.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1007 YSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTG 1086
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1087 TMRKNLDPFNEH-TDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVD 1165
Cdd:PRK11174 438 TLRDNVLLGNPDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1166 PRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE---YDEpyvlLQNPESLFYKMVQQ 1232
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-594 |
7.08e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.23 E-value: 7.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 343 IKNFLLLDELPQRKAHVPSDGKAIVHV--QDFTAFwdkALDSPTLQG-LSFIARPGELLAVVGPVGAGKSSLLSAVLGEL 419
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASNDPVTIeaEDLEIL---SPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 420 PpASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVI 485
Cdd:PRK11174 401 P-YQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPI 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 486 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCICQALHEKITILVTHQLQYLKAASHILILKD 565
Cdd:PRK11174 480 GDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ-ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQD 558
|
250 260
....*....|....*....|....*....
gi 255683324 566 GEMVQKGTYTEFLKSGVDFGSLLKKENEE 594
Cdd:PRK11174 559 GQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
995-1209 |
2.13e-38 |
|
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: 143.38 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 995 EGVIVFDNVNFTY-SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRK 1072
Cdd:cd03248 9 KGIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEPVLFTGTMRKNLD-PFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKN 1151
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1152 NRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1209
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
381-581 |
4.56e-38 |
|
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: 142.68 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVR 447
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGKKYEK-ERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:cd03249 95 ENIRYGKPDATdEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 527 GKhLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:cd03249 175 EK-LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
46-588 |
1.27e-37 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 152.18 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 46 WKsYLILGIFTL-IEEGTRVVQPLFLGKIIEY-FEKYDPDdsvALHTAygyaaVLSMCTLILAilhhlYFYHVQCAGMRL 123
Cdd:TIGR00958 160 WP-WLISAFVFLtLSSLGEMFIPFYTGRVIDTlGGDKGPP---ALASA-----IFFMCLLSIA-----SSVSAGLRGGSF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 124 RVAMCHM-------IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKF-DQVTIFLH-FLWAGPLQAIAVTVLLWVEIGISC 194
Cdd:TIGR00958 226 NYTMARInlriredLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsRSLSLNVNvLLRNLVMLLGLLGFMLWLSPRLTM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 195 LAGLAV-LVILLPlqSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS----FADLIANL----RKKEIS 265
Cdd:TIGR00958 306 VTLINLpLVFLAE--KVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKRKALA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 266 KILGSSYLRGMNMASFF----------IANKVI--LFVTFtsyvLLGNEITASHVFVAMTLYGAVRltvtlffpsaierg 333
Cdd:TIGR00958 384 YAGYLWTTSVLGMLIQVlvlyyggqlvLTGKVSsgNLVSF----LLYQEQLGEAVRVLSYVYSGMM-------------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 334 sEAIVSIRRIknFLLLD---ELPQRKAHVPSDGKAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSS 410
Cdd:TIGR00958 446 -QAVGASEKV--FEYLDrkpNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 411 LLSAVLGELPPASGLV-------------SVHGRIAYVSQQPWVFSGTVRSNILFG-KKYEKERYEKVIKACALKKDLQL 476
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVlldgvplvqydhhYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIME 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 477 LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgKHLFQLCICQAlhEKITILVTHQLQYLKA 556
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQLLQESRSRA--SRTVLLIAHRLSTVER 679
|
570 580 590
....*....|....*....|....*....|..
gi 255683324 557 ASHILILKDGEMVQKGTYTEFLKSGVDFGSLL 588
Cdd:TIGR00958 680 ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
381-581 |
1.91e-37 |
|
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: 140.83 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVR 447
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGKKYE-KERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 526
Cdd:cd03251 94 ENIAYGRPGAtREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 527 GKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:cd03251 173 SERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
966-1233 |
3.35e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 148.82 E-value: 3.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 966 SVERVIEYTDLEKEAPWECKKRPPPGwphEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISAL 1045
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1046 FRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWRALEEVQLKEAIEDLPG 1121
Cdd:PRK11160 387 TRAWDPQqGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDDKG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1122 kMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKI 1201
Cdd:PRK11160 465 -LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260 270
....*....|....*....|....*....|..
gi 255683324 1202 MVLDSGRLKEYDEPYVLLQNpESLFYKMVQQL 1233
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
92-343 |
4.64e-37 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 141.58 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 92 YGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHF 171
Cdd:cd18559 38 QVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 172 LWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS 251
Cdd:cd18559 118 MWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 252 FADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTSYVLLG--NEITASHVFVAMTLYGAVRLTVTLfFPSA 329
Cdd:cd18559 198 FIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslAGLVALKVFYSLALTTYLNWPLNM-SPEV 276
|
250
....*....|....
gi 255683324 330 IERGSEAIVSIRRI 343
Cdd:cd18559 277 ITNIVAAEVSLERS 290
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
381-581 |
8.19e-37 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 147.92 E-value: 8.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVR 447
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGKKYEKEryEKVIKACALKKD---LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:TIGR02204 432 ENIRYGRPDATD--EEVEAAARAAHAhefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 525 EvGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
360-568 |
8.10e-36 |
|
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: 136.06 E-value: 8.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 360 PSDGKAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV----------- 428
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqyehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 429 --HGRIAYVSQQPWVFSGTVRSNILFG---KKYEKeryekvIKACALKKD----LQLLEDGDLTVIGDRGATLSGGQKAR 499
Cdd:cd03248 85 ylHSKVSLVGQEPVLFARSLQDNIAYGlqsCSFEC------VKEAAQKAHahsfISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 500 VNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQAL---HEKITILV-THQLQYLKAASHILILKDGEM 568
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAES-----EQQVQQALydwPERRTVLViAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
383-572 |
1.02e-35 |
|
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: 135.41 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSN 449
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 528
Cdd:cd03245 98 ITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255683324 529 HLFQlCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKG 572
Cdd:cd03245 178 RLKE-RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
330-574 |
1.21e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.08 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 330 IERGSEAIVSIRRiknflLLDELPqrkahVPSDGKAIVHVQ------DFTAFWDKALDSPTLQGLSFIARPGELLAVVGP 403
Cdd:PRK10789 280 VERGSAAYSRIRA-----MLAEAP-----VVKDGSEPVPEGrgeldvNIRQFTYPQTDHPALENVNFTLKPGQMLGICGP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 404 VGAGKSSLLSAVLGELPPASGLVSVH-------------GRIAYVSQQPWVFSGTVRSNILFGK-KYEKERYEKVIKACA 469
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLAS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 470 LKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCICQALHEKITILVTH 549
Cdd:PRK10789 430 VHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH-NLRQWGEGRTVIISAH 508
|
250 260
....*....|....*....|....*
gi 255683324 550 QLQYLKAASHILILKDGEMVQKGTY 574
Cdd:PRK10789 509 RLSALTEASEILVMQHGHIAQRGNH 533
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
334-580 |
2.40e-35 |
|
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: 142.96 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 334 SEAIVSIRRIKNflLLDELPQRKAHVPS-DGKAIVHVQDFTAFwDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLL 412
Cdd:COG4618 299 VSARQAYRRLNE--LLAAVPAEPERMPLpRPKGRLSVENLTVV-PPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 413 SAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSNI-LFGKkyekERYEKVIKACALK--KDLQL 476
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIAENIaRFGD----ADPEKVVAAAKLAgvHEMIL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 477 -LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCIcQALHE--KITILVTHQLQY 553
Cdd:COG4618 452 rLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA-AI-RALKArgATVVVITHRPSL 529
|
250 260
....*....|....*....|....*..
gi 255683324 554 LKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:COG4618 530 LAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
753-1219 |
4.52e-35 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 142.47 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 753 TLHNRMFESILKAPVLFFDRNPIGRILNRFSKD----------------------IGhmddLLPLTFLDFIQTLLlvvsv 810
Cdd:PRK11176 99 TMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalitvvregasiIG----LFIMMFYYSWQLSL----- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 811 iavaaavipwILIPLVPL-SVVFLVLRRYFLETSRDVKrlesTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQD 889
Cdd:PRK11176 170 ----------ILIVIAPIvSIAIRVVSKRFRNISKNMQ----NTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 890 LHSEAWFLFLTTSRWF--AVRLDAICAIFVIVVAFGSLVLAKTLNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISV 967
Cdd:PRK11176 236 RMRQQGMKMVSASSISdpIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAAC 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 968 ERVIEYTDLEKEAPwECKKRPPPGwphEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFR 1047
Cdd:PRK11176 316 QTLFAILDLEQEKD-EGKRVIERA---KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1048 LSE-PEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLD-PFNEH-TDEELWRALEEVQLKEAIEDLPGKMD 1124
Cdd:PRK11176 392 FYDiDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyARTEQySREQIEEAARMAYAMDFINKMDNGLD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1125 TELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVL 1204
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551
|
490
....*....|....*
gi 255683324 1205 DSGRLKEYDEPYVLL 1219
Cdd:PRK11176 552 EDGEIVERGTHAELL 566
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
383-564 |
6.19e-35 |
|
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: 133.04 E-value: 6.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------RIAYVSQQ---PWVFSGTVR---- 447
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRrsiDRDFPISVRdvvl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 ----SNILFGKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 522
Cdd:cd03235 93 mglyGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255683324 523 DAEVGKHLFQLciCQALHEK-ITIL-VTHQL-QYLKAASHILILK 564
Cdd:cd03235 164 DPKTQEDIYEL--LRELRREgMTILvVTHDLgLVLEYFDRVLLLN 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
365-580 |
7.57e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 7.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 365 AIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------RIAYVS 436
Cdd:COG1121 5 PAIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 437 QQ---PWVFSGTVR--------SNILFGKKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLAR 504
Cdd:COG1121 82 QRaevDWDFPITVRdvvlmgryGRRGLFRRPSRADREAVDEA---------LERVGLEDLADRPiGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 505 AVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITIL-VTHQLQYL-KAASHILILkDGEMVQKGTYTEFLKS 580
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILvVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
383-591 |
2.21e-32 |
|
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: 126.58 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSN 449
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 528
Cdd:cd03253 95 IRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 529 HLFQlCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKE 591
Cdd:cd03253 175 EIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
385-573 |
7.93e-32 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 125.16 E-value: 7.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWV-FSGTVRSNI 450
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFG--------KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 521
Cdd:COG1120 97 ALGryphlglfGRPSAEDREAVEEA---------LERTGLEHLADRPvDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 522 VD----AEVGKHLFQLCicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 573
Cdd:COG1120 168 LDlahqLEVLELLRRLA---RERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1000-1162 |
1.58e-31 |
|
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: 120.83 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1000 FDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIP 1078
Cdd:pfam00005 1 LKNVSLT---------------LNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTDDERKSLRKEIGYVF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1079 QEPVLFTG-TMRKNL-------DPFNEHTDEELWRALEEVqlkeaieDLPGKMDTELAESGSNFSVGQRQLVCLARAILK 1150
Cdd:pfam00005 66 QDPQLFPRlTVRENLrlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLT 138
|
170
....*....|..
gi 255683324 1151 NNRILIIDEATA 1162
Cdd:pfam00005 139 KPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
367-573 |
1.99e-31 |
|
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: 122.99 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKALDsPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIA 433
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 434 YVSQQPWVFSGTVRSNI-LFGKKYEKERYEkVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADI 512
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 513 YLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGT 573
Cdd:cd03244 161 LVLDEATASVDPETDALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
385-593 |
2.06e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 123.64 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNIL 451
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 F-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 525 EVGKHLFQLcICQALHEKITILV-THQLQYL-KAASHILILKDGEMVQKGTYTEFLKSGVD--FGSLLKKENE 593
Cdd:COG1131 165 EARRELWEL-LRELAAEGKTVLLsTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLLEdvFLELTGEEAR 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
998-1211 |
3.16e-31 |
|
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: 120.88 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFR-LSEPEGKIWIDKILTTEIGlHDLRKKMSI 1076
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTGTMRKNLdpfnehtdeelwraleevqlkeaiedlpgkmdtelaesGSNFSVGQRQLVCLARAILKNNRILI 1156
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1157 IDEATANVDPRTD----ELIQQKIREKfaqcTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1211
Cdd:cd03247 122 LDEPTVGLDPITErqllSLIFEVLKDK----TLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
50-322 |
3.27e-31 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 124.29 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSVALhtaYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCH 129
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAL---NVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 130 MIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGIS-CLAGLAVLVILLPLQ 208
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 209 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRG-MNMASFFIANKV 287
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGlSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 255683324 288 ILFVTFTSYVL-LGNEITASHVFVAMTLYGAVRLTV 322
Cdd:pfam00664 239 YALALWFGAYLvISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
385-520 |
4.71e-31 |
|
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: 119.67 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TVRSNI 450
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 451 LFGKkyEKERYEKVIKACALKKDLQLLEDGDL--TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLS 520
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
998-1209 |
4.79e-31 |
|
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: 120.40 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1076
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPtSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTGTMRKNLdpfnehtdeelwraleevqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKNNRILI 1156
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255683324 1157 IDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1209
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
998-1208 |
3.36e-30 |
|
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: 119.11 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTY---SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALfrLSE---PEGKIWIdkiltteiglhdlR 1071
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGElekLSGSVSV-------------P 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1072 KKMSIIPQEPVLFTGTMRKNL---DPFNEhtdEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAI 1148
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1149 LKNNRILIIDEATANVDPRT-DELIQQKIREKFAQC-TVLTIAHRLNTIIDSDKIMVLDSGR 1208
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
385-572 |
6.43e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 117.15 E-value: 6.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQqpwvfsgtvrsnil 451
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 fgkkyekeryekvikacalkkdlqLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEV 526
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 527 GKHLFQLCicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQKG 572
Cdd:cd03214 137 LELLRRLA---RERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
998-1225 |
8.26e-30 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 118.59 E-value: 8.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1076
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPV--LFTGTMR-------KNLDpfneHTDEELWR----ALEEVQLkeaiedlpgkmdTELAE------SGsnfsvG 1137
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpENLG----LPREEIRErveeALELVGL------------EHLADrpphelSG-----G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1138 QRQLVCLARAILKNNRILIIDEATANVDPR-TDELIQ--QKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1213
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRgRRELLEllKRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADG 216
|
250
....*....|..
gi 255683324 1214 EPYVLLQNPESL 1225
Cdd:COG1122 217 TPREVFSDYELL 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
381-595 |
1.36e-29 |
|
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: 118.42 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVR 447
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNI-LFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeV 526
Cdd:COG4555 93 ENIrYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-M 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 527 GKHLFQLCICQALHEKITILV-THQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGVD------FGSLLKKENEEA 595
Cdd:COG4555 167 ARRLLREILRALKKEGKTVLFsSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEenledaFVALIGSEEGEA 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
346-604 |
1.37e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.84 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 346 FLLLDELPQRkaHVPSDGKAIVHVQDFTAFWDKALD----SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP 421
Cdd:PRK13657 310 FEVEDAVPDV--RDPPGAIDLGRVKGAVEFDDVSFSydnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 422 ASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGKK--YEKERYEKVIKACALkkDLQLL-EDGDLTVI 485
Cdd:PRK13657 388 QSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAH--DFIERkPDGYDTVV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 486 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLfQLCICQALHEKITILVTHQLQYLKAASHILILKD 565
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255683324 566 GEMVQKGTYTEFLKSGVDFGSLLK-----KENEEAEPSTAPGTP 604
Cdd:PRK13657 545 GRVVESGSFDELVARGGRFAALLRaqgmlQEDERRKQPAAEGAN 588
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1000-1208 |
2.71e-29 |
|
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: 114.65 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1000 FDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIP 1078
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1079 QepvlftgtmrknldpfnehtdeelwraleevqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKNNRILIID 1158
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1159 EATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
383-563 |
4.26e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.41 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQQ---PWVFSGTVRSNI---LFGK 454
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 455 KYEKERY----EKVIKACALKKDLQLLEDGDLtvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 530
Cdd:NF040873 86 RGLWRRLtrddRAAVDDALERVGLADLAGRQL-------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|....
gi 255683324 531 FQLcICQALHEKITIL-VTHQLQYLKAASHILIL 563
Cdd:NF040873 159 IAL-LAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
381-581 |
8.42e-29 |
|
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: 116.05 E-value: 8.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSP-TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTV 446
Cdd:cd03252 13 DGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RSNILFGKkyEKERYEKVIKACALKKD---LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:cd03252 93 RDNIALAD--PGMSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 524 AEvGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:cd03252 171 YE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
367-572 |
9.36e-29 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 115.31 E-value: 9.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKAldsPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYV 435
Cdd:cd03259 1 LELKGLSKTYGSV---RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 436 SQQPWVFSG-TVRSNILFG----KKYEKERYEKVIKAcalkkdLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQDA 510
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrGVPKAEIRARVREL------LELVGLEGL--LNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 511 DIYLLDDPLSAVDAEVGKHLF-QLCICQALHEKITILVTH-QLQYLKAASHILILKDGEMVQKG 572
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELReELKELQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
385-573 |
3.13e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 117.56 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQP------WVFSG-------TVRSNIL 451
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgFVFQHyalfphmTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:COG1118 98 FGlrvrPPSKAEIRARV---------EELLELVQLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 527 GKHLFQLCIcqALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGT 573
Cdd:COG1118 169 RKELRRWLR--RLHDELggtTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
385-563 |
4.31e-28 |
|
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: 113.34 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------IAYVSQQ----PWVfsgTVRSNILF 452
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQdallPWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 453 G----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--- 524
Cdd:cd03293 97 GlelqGVPKAEARERA---------EELLELVGLSGFENAyPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltr 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255683324 525 -EVGKHLFQLCicqALHEKITILVTHQLQ---YLkaASHILIL 563
Cdd:cd03293 168 eQLQEELLDIW---RETGKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
999-1208 |
8.33e-28 |
|
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: 112.18 E-value: 8.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 999 VFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSII 1077
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1078 PQEP--VLFTGTMRKNL--DPFNEHTDEE-----LWRALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLVCLARAI 1148
Cdd:cd03225 81 FQNPddQFFGPTVEEEVafGLENLGLPEEeieerVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1149 LKNNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
383-568 |
1.01e-27 |
|
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: 110.77 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSN 449
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelgdHVGYLPQDDELFSGSIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILfgkkyekeryekvikacalkkdlqlledgdltvigdrgatlSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 529
Cdd:cd03246 96 IL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 255683324 530 LFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEM 568
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
361-566 |
1.23e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 113.26 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 361 SDGKAIVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------R 431
Cdd:COG1116 2 SAAAPALELRGVSkRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 432 IAYVSQQ----PWVfsgTVRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTviGDRGA---TLSGGQKARV 500
Cdd:COG1116 82 RGVVFQEpallPWL---TVLDNVALGlelrGVPKAERRERA---------RELLELVGLA--GFEDAyphQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 501 NLARAVYQDADIYLLDDPLSAVDA----EVGKHLFQLCicqALHEKITILVTHQLQ---YLkaASHILILKDG 566
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDAltreRLQDELLRLW---QETGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
998-1215 |
2.08e-27 |
|
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: 111.89 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYsldGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE------PEGKIWID--KILTTEIGLH 1068
Cdd:cd03260 1 IELRDLNVYY---GDKhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapDEGEVLLDgkDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1069 DLRKKMSIIPQEPVLFTGTMRKNLD----PFNEHTDEELwRALEEVQLKEAieDLPGKMDTELAESGsnFSVGQRQLVCL 1144
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEEL-DERVEEALRKA--ALWDEVKDRLHALG--LSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1215
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPT 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
988-1212 |
3.50e-27 |
|
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: 117.93 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 988 PPPgwphEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKIlttEIG 1066
Cdd:COG4618 325 PRP----KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPtAGSVRLDGA---DLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1067 LHDLRKKMSII---PQEPVLFTGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVC 1143
Cdd:COG4618 398 QWDREELGRHIgylPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1144 LARAILKNNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEY 1212
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
385-568 |
3.79e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.29 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNIL 451
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FGKKYEKERYEKViKACALKKDLQLledgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----VG 527
Cdd:COG4619 96 FPFQLRERKFDRE-RALELLERLGL----PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEntrrVE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255683324 528 KHLFQLCicqaLHEKITIL-VTH-QLQYLKAASHILILKDGEM 568
Cdd:COG4619 171 ELLREYL----AEEGRAVLwVSHdPEQIERVADRVLTLEAGRL 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
993-1222 |
1.02e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 116.74 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 993 PHE-GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE-PEGKIWIDKILTTEIGLHDL 1070
Cdd:PRK10789 308 PEGrGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEPVLFTGTMRKNL---DPfnEHTDEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARA 1147
Cdd:PRK10789 388 RSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1148 ILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNP 1222
Cdd:PRK10789 466 LLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
381-572 |
1.44e-26 |
|
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: 107.78 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSGTVRS 448
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NIlfgkkyekeryekvikacalkkdlqlledgdltvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 528
Cdd:cd03247 94 NL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255683324 529 HLFQLcICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKG 572
Cdd:cd03247 136 QLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
369-567 |
2.46e-26 |
|
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: 107.94 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 369 VQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYV 435
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 436 SQQP--WVFSGTVRSNILFGKKYEKERYEKVIkacalKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADI 512
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIE-----ERVEEALELVGLEGLRDRSpFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 513 YLLDDPLSAVDAEVGKHLFQLcICQALHEKITIL-VTHQLQYLKA-ASHILILKDGE 567
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLEL-LKKLKAEGKTIIiVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
997-1212 |
3.84e-26 |
|
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: 107.98 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDL 1070
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtSGSIIFDgKDLLKlsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEPVL-FTGTMR--KNL-DPFNEHT----DEELWRA----LEEVQLKEAIED-LPGKmdtelaesgsnFSVG 1137
Cdd:cd03257 81 RKEIQMVFQDPMSsLNPRMTigEQIaEPLRIHGklskKEARKEAvlllLVGVGLPEEVLNrYPHE-----------LSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1138 QRQLVCLARAILKNNRILIIDEATANVDPRT-DELIQ--QKIREKFaQCTVLTIAHRLNTI-IDSDKIMVLDSGRLKEY 1212
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
383-576 |
4.24e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.32 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVF-SGTVRSNI 450
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYpHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFG----KKYEKERYEKVIKACALkkdLQLLEdgdltvIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 525
Cdd:COG3839 97 AFPlklrKVPKAEIDRRVREAAEL---LGLED------LLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 526 VgKHLFQLCIcQALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 576
Cdd:COG3839 168 L-RVEMRAEI-KRLHRRLgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
997-1225 |
7.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS 1075
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPqSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEP------------VLFtGTMRKNLDPfnehtdEELWRALEEVQLKEAIEDLpgkmdteLAESGSNFSVGQRQLVC 1143
Cdd:PRK13632 87 IIFQNPdnqfigatveddIAF-GLENKKVPP------KKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1144 LARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQN 1221
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
....
gi 255683324 1222 PESL 1225
Cdd:PRK13632 233 KEIL 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
381-576 |
7.69e-26 |
|
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: 107.43 E-value: 7.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRS 448
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGKKyEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 527
Cdd:cd03296 94 NVAFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 528 KHLFQLciCQALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 576
Cdd:cd03296 173 KELRRW--LRRLHDELhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
385-577 |
1.42e-25 |
|
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: 106.88 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQ-PWVFSGTVR 447
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGK---------------KYEKERyekvikACALKKDLQLLEDgdltvIGDRGATLSGGQKARVNLARAVYQDADI 512
Cdd:cd03256 97 ENVLSGRlgrrstwrslfglfpKEEKQR------ALAALERVGLLDK-----AYQRADQLSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 513 YLLDDPLSAVD---AEVGKHLFqLCICQalHEKITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTEF 577
Cdd:cd03256 166 ILADEPVASLDpasSRQVMDLL-KRINR--EEGITVIVSlHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
382-580 |
1.67e-25 |
|
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: 106.62 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 382 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TVR 447
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNI-LFGK--KYEKERYEKVIKacalkkdlQLLEDGDLTVIGDRG---ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 521
Cdd:cd03295 94 ENIaLVPKllKWPKEKIRERAD--------ELLALVGLDPAEFADrypHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 522 VDAEVGKHLFQ--LCICQALHEKItILVTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:cd03295 166 LDPITRDQLQEefKRLQQELGKTI-VFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
385-580 |
1.87e-25 |
|
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: 106.43 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPWVFSG-TVR 447
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGKKYEKERYEKVIKACALKKdLQ---LLEDGDLtvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:cd03261 96 ENVAFPLREHTRLSEEEIREIVLEK-LEavgLRGAEDL-----YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 525 eVGKHLFQLCI--CQALHEKITILVTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:cd03261 170 -IASGVIDDLIrsLKKELGLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
997-1225 |
2.54e-25 |
|
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: 111.92 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL----SEPEGKIWIDKILTTEIGLHDLRK 1072
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphgGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEP------------VLFtGTMRKNLDPfnEHTDEELWRALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQ 1140
Cdd:COG1123 84 RIGMVFQDPmtqlnpvtvgdqIAE-ALENLGLSR--AEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1141 LVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYV 1217
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....*...
gi 255683324 1218 LLQNPESL 1225
Cdd:COG1123 230 ILAAPQAL 237
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
669-973 |
2.79e-25 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 107.30 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 669 FFIIFLVLLNMVgqvFYVLQDWWLSHWANKQGalnntrnaNGNITETLdlsWYLGIYAGLTAVTVLFGIARSLLVFYILV 748
Cdd:cd18559 2 FLLIKLVLCNHV---FSGPSNLWLLLWFDDPV--------NGPQEHGQ---VYLSVLGALAILQGITVFQYSMAVSIGGI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 749 NASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIpLVPL 828
Cdd:cd18559 68 FASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV-GIPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 829 SVVFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDlHSEAWFLFLTTSRWFAVR 908
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVR 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 909 LDAICAIFVIVVAFGSLVLAKTlNAGQVGLALSYALTLMGMFQWSVRQSAEVENMMISVERVIEY 973
Cdd:cd18559 226 LWCVGPCIVLFASFFAYVSRHS-LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1004-1209 |
5.36e-25 |
|
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: 103.28 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQepv 1082
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDGKDLASLSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 lftgtmrknldpfnehtdeelwrALEEVQlkeaIEDLPGKMDTELaeSGsnfsvGQRQLVCLARAILKNNRILIIDEATA 1162
Cdd:cd03214 81 -----------------------ALELLG----LAHLADRPFNEL--SG-----GERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1163 NVDP----RTDELIQQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03214 127 HLDIahqiELLELLRRLARER--GKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
385-562 |
6.24e-25 |
|
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: 103.71 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNIL 451
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FgkkyekeryekvikACALKKD-------LQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:COG4133 98 F--------------WAALYGLradreaiDEALEAVGLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255683324 524 AEvGKHLFQLCICQALHE-KITILVTHQLQYLKAASHILI 562
Cdd:COG4133 164 AA-GVALLAELIAAHLARgGAVLLTTHQPLELAAARVLDL 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
383-578 |
1.30e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.30 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSN 449
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGK-KYEKERYEKVIKACALKKdlqLLEDGD-L-TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:PRK11160 434 LLLAApNASDEALIEVLQQVGLEK---LLEDDKgLnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 527 GKHLFQLCICQALHeKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL 578
Cdd:PRK11160 511 ERQILELLAEHAQN-KTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
381-563 |
1.78e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.56 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP---ASGLVSVHG-----------RIAYVSQQPWVFSG-T 445
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrRIGILFQDDLLFPHlS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 446 VRSNILFG-----KKyeKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:COG4136 93 VGENLAFAlpptiGR--AQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 255683324 520 SAVDAEVGKHLFQLCICQALHEKI-TILVTHQLQYLKAASHILIL 563
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIpALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
385-567 |
2.31e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 101.49 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 448
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----A 524
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDpitrR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255683324 525 EVGKHLFQLcicQALHEKITILVTHQLQYL-KAASHILILKDGE 567
Cdd:cd03229 138 EVRALLKSL---QAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
381-579 |
2.85e-24 |
|
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: 102.80 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPW--VFSGT 445
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 446 VRSNILFGKKY----EKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLS 520
Cdd:COG1122 93 VEEDVAFGPENlglpREEIRERVEEA---------LELVGLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 521 AVDAEVGKHLFQlcICQALHEK-IT-ILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLK 579
Cdd:COG1122 164 GLDPRGRRELLE--LLKRLNKEgKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
364-607 |
5.23e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.68 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 364 KAIVHVQDFTaFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHG---------- 430
Cdd:COG1123 2 TPLLEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 ---RIAYVSQQPWV--FSGTVRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLAR 504
Cdd:COG1123 81 rgrRIGMVFQDPMTqlNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYpHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 505 AVYQDADIYLLDDPLSAVDAEVGKHLFQL-CICQALHEKITILVTHQLQY-LKAASHILILKDGEMVQKGTYTEFLKSGV 582
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLlRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260
....*....|....*....|....*..
gi 255683324 583 DFGSL--LKKENEEAEPSTAPGTPTLR 607
Cdd:COG1123 236 ALAAVprLGAARGRAAPAAAAAEPLLE 262
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
366-576 |
9.02e-24 |
|
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: 101.50 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 366 IVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------- 430
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 --RIAYVSQQPWVFSG-TVRSNILF----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNL 502
Cdd:cd03258 81 rrRIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEERV---------LELLELVGLEDKADAyPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 503 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcicqaLHE-----KITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYT 575
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILAL-----LRDinrelGLTIvLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
.
gi 255683324 576 E 576
Cdd:cd03258 227 E 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
381-567 |
9.35e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 98.86 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQqpwvfsgtvr 447
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiaklpleelrrRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 snilfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 527
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255683324 528 KHLFQLCICQALHEKITILVTHQLQYL-KAASHILILKDGE 567
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
381-573 |
1.17e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.02 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQqpwvfSG----- 444
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ-----DYalfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 -TVRSNILFG----KKYEKERYEKVIKACALkkdLQLledGDLtviGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 518
Cdd:COG3842 92 lTVAENVAFGlrmrGVPKAEIRARVAELLEL---VGL---EGL---ADRYpHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 519 LSAVDAEVGKHLfQLCICQALHE-KIT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 573
Cdd:COG3842 163 LSALDAKLREEM-REELRRLQRElGITfIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
346-582 |
1.26e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.03 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 346 FLLLDeLPQRK---AHVPSDGKAIVHVQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA 422
Cdd:PRK11176 319 FAILD-LEQEKdegKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 423 SG-------------LVSVHGRIAYVSQQPWVFSGTVRSNILF--GKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGD 487
Cdd:PRK11176 397 EGeilldghdlrdytLASLRNQVALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 488 RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQALHE----KITILVTHQLQYLKAASHILIL 563
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES-----ERAIQAALDElqknRTSLVIAHRLSTIEKADEILVV 551
|
250 260
....*....|....*....|
gi 255683324 564 KDGEMVQKGTYTEFL-KSGV 582
Cdd:PRK11176 552 EDGEIVERGTHAELLaQNGV 571
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1004-1217 |
1.60e-23 |
|
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: 100.65 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKI---LTTEIGLHDLRKKMSIIPQ 1079
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEdisGLSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1080 EPVLFTG-TMRKNLD-PFNEHT--DEELWRA-----LEEVQLKEAIEDLPGkmdtELaeSGsnfsvGQRQLVCLARAILK 1150
Cdd:cd03261 85 SGALFDSlTVFENVAfPLREHTrlSEEEIREivlekLEAVGLRGAEDLYPA----EL--SG-----GMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1151 NNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR---------LKEYDEPYV 1217
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKivaegtpeeLRASDDPLV 232
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
380-587 |
2.01e-23 |
|
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: 107.13 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 380 LDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTV 446
Cdd:TIGR01193 485 YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RSNILFGKKyEKERYEKVIKACAL---KKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 524 AEVGKHLFQLCIcqALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSL 587
Cdd:TIGR01193 644 TITEKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
384-569 |
2.63e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 99.25 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 384 TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------IAYVSQQP--WVFSGTVRSNIL 451
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksIGYVMQDVdyQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FGKKYEKERYEKVikACALKK-DLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----V 526
Cdd:cd03226 95 LGLKELDAGNEQA--ETVLKDlDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255683324 527 GKHLFQLcicqALHEKITILVTHQLQYL-KAASHILILKDGEMV 569
Cdd:cd03226 166 GELIREL----AAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
385-580 |
3.18e-23 |
|
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: 99.72 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILF 452
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 453 GKKyeKERYEKVIKAcalKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 531
Cdd:cd03299 95 GLK--KRKVDKKEIE---RKVLEIAEMLGIDHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 532 QLcICQALHE-KITIL-VTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 580
Cdd:cd03299 170 EE-LKKIRKEfGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
46-578 |
5.50e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 105.19 E-value: 5.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 46 WKSYLILGIFTL-IEEGTRVVQPLflgkIIEYFekydPDDSVALHT-----AYGYAAVLSMCTLILAILHH---LYFYH- 115
Cdd:PRK10790 21 WRKPLGLAVLMLwVAAAAEVSGPL----LISYF----IDNMVAKGNlplglVAGLAAAYVGLQLLAAGLHYaqsLLFNRa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 116 ----VQcagmRLRVAmchmIYRKALRLSNSAMGKTTTGQIVNLLSND--VNKFDQVTIFLHFLWAGPL---QAIAVTVLL 186
Cdd:PRK10790 93 avgvVQ----QLRTD----VMDAALRQPLSAFDTQPVGQLISRVTNDteVIRDLYVTVVATVLRSAALigaMLVAMFSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 187 WVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEKSFADlianlRKKEISK 266
Cdd:PRK10790 165 WRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDG----FNEVINGMSVIQQFRQQARFGE-----RMGEASR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 267 ilgSSYLRGMN---MASFFIANkviLFVTFTSYVLLGneitashvfvAMTLYG-----AVRLTVTLFFPSAIERGSE--- 335
Cdd:PRK10790 236 ---SHYMARMQtlrLDGFLLRP---LLSLFSALILCG----------LLMLFGfsasgTIEVGVLYAFISYLGRLNEpli 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 336 -----------AIVSIRRIknFLLLDELPQRKAhvpSDGKAI----VHVQDFTAFWDKalDSPTLQGLSFIARPGELLAV 400
Cdd:PRK10790 300 elttqqsmlqqAVVAGERV--FELMDGPRQQYG---NDDRPLqsgrIDIDNVSFAYRD--DNLVLQNINLSVPSRGFVAL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 401 VGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKA 467
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 468 CALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQAL---HEKIT 544
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAIQQALaavREHTT 527
|
570 580 590
....*....|....*....|....*....|....*
gi 255683324 545 ILV-THQLQYLKAASHILILKDGEMVQKGTYTEFL 578
Cdd:PRK10790 528 LVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
991-1211 |
5.89e-23 |
|
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: 99.49 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 991 GWPHEGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHD 1069
Cdd:COG1124 12 GQGGRRVPVLKDVSLE---------------VAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1070 LRKKMSIIPQEPvlfTGTM--RKNLD-----PFNEH----TDEELWRALEEVQLKEAIED-LPGkmdtELaeSGsnfsvG 1137
Cdd:COG1124 77 FRRRVQMVFQDP---YASLhpRHTVDrilaePLRIHglpdREERIAELLEQVGLPPSFLDrYPH----QL--SG-----G 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1138 QRQLVCLARAILKNNRILIIDEATANVDPRT-DELIQ--QKIREKFaQCTVLTIAHRLNtIID--SDKIMVLDSGRLKE 1211
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVqAEILNllKDLREER-GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVE 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
389-578 |
6.99e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.67 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 389 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGK-- 454
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQENNLFPHlTVAQNIGLGLrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 455 --KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEVG 527
Cdd:COG3840 99 glKLTAEQRAQVEQA---------LERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 528 KHLFQLCicqaLHEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTEFL 578
Cdd:COG3840 170 DLVDELC----RERGLTVLmVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
389-578 |
1.26e-22 |
|
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: 99.26 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 389 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPWVFSG-TVRSNI 450
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFG-------KKYEKERYEKVIKACALKKDLQLLEDgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:cd03294 124 AFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 524 ----AEVGKHLFQLcicQALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFL 578
Cdd:cd03294 193 plirREMQDELLRL---QAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
990-1226 |
3.06e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 990 PGWPHEGViVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTE--IG 1066
Cdd:PRK13637 14 EGTPFEKK-ALDNVNIE---------------IEDGEFVGLIGHTGSGKSTLIQHLNGLLKPtSGKIIIDGVDITDkkVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1067 LHDLRKKMSIIPQEP--VLFTGTMRK-------NLDPFNEHTDEELWRALEEVQLKeaIEDLPGKMDTELaeSGsnfsvG 1137
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyQLFEETIEKdiafgpiNLGLSEEEIENRVKRAMNIVGLD--YEDYKDKSPFEL--SG-----G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1138 QRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLkeyde 1214
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKC----- 223
|
250
....*....|..
gi 255683324 1215 pyVLLQNPESLF 1226
Cdd:PRK13637 224 --ELQGTPREVF 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
997-1214 |
3.29e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.66 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEI---GLHDLRK 1072
Cdd:COG2884 1 MIRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQ-----------EPVLF----TGTMRKNLdpfNEHTDEelwrALEEVQLKEAIEDLPGkmdtELaeSGsnfsvG 1137
Cdd:COG2884 80 RIGVVFQdfrllpdrtvyENVALplrvTGKSRKEI---RRRVRE----VLDLVGLSDKAKALPH----EL--SG-----G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1138 QRQLVCLARAILKNNRILIIDEATANVDPRT-DELIQ--QKIREkfAQCTVLtIA-HRLNtIIDS--DKIMVLDSGRLKE 1211
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETsWEIMEllEEINR--RGTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
...
gi 255683324 1212 YDE 1214
Cdd:COG2884 218 DEA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
383-567 |
3.49e-22 |
|
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: 96.40 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------------IAYVSQQPWVFSG- 444
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLPDl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:cd03255 98 TALENVELPL-----LLAGVPKKERRERAEELLERVGLGdRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 524 AEVGKHLFQLciCQALHEK--ITIL-VTHQLQYLKAASHILILKDGE 567
Cdd:cd03255 173 SETGKEVMEL--LRELNKEagTTIVvVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
998-1209 |
3.54e-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: 94.77 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSI 1076
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTG-TMRKNLDpfnehtdeelwraleevqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKNNRIL 1155
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 1156 IIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
385-573 |
3.82e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.49 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRiAYVSQQPWV---------------FSGTVRSN 449
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGK---KYEKERYEKVIKACALKKDLQLLEDGDLTvigdrgaTLSGGQKARVNLARA---VYQDAD----IYLLDDPL 519
Cdd:COG4559 96 VALGRaphGSSAAQDRQIVREALALVGLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqLWEPVDggprWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 520 SAVDAevgKHlfQLCICQAL----HEKITIL-VTHQL----QYlkaASHILILKDGEMVQKGT 573
Cdd:COG4559 169 SALDL---AH--QHAVLRLArqlaRRGGGVVaVLHDLnlaaQY---ADRILLLHQGRLVAQGT 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
997-1225 |
8.05e-22 |
|
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: 101.13 E-value: 8.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPlvlKHLTAL------IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG--- 1066
Cdd:COG1123 260 LLEVRNLSKRYPVRGK---GGVRAVddvsltLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFDGKDLTKLSrrs 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1067 LHDLRKKMSIIPQ-----------------EPVLFTGTMRKnldpfnEHTDEELWRALEEVQLKEAIED-LPGkmdtELa 1128
Cdd:COG1123 337 LRELRRRVQMVFQdpysslnprmtvgdiiaEPLRLHGLLSR------AERRERVAELLERVGLPPDLADrYPH----EL- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1129 eSGsnfsvGQRQLVCLARAILKNNRILIIDEATANVDPRTD----ELIqQKIREKFaQCTVLTIAHRLNTIID-SDKIMV 1203
Cdd:COG1123 406 -SG-----GQRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLL-RDLQREL-GLTYLFISHDLAVVRYiADRVAV 477
|
250 260
....*....|....*....|..
gi 255683324 1204 LDSGRLKEYDEPYVLLQNPESL 1225
Cdd:COG1123 478 MYDGRIVEDGPTEEVFANPQHP 499
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
993-1191 |
1.02e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.04 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 993 PHEGVIVFDNVNFtYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSePEGkiwidkilTTEIGLHDLRK 1072
Cdd:COG4178 358 SEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW-PYG--------SGRIARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMsIIPQEPVLFTGTMRKNL---DPFNEHTDEELWRALEEVQLkeaiEDLPGKMDTElAESGSNFSVGQRQLVCLARAIL 1149
Cdd:COG4178 428 VL-FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----GHLAERLDEE-ADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 255683324 1150 KNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHR 1191
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
378-572 |
1.03e-21 |
|
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: 95.05 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDSPTLQgLSFIArPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPW 440
Cdd:cd03297 8 KRLPDFTLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 441 VFSG-TVRSNILFGKKYeKERYEKVIKACALkkdLQLLedgDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 518
Cdd:cd03297 86 LFPHlNVRENLAFGLKR-KRNREDRISVDEL---LDLL---GLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 519 LSAVDAEVGKHLFQLciCQALHEKI---TILVTH---QLQYLkaASHILILKDGEMVQKG 572
Cdd:cd03297 159 FSALDRALRLQLLPE--LKQIKKNLnipVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
997-1209 |
1.09e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 95.54 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidKILTTEIGLHdlRKKMS 1075
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPtSGTV---RLFGKPPRRA--RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEP------------VLFTGTMRKN--LDPFNEHTDEELWRALEEVQLkeaiEDLPGKMDTELaeSGsnfsvGQRQL 1141
Cdd:COG1121 79 YVPQRAevdwdfpitvrdVVLMGRYGRRglFRRPSRADREAVDEALERVGL----EDLADRPIGEL--SG-----GQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1142 VCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
997-1223 |
1.22e-21 |
|
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: 95.34 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDL 1070
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtSGSVLVDgTDLTLlsGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEPVLFTG-TMRKNLD-PF------NEHTDEELWRALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLV 1142
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1143 CLARAILKNNRILIIDEATANVDPRTDELIQQ---KIREKFAqCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVL 1218
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILAllrDINRELG-LTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
....*
gi 255683324 1219 LQNPE 1223
Cdd:cd03258 229 FANPQ 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
384-572 |
1.55e-21 |
|
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: 94.24 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 384 TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNIL 451
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FGKKYEKERY----EKVIKACALKKDLQLLEDgdltvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--- 524
Cdd:cd03301 95 FGLKLRKVPKdeidERVREVAELLQIEHLLDR--------KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAklr 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255683324 525 -EVGKHLFQLcicQALHEKITILVTH-QLQYLKAASHILILKDGEMVQKG 572
Cdd:cd03301 167 vQMRAELKRL---QQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
385-568 |
1.70e-21 |
|
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: 92.85 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNIl 451
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 fgkkyekeryekvikacalkkdlqlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 531
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 255683324 532 QLcICQALHEKITILV-THQLQYLKA-ASHILILKDGEM 568
Cdd:cd03230 136 EL-LRELKKEGKTILLsSHILEEAERlCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
385-569 |
1.75e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.73 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPWVFSG-TV 446
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserelarlrrrHIGFVFQFFNLLPElTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RSNI----LFGKKYEKERYEKVikacalkkdLQLLED-GdltvIGDRG----ATLSGGQKARVNLARAVYQDADIYLLDD 517
Cdd:COG1136 104 LENValplLLAGVSRKERRERA---------RELLERvG----LGDRLdhrpSQLSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 518 PLSAVDAEVGKHLFQLciCQALHEK--ITIL-VTHQLQYLKAASHILILKDGEMV 569
Cdd:COG1136 171 PTGNLDSKTGEEVLEL--LRELNRElgTTIVmVTHDPELAARADRVIRLRDGRIV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
997-1215 |
2.63e-21 |
|
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: 94.73 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS 1075
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPsSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEPVL---FT-------GTM--RKNLDPFNEHTDEELWRALEEVQlkeaIEDLPGKMDTELaeSGsnfsvGQRQLVC 1143
Cdd:COG1120 79 YVPQEPPApfgLTvrelvalGRYphLGLFGRPSAEDREAVEEALERTG----LEHLADRPVDEL--SG-----GERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1144 LARAILKNNRILIIDEATANVDPR----TDELIQQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1215
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAhqleVLELLRRLARER--GRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPP 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
385-577 |
2.94e-21 |
|
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: 93.78 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAV-----LGELPPASGLVSVHG---------------RIAYVSQQPWVFSG 444
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILFGKKYEKERYEKVIKAcalkKDLQLLEDGDLT-VIGDR--GATLSGGQKARVNLARAVYQDADIYLLDDPLSA 521
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDE----RVEEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 522 VDAeVGKHLFQLCIcQALHEKITIL-VTHQL-QYLKAASHILILKDGEMVQKGTYTEF 577
Cdd:cd03260 172 LDP-ISTAKIEELI-AELKKEYTIViVTHNMqQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
395-573 |
3.70e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILFGKKYeKERYE 462
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQHYALFRHmTVFDNIAFGLTV-LPRRE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 463 KVIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALHE 541
Cdd:PRK10851 107 RPNAAAIKAKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW--LRQLHE 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 255683324 542 --KIT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 573
Cdd:PRK10851 185 elKFTsVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
994-1234 |
4.11e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.82 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 994 HEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRK 1072
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEPV-LFTGTMRK---------NLDPFNEhTDEELWRALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLV 1142
Cdd:PRK13648 84 HIGIVFQNPDnQFVGSIVKydvafglenHAVPYDE-MHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1143 CLARAILKNNRILIIDEATANVDP--RTD--ELIQQKIREKfaQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVL 1218
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPdaRQNllDLVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
250 260
....*....|....*....|....*
gi 255683324 1219 LQNPESLF---------YKMVQQLG 1234
Cdd:PRK13648 230 FDHAEELTrigldlpfpIKINQMLG 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
385-578 |
5.30e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 5.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWV-FSGTVRSNI 450
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGkkyekeRYekvIKACALKKDLQL----LEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDAD------IYLLDDPL 519
Cdd:PRK13548 98 AMG------RA---PHGLSRAEDDALvaaaLAQVDLAHLAGRDyPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 520 SAVDAEVGKHLFQLCICQALHEKITIL-VTHQL----QYlkaASHILILKDGEMVQKGTYTEFL 578
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERGLAVIvVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
369-578 |
5.33e-21 |
|
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: 92.88 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 369 VQDFTAFWDKaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAY 434
Cdd:cd03224 3 VENLNAGYGK---SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 435 VSQQPWVFSG-TVRSNILFG-----KKYEKERYEKVikacalkkdLQL---LEDgdltVIGDRGATLSGGQKARVNLARA 505
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGayarrRAKRKARLERV---------YELfprLKE----RRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 506 VYQDADIYLLDDP---LS-AVDAEVGKHLFQLCicqalHEKITILVTHqlQYLKAASHI----LILKDGEMVQKGTYTEF 577
Cdd:cd03224 147 LMSRPKLLLLDEPsegLApKIVEEIFEAIRELR-----DEGVTILLVE--QNARFALEIadraYVLERGRVVLEGTAAEL 219
|
.
gi 255683324 578 L 578
Cdd:cd03224 220 L 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
374-580 |
6.68e-21 |
|
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: 93.33 E-value: 6.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 374 AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQP- 439
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRVQMVFQDPy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 440 ------WvfsgTVRSNI-----LFGKKYEKERYEKVIKACALKKDLQlledgdltvigDR-GATLSGGQKARVNLARAVY 507
Cdd:COG1124 90 aslhprH----TVDRILaeplrIHGLPDREERIAELLEQVGLPPSFL-----------DRyPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 508 QDADIYLLDDPLSAVDAEVGKHLFQLciCQALHE--KIT-ILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 580
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNL--LKDLREerGLTyLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
366-572 |
6.72e-21 |
|
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: 92.95 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 366 IVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------- 430
Cdd:cd03257 1 LLEVKNLSvSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 --RIAYVSQQPwvFSG-----TVRSNI-----LFGKKYEKERYEKVIkaCALKKDLQLLEDgdltVIGDRGATLSGGQKA 498
Cdd:cd03257 81 rkEIQMVFQDP--MSSlnprmTIGEQIaeplrIHGKLSKKEARKEAV--LLLLVGVGLPEE----VLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 499 RVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQALHE-----KITIL-VTHQLQYLKA-ASHILILKDGEMVQK 571
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKlqeelGLTLLfITHDLGVVAKiADRVAVMYAGKIVEE 227
|
.
gi 255683324 572 G 572
Cdd:cd03257 228 G 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
998-1208 |
8.05e-21 |
|
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: 91.09 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSldGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKKM 1074
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPdSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTG-TMRKNLdpfnehtdeelwraleevqlkeaiedlpgkmdtELAESGsnfsvGQRQLVCLARAILKNNR 1153
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI---------------------------------ALGLSG-----GQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1154 ILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
385-580 |
8.09e-21 |
|
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: 93.12 E-value: 8.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPWVFSG-TVR 447
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILF-----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 521
Cdd:COG1127 101 ENVAFplrehTDLSEAEIRELV---------LEKLELVGLPGAADKMpSELSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 522 VDAEVGKHLFQLcIcQALHEKI---TILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 580
Cdd:COG1127 172 LDPITSAVIDEL-I-RELRDELgltSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
385-567 |
9.10e-21 |
|
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: 92.21 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 448
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGKKYEKeryeKVIKACALKKDLQLLED-GDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 527
Cdd:cd03262 96 NITLAPIKVK----GMSKAEAEERALELLEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 255683324 528 KHLFQLcICQALHEKIT-ILVTHQLQY-LKAASHILILKDGE 567
Cdd:cd03262 172 GEVLDV-MKDLAEEGMTmVVVTHEMGFaREVADRVIFMDDGR 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1004-1205 |
1.05e-20 |
|
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: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKIltteiGLHDLRKKMSIIPQ--- 1079
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtSGSIRVFGK-----PLEKERKRIGYVPQrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1080 ----------EPVLFTGTMRKNLDPFNEHTD-EELWRALEEVQLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVCLARAI 1148
Cdd:cd03235 79 idrdfpisvrDVVLMGLYGHKGLFRRLSKADkAKVDEALERVGLSELADRQIGEL------SG-----GQQQRVLLARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1149 LKNNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIIDS-DKIMVLD 1205
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
998-1222 |
1.47e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.95 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILTTEIGLHDLRKKM 1074
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPtEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTGTMRKNL--------------DPFNEHT----------------------------------------- 1099
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIkyslyslkdlealsNYYNEDGndsqenknkrnscrakcagdlndmsnttdsneliemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1100 ---DEELWRALEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKI 1176
Cdd:PTZ00265 543 tikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 255683324 1177 REKFAQCTVLT--IAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNP 1222
Cdd:PTZ00265 623 NNLKGNENRITiiIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
998-1209 |
1.68e-20 |
|
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: 91.40 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGP--LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL---- 1070
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQE---------------PVLFTGTmrknldpFNEHTDEELWRALEEVQLKEAIEDLPGKMdtelaesgsnfS 1135
Cdd:cd03255 81 RRHIGFVFQSfnllpdltalenvelPLLLAGV-------PKKERRERAEELLERVGLGDRLNHYPSEL-----------S 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 1136 VGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1209
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
381-581 |
4.53e-20 |
|
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: 96.04 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV-------------SVHGRIAYVSQQPWVFSGTVR 447
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:COG5265 450 YNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 527 GKHlfqlcICQALHE----KITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:COG5265 530 ERA-----IQAALREvargRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
385-572 |
4.65e-20 |
|
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: 90.28 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAyvsqqpWVF---SG-----TVRSNILFG--- 453
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLglgGGfnpelTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 454 ----KKYEKERYEKVIKACALKKDLqlledgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvgkh 529
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFI------DLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA---- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255683324 530 lFQL-CIcQALHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKG 572
Cdd:cd03220 177 -FQEkCQ-RRLREllkqgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
998-1226 |
9.26e-20 |
|
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: 90.05 E-value: 9.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1076
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPtSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTG-TMRKN--LDPFNEHTDEELWRAleevQLKEAIE--DLPgkmDTELAES-GSNFSVGQRQLVCLARAILK 1150
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKWPKEKIRE----RADELLAlvGLD---PAEFADRyPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1151 NNRILIIDEATANVDPRTDELIQQ---KIREKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPESLF 1226
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEefkRLQQELGK-TIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
349-573 |
1.39e-19 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 93.81 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 349 LDELPQRKAHVPSDGKAIVHVQDFTA-FWDKALDSPT-LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV 426
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKrYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 427 SVHG----------------RIAYVSQQPwvFSG-----TVRSNI-----LFGKKYEKERYEKVikacalkkdLQLLEDG 480
Cdd:COG1123 323 LFDGkdltklsrrslrelrrRVQMVFQDP--YSSlnprmTVGDIIaeplrLHGLLSRAERRERV---------AELLERV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 481 DL--TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALHEK--ITIL-VTHQL---Q 552
Cdd:COG1123 392 GLppDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL--LRDLQRElgLTYLfISHDLavvR 469
|
250 260
....*....|....*....|.
gi 255683324 553 YLkaASHILILKDGEMVQKGT 573
Cdd:COG1123 470 YI--ADRVAVMYDGRIVEDGP 488
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
389-588 |
2.22e-19 |
|
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: 91.32 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 389 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPWVFSG-TVRSNI 450
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGKKYE-----KERYEKVIkacalkkdlQLLEDGDLTvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 523
Cdd:COG4148 99 LYGRKRApraerRISFDEVV---------ELLGIGHLL---DRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDl 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 524 ---AEVGKHLfqlcicQALHEKITI---LVTHQL---QYLkaASHILILKDGEMVQKGTYTEFLkSGVDFGSLL 588
Cdd:COG4148 167 arkAEILPYL------ERLRDELDIpilYVSHSLdevARL--ADHVVLLEQGRVVASGPLAEVL-SRPDLLPLA 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
362-581 |
2.93e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.30 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 362 DGKAIVHVQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------- 430
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 --RIAYVSQQP-WVFSG-TVRSNILFGKKYE----KERYEKVIKACALKKDLQLLEdgdltvigDRGATLSGGQKARVNL 502
Cdd:PRK13635 80 rrQVGMVFQNPdNQFVGaTVQDDVAFGLENIgvprEEMVERVDQALRQVGMEDFLN--------REPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 503 ARAVYQDADIYLLDDPLSAVD----AEVgkhlfqLCICQALHEK--ITIL-VTHQLQYLKAASHILILKDGEMVQKGTYT 575
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDprgrREV------LETVRQLKEQkgITVLsITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*.
gi 255683324 576 EFLKSG 581
Cdd:PRK13635 226 EIFKSG 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
718-970 |
3.62e-19 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 89.53 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd07346 38 LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIP----WILIPLVPLSVVFLVLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWTIRA 873
Cdd:cd07346 118 LQLLSDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRRRIRKASREVRESLAE----LSAFLQESLSGIRVVKA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 874 YKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAI-FVIVVAFG-SLVLAKTLNAGQVGLALSYaltlMGMFQ 951
Cdd:cd07346 194 FAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALgTALVLLYGgYLVLQGSLTIGELVAFLAY----LGMLF 269
|
250 260
....*....|....*....|...
gi 255683324 952 WSVRQSAEVENM----MISVERV 970
Cdd:cd07346 270 GPIQRLANLYNQlqqaLASLERI 292
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
995-1215 |
5.16e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.92 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 995 EGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKK 1073
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQEP-VLFTGTMRKNLDPFN------EHTD--EELWRALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLVCL 1144
Cdd:PRK13635 83 VGMVFQNPdNQFVGATVQDDVAFGlenigvPREEmvERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEP 1215
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
395-572 |
5.41e-19 |
|
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: 86.78 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGK----KYEK 458
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLspglKLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 459 ERYEKVIKACAlKKDLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQA 538
Cdd:cd03298 104 EDRQAIEVALA-RVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 255683324 539 LHEKITIL-VTHQLQYLKA-ASHILILKDGEMVQKG 572
Cdd:cd03298 176 AETKMTVLmVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
360-573 |
7.15e-19 |
|
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: 86.31 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 360 PSDGKaiVHVQDFTAFWDKALdSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------- 430
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDL-PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistiple 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 ----RIAYVSQQPWVFSGTVRSNI-LFGKKYEKERYEkvikacALKkdlqlledgdltvIGDRGATLSGGQKARVNLARA 505
Cdd:cd03369 79 dlrsSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 506 VYQDADIYLLDDPLSAVDAEVgKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGT 573
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
998-1207 |
7.23e-19 |
|
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: 86.62 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALF-RLSEPEGKIWIDKILTTEIGLHDLRKK--- 1073
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 -MSIIPQEPVLFTGTMRKNL---DPFNEHTDEELwraLEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAIL 1149
Cdd:cd03290 80 sVAYAAQKPWLLNATVEENItfgSPFNKQRYKAV---TDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1150 KNNRILIIDEATANVDPR-TDELIQQKIReKFAQ---CTVLTIAHRLNTIIDSDKIMVLDSG 1207
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHLMQEGIL-KFLQddkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
381-573 |
7.59e-19 |
|
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: 86.91 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRI-----AYVSQQPWVFSG-------TVRS 448
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVFQNyalfphlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFG----KKYEKERYEKVIKACALkkdLQLLEDGDltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:cd03300 92 NIAFGlrlkKLPKAEIKERVAEALDL---VQLEGYAN-----RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 525 EVGKHLfQLCIcQALHEK--IT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 573
Cdd:cd03300 164 KLRKDM-QLEL-KRLQKElgITfVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
997-1234 |
7.84e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 7.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGP-LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKM 1074
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEP-VLFTGTMRKNLDPFN-EHTDEELWRALEEVQlkEAIEdLPGKMDTELAESgSNFSVGQRQLVCLARAILKNN 1152
Cdd:PRK13650 84 GMVFQNPdNQFVGATVEDDVAFGlENKGIPHEEMKERVN--EALE-LVGMQDFKEREP-ARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1153 RILIIDEATANVDPRTD-ELIQ--QKIREKFaQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLfykm 1229
Cdd:PRK13650 160 KIIILDEATSMLDPEGRlELIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL---- 234
|
....*
gi 255683324 1230 vQQLG 1234
Cdd:PRK13650 235 -LQLG 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
381-573 |
1.44e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TV 446
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RS---------NILFGKKYEKERyEKVIKAcalkkdlqlLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLD 516
Cdd:PRK11231 94 RElvaygrspwLSLWGRLSAEDN-ARVNQA---------MEQTRINHLADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 517 DPLSAVD----AEVGKHLFQLcicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 573
Cdd:PRK11231 164 EPTTYLDinhqVELMRLMREL----NTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
385-580 |
1.64e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 86.06 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV----------SVHGR----IAYVSQQPWVFSG-TVRSN 449
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRarlgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 523
Cdd:cd03218 96 ILavleIRGLSKKEREEKLE---------ELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 524 ---AEVGKhlfqlcICQALHEK-ITILVT-HQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:cd03218 167 iavQDIQK------IIKILKDRgIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
381-523 |
1.98e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWV-FSGTV 446
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 447 RSNILFGKKYEKERYEKVIKACALKKDlQLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
997-1222 |
1.98e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIG-LHDLRKKM 1074
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEP-VLFTGTMrknldpfnehTDEELWRALEEVQLKEAieDLPGKMDTELAESG---------SNFSVGQRQLVCL 1144
Cdd:PRK13644 80 GIVFQNPeTQFVGRT----------VEEDLAFGPENLCLPPI--EIRKRVDRALAEIGlekyrhrspKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQC-TVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNP 1222
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
385-573 |
2.21e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAyvsqqpWVF---SG-----TVRSNILFG--- 453
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgAGfhpelTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 454 ----KKYEKERYEKVIkacalkkdlqlledgDLTVIGD------RgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 524 AEvgkhlFQL-CIcQALHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKGT 573
Cdd:COG1134 179 AA-----FQKkCL-ARIRElresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
385-576 |
2.77e-18 |
|
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: 85.57 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 449
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFG--------------KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYL 514
Cdd:cd03219 96 VMVAaqartgsglllaraRREEREARERA---------EELLERVGLADLADRPAgELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 515 LDDPLSAVDAEVGKHLFQLcICQALHEKITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTE 576
Cdd:cd03219 167 LDEPAAGLNPEETEELAEL-IRELRERGITVLLVeHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
998-1208 |
3.33e-18 |
|
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: 85.31 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG---LHDLRKK 1073
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQEP-----------VL-----FTGTMRKNLDPFNEHTDEELWRALEEVQLkeaiEDLPGKMDTELaeSGsnfsvG 1137
Cdd:cd03256 80 IGMIFQQFnlierlsvlenVLsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGL----LDKAYQRADQL--SG-----G 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 1138 QRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
389-588 |
3.39e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 389 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---RIAYVSQQPW--------VFSG-TVRSNILFG--- 453
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRPVsmlfqennLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 454 ----KKYEKERYEKVIKACALKKDLQLLEdgdltvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 529
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 530 LFQLC--ICQalHEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL 588
Cdd:PRK10771 168 MLTLVsqVCQ--ERQLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
383-524 |
3.65e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.68 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRI--------AYVSQQ----PWVfsgTVRSNI 450
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGKKY----EKERYEKvikACALkkdLQL--LEDgdltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:COG4525 98 AFGLRLrgvpKAERRAR---AEEL---LALvgLAD----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
998-1225 |
4.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.04 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTAL---IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILTTEIG---LHD 1069
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNIsfeLEEGSFVALVGHTGSGKSTLMQHFNALLKPsSGTITIaGYHITPETGnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1070 LRKKMSIIPQ--EPVLFTGTMRKNLD--PFN-----EHTDEELWRALEEVQLKeaiEDLPGKMDTELaesgsnfSVGQRQ 1140
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfgfseDEAKEKALKWLKKVGLS---EDLISKSPFEL-------SGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1141 LVCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVL 1218
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
....*..
gi 255683324 1219 LQNPESL 1225
Cdd:PRK13641 233 FSDKEWL 239
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
325-566 |
5.05e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 325 FFPSAIERGSEAIVSIRRIKNFL----LLDELPQRKAHVPSDGKAIVHVQDFTafwdkaLDSPT----LQGLSFIARPGE 396
Cdd:COG4178 317 WFVDNYQSLAEWRATVDRLAGFEealeAADALPEAASRIETSEDGALALEDLT------LRTPDgrplLEDLSLSLKPGE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 397 LLAVVGPVGAGKSSLLSAVLGELPPASGLVSV--HGRIAYVSQQPWVFSGTVRSNILF---GKKYEKERYEKVIKACALK 471
Cdd:COG4178 391 RLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 472 KDLQLLEDGDltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQL 551
Cdd:COG4178 471 HLAERLDEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPGTTVISVGHRS 544
|
250
....*....|....*
gi 255683324 552 QYLKAASHILILKDG 566
Cdd:COG4178 545 TLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
993-1235 |
6.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.62 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 993 PHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSS---LISALFRLSE-PEGKIWIDKILTTEIGLH 1068
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1069 DLRKKMSIIPQEP-VLFTGTMRKNLDPFNEHTdeelwRALEEVQLKEAIEDL---PGKMDTELAESgSNFSVGQRQLVCL 1144
Cdd:PRK13640 81 DIREKVGIVFQNPdNQFVGATVGDDVAFGLEN-----RAVPRPEMIKIVRDVladVGMLDYIDSEP-ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNP 1222
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
250 260
....*....|....*....|..
gi 255683324 1223 ESL---------FYKMVQQLGK 1235
Cdd:PRK13640 235 EMLkeigldipfVYKLKNKLKE 256
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
385-550 |
8.49e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 8.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------RIAYVSQQ----PwvfSGTVRSNI 450
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRnamkP---ALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGKKYeKERYEKVIKACALKKDLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGKHL 530
Cdd:PRK13539 95 EFWAAF-LGGEELDIAAALEAVGLAPLAH-------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVAL 165
|
170 180
....*....|....*....|...
gi 255683324 531 FQLCIcqALHEK---ITILVTHQ 550
Cdd:PRK13539 166 FAELI--RAHLAqggIVIAATHI 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
385-580 |
1.11e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 83.98 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGL-VSVHG-------------RIAYVS---QQPWVFSGTVR 447
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIGLVSpalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNIL---FG-----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 518
Cdd:COG1119 99 DVVLsgfFDsiglyREPTDEQRERA---------RELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 519 LSAVDAEvGKHLF-----QLCicqALHEKITILVTHQLQYLKAA-SHILILKDGEMVQKGTYTEFLKS 580
Cdd:COG1119 170 TAGLDLG-ARELLlalldKLA---AEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
367-567 |
1.26e-17 |
|
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: 80.96 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQqpwvfsg 444
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 tvrsnilfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 255683324 525 EVgkhlfqlciCQAL------HEKITILVTHQLQYLKA-ASHILILKDGE 567
Cdd:cd03221 104 ES---------IEALeealkeYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
381-579 |
1.63e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 82.94 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVR 447
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILF-------GKKYEKERYEKVIKACALKKDLqlledgdltvigDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:cd03263 94 EHLRFyarlkglPKSEIKEEVELLLRVLGLTDKA------------NKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 520 SAVDAeVGKHLfqlcICQALHEKIT----ILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEfLK 579
Cdd:cd03263 162 SGLDP-ASRRA----IWDLILEVRKgrsiILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE-LK 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
998-1209 |
1.92e-17 |
|
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: 82.57 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlRKKMSI 1076
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPdSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFTG-TMRKN----LDPFNEHTDEELWRALEEVQLKEaIEDLPGKMDTELaeSGsnfsvGQRQLVCLARAILKN 1151
Cdd:cd03259 77 VFQDYALFPHlTVAENiafgLKLRGVPKAEIRARVRELLELVG-LEGLLNRYPHEL--SG-----GQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1152 NRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRI 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
374-596 |
2.29e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 374 AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQQPWVFSG-TVRSNI 450
Cdd:COG0488 7 SFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFG--------KKYEK------------ERYEKVI-------------KACALKKDLQL-LEDGDLTVigdrgATLSGGQ 496
Cdd:COG0488 83 LDGdaelraleAELEEleaklaepdedlERLAELQeefealggweaeaRAEEILSGLGFpEEDLDRPV-----SELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 497 KARVNLARAVYQDADIYLLDDP---LsavDAE-VG---KHLfqlcicqaLHEKIT-ILVTHQLQYL-KAASHILILKDGE 567
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPtnhL---DLEsIEwleEFL--------KNYPGTvLVVSHDRYFLdRVATRILELDRGK 226
|
250 260 270
....*....|....*....|....*....|
gi 255683324 568 MVQ-KGTYTEFLKSgvdfgsllKKENEEAE 596
Cdd:COG0488 227 LTLyPGNYSAYLEQ--------RAERLEQE 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
998-1225 |
2.57e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.92 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGP---LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILTTEI---GLHD 1069
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPtSGTVTIgERVITAGKknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1070 LRKKMSIIPQ--EPVLFTGTMRKNL--DPFNEHTDEE--LWRALEEVQLKEAIEDLpgkmdteLAESGSNFSVGQRQLVC 1143
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMNFGVSEEdaKQKAREMIELVGLPEEL-------LARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1144 LARAILKNNRILIIDEATANVDPRTdeliQQKIREKFAQC------TVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPY 1216
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYKLhkekglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*....
gi 255683324 1217 VLLQNPESL 1225
Cdd:PRK13634 232 EIFADPDEL 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1004-1178 |
3.00e-17 |
|
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: 81.76 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSIIPQEPV 1082
Cdd:COG4133 7 NLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPsAGEVLWNGEPIRDAR-EDYRRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 LFTG-TMRKNLDpF------NEHTDEELWRALEEVQLkEAIEDLPGKMdtelaesgsnFSVGQRQLVCLARAILKNNRIL 1155
Cdd:COG4133 86 LKPElTVRENLR-FwaalygLRADREAIDEALEAVGL-AGLADLPVRQ----------LSAGQKRRVALARLLLSPAPLW 153
|
170 180
....*....|....*....|...
gi 255683324 1156 IIDEATANVDPRTDELIQQKIRE 1178
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
366-572 |
5.72e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 81.26 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 366 IVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGriAYVSQQPW---- 440
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 441 ---VFSG--------TVRSNIL-FGKKYEKERYEkvIKAcALKKDLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQ 508
Cdd:cd03266 79 rlgFVSDstglydrlTARENLEyFAGLYGLKGDE--LTA-RLEELADRLGMEEL--LDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 509 DADIYLLDDPLSAVDAEVGKHLFQlcICQALHE--KITILVTHQLQYLKA-ASHILILKDGEMVQKG 572
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALRE--FIRQLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
997-1211 |
6.60e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 81.24 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL--- 1070
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 -RKKMSIIPQE---------------PVLFTGTMRKNldpfnehTDEELWRALEEVQLKEAIEDLPGKMdtelaesgsnf 1134
Cdd:COG1136 84 rRRHIGFVFQFfnllpeltalenvalPLLLAGVSRKE-------RRERARELLERVGLGDRLDHRPSQL----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1135 SVGQRQLVCLARAILKNNRILIIDEATANVDPRT-DELIQ--QKIREKFaQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1211
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
383-550 |
8.33e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.10 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------------IAYVSQQPWVFSG-TVRSN 449
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGKKyekeryekvIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGK 528
Cdd:TIGR01189 94 LHFWAA---------IHGGAQRTIEDALAAVGLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GV 163
|
170 180
....*....|....*....|...
gi 255683324 529 HLFQLCICQALHEK-ITILVTHQ 550
Cdd:TIGR01189 164 ALLAGLLRAHLARGgIVLLTTHQ 186
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
388-577 |
1.03e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 388 LSFIARPGELLAVVGPVGAGKSSLLSaVLGELP-PASGLVSVHGRIAYVSQQP-------------WVFSG-------TV 446
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGNHFDFSKTPsdkairelrrnvgMVFQQynlwphlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RSNILfgkkyekERYEKVI---KACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 522
Cdd:PRK11124 100 QQNLI-------EAPCRVLglsKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 523 DAEVGKHLFQlcICQALHE-KIT-ILVTHQLQYL-KAASHILILKDGEMVQKGTYTEF 577
Cdd:PRK11124 173 DPEITAQIVS--IIRELAEtGITqVIVTHEVEVArKTASRVVYMENGHIVEQGDASCF 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
385-572 |
1.79e-16 |
|
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: 79.54 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGeLLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPwvfsgTVRSNIlf 452
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPNF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 453 gKKYEKERYEKVIKACALKKD----LQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvG 527
Cdd:cd03264 88 -TVREFLDYIAWLKGIPSKEVkarvDEVLELVNLGdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE-E 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255683324 528 KHLFQLCICQALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 572
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
996-1209 |
1.95e-16 |
|
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: 77.85 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDkiltteiglhdlrkkm 1074
Cdd:cd03216 12 GVKALDGVSLS---------------VRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVD---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 siipQEPVLFtgtmrknldpfneHTDEELWRA-LEEV-QLkeaiedlpgkmdtelaesgsnfSVGQRQLVCLARAILKNN 1152
Cdd:cd03216 61 ----GKEVSF-------------ASPRDARRAgIAMVyQL----------------------SVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1153 RILIIDEATANVDPR-TDELIQQkIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03216 102 RLLILDEPTAALTPAeVERLFKV-IRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
381-569 |
3.34e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.94 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPWVFSG 444
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 -TVRSNILF-----GKKyEKERYEKVIKacALKKdlqlledgdltV-IGDRG----ATLSGGQKARVNLARAVYQDADIY 513
Cdd:COG2884 94 rTVYENVALplrvtGKS-RKEIRRRVRE--VLDL-----------VgLSDKAkalpHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 514 LLDDPLSAVDAEVGKHLFQLciCQALHEK-ITILV-THQLQYLKAASH-ILILKDGEMV 569
Cdd:COG2884 160 LADEPTGNLDPETSWEIMEL--LEEINRRgTTVLIaTHDLELVDRMPKrVLELEDGRLV 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
993-1223 |
3.35e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.08 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 993 PHEGVIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE--P----EGKIWIDK--ILTTE 1064
Cdd:COG1117 7 TLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarvEGEILLDGedIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1065 IGLHDLRKKMSIIPQEPVLFTGTMRKN----------LDPfnEHTDEELWRALEEVQLKEAIEDlpgkmdtELAESGSNF 1134
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPFPKSIYDNvayglrlhgiKSK--SELDEIVEESLRKAALWDEVKD-------RLKKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1135 SVGQRQLVCLARAILKNNRILIIDEATANVDP----RTDELIQQkIREKFaqcTVLTIAH------RLntiidSDKIMVL 1204
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPistaKIEELILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFF 226
|
250
....*....|....*....
gi 255683324 1205 DSGRLKEYDEPYVLLQNPE 1223
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPK 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
385-572 |
4.18e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.98 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA--SGLVSVHGR----------IAYVSQQPWVFSG-TVRSNIL 451
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkrsfrkiIGYVPQDDILHPTlTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FgkkyekeryekvikACALKKdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 531
Cdd:cd03213 105 F--------------AAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255683324 532 QLCICQALHEKITILVTHQLQYL--KAASHILILKDGEMVQKG 572
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
718-970 |
5.83e-16 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 80.12 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIP----WILIPLVPLSVVFLVLRRYfletSRDVKRLESTTRSPVFSHLSSSLQGLWTIRA 873
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWrlalISLLVLPLLLLATYLFRKK----SRKAYREVREKLSRLNAFLQESISGMSVIQL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 874 YKAEERCQELFDAHQDLHSEAWFLFLTTSRWF--AVRLDAICAIFVIVVAFGSLVLAKTLNAGQVglalsYA-LTLMGMF 950
Cdd:cd18544 196 FNREKREFEEFDEINQEYRKANLKSIKLFALFrpLVELLSSLALALVLWYGGGQVLSGAVTLGVL-----YAfIQYIQRF 270
|
250 260
....*....|....*....|....*....
gi 255683324 951 ---------QWSVRQSAevenmMISVERV 970
Cdd:cd18544 271 frpirdlaeKFNILQSA-----MASAERI 294
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
383-552 |
6.95e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.97 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRI--------AYVSQQ----PWVfsgTVRSNI 450
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 529
Cdd:PRK11248 92 AFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*
gi 255683324 530 LfQLCICQALHE--KITILVTHQLQ 552
Cdd:PRK11248 167 M-QTLLLKLWQEtgKQVLLITHDIE 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
997-1209 |
7.00e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.21 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVnfTYSLDGPL------VLKHLTALIKSREKVGIVGRTGAGKSSLISALF-RLSEP--EGKIWIDKIlttEIGL 1067
Cdd:cd03213 3 TLSFRNL--TVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLgvSGEVLINGR---PLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1068 HDLRKKMSIIPQEPVLF-TGTMRKNLDpFNehtdeelwraleeVQLKeaiedlpgkmdtelaesgsNFSVGQRQLVCLAR 1146
Cdd:cd03213 78 RSFRKIIGYVPQDDILHpTLTVRETLM-FA-------------AKLR-------------------GLSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1147 AILKNNRILIIDEATANVDPRTDELIQQKIReKFAQ--CTVLTIAHRLNTIIDS--DKIMVLDSGRL 1209
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
385-579 |
1.04e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.80 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNI- 450
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGKKY------EKERYEKVIKAcalkkdLQLLEDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:cd03265 96 IHARLYgvpgaeRRERIDELLDF------VGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 525 EVGKHLFQlcICQALHEK--ITILVThqLQYL----KAASHILILKDGEMVQKGTYTEfLK 579
Cdd:cd03265 165 QTRAHVWE--YIEKLKEEfgMTILLT--THYMeeaeQLCDRVAIIDHGRIIAEGTPEE-LK 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
998-1168 |
1.60e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 77.06 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTeiGLHD-----LR 1071
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPtSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1072 KKMSIIPQE-PVLFTGTMRKNLDPFNEHTDE--ELWR-----ALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLVC 1143
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYENVAFALEVTGVppREIRkrvpaALELVGLSHKHRALP-----------AELSGGEQQRVA 146
|
170 180
....*....|....*....|....*
gi 255683324 1144 LARAILKNNRILIIDEATANVDPRT 1168
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDT 171
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
385-572 |
1.76e-15 |
|
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: 76.93 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHG----------RIAYVSQQP-WVFSGTVR--- 447
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRetl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 --SNILFGKKYEKERYEKVIKACALKKDLqlledGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA- 524
Cdd:cd03234 103 tyTAILRLPRKSSDAIRKKRVEDVLLRDL-----ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSf 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255683324 525 ---EVGKHLFQLCicqalHEKITILVT-HQ--LQYLKAASHILILKDGEMVQKG 572
Cdd:cd03234 178 talNLVSTLSQLA-----RRNRIVILTiHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
385-572 |
1.97e-15 |
|
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: 76.49 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILF 452
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIEAPGFYPNlTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 453 GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 531
Cdd:cd03268 96 LARLLGIRKKRI---------DEVLDVVGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255683324 532 QLCICQAlHEKITILV-THQLQYL-KAASHILILKDGEMVQKG 572
Cdd:cd03268 167 ELILSLR-DQGITVLIsSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
385-550 |
2.15e-15 |
|
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: 76.38 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------------IAYVSQQPWVFSG-TVRSNIL 451
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIKTTlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FGKKYekeryekvikaCALKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 530
Cdd:cd03231 96 FWHAD-----------HSDEQVEEALARVGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 255683324 531 FQLCICQALHEKITILVTHQ 550
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQ 184
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
381-582 |
2.23e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TV 446
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RSNILFGK------KYEKERYEKVIKAcalkkdLQLLedgDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:COG4604 93 RELVAFGRfpyskgRLTAEDREIIDEA------IAYL---DLEDLADRYLdELSGGQRQRAFIAMVLAQDTDYVLLDEPL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 520 SAVD----AEVGKHLFQLCicqalHE--KITILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGV 582
Cdd:COG4604 164 NNLDmkhsVQMMKLLRRLA-----DElgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1029-1210 |
2.92e-15 |
|
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: 76.08 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1029 GIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSIIPQEPVLFTG-TMRKNLDPF-------NEHT 1099
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPsSGTIRIDGQDVLKQP-QKLRRRIGYLPQEFGVYPNfTVREFLDYIawlkgipSKEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1100 DEELWRALEEVQLKEAIEDLPGKmdtelaesgsnFSVGQRQLVCLARAILKNNRILIIDEATANVDP----RTDELIQQK 1175
Cdd:cd03264 108 KARVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeeriRFRNLLSEL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 255683324 1176 IREKfaqcTVLTIAHRLNTIIDS-DKIMVLDSGRLK 1210
Cdd:cd03264 177 GEDR----IVILSTHIVEDVESLcNQVAVLNKGKLV 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1001-1222 |
2.95e-15 |
|
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: 78.17 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1001 DNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP----EGKIWIDKILTTEIGLHDLR----K 1072
Cdd:COG0444 22 DGVSFD---------------VRRGETLGLVGESGSGKSTLARAILGLLPPpgitSGEILFDGEDLLKLSEKELRkirgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQE------PVLftgTMRKNL-DPFNEHTD---EELWR----ALEEVQLKEAIEDL---PGkmdtELaeSGsnfs 1135
Cdd:COG0444 87 EIQMIFQDpmtslnPVM---TVGDQIaEPLRIHGGlskAEAREraieLLERVGLPDPERRLdryPH----EL--SG---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1136 vGQRQLVCLARAILKNNRILIIDEATANVDPrtdeLIQ-------QKIREKFaQCTVLTIAHRLNTI--IdSDKIMVLDS 1206
Cdd:COG0444 154 -GMRQRVMIARALALEPKLLIADEPTTALDV----TIQaqilnllKDLQREL-GLAILFITHDLGVVaeI-ADRVAVMYA 226
|
250
....*....|....*.
gi 255683324 1207 GRLKEYDEPYVLLQNP 1222
Cdd:COG0444 227 GRIVEEGPVEELFENP 242
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
998-1223 |
2.98e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 76.72 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYsldgPLVLKHLTALIKSREKVGIVGRTGAGKSSLISAL--FrLSEPEGKIWID--KILTTEIGlhdlRKK 1073
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIagF-LPPDSGRILWNgqDLTALPPA----ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQEPVLFTG-TMRKN----LDP---FNEHTDEELWRALEEVQLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVCLA 1145
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNiglgLRPglkLTAEQRAQVEQALERVGLAGLLDRLPGQL------SG-----GQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1146 RAILKNNRILIIDEATANVDP--RTD--ELIQQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLkEYDEPYVLLQ 1220
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPalRQEmlDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRI-AADGPTAALL 218
|
...
gi 255683324 1221 NPE 1223
Cdd:COG3840 219 DGE 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
385-523 |
3.15e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 449
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 450 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:COG1137 99 ILavleLRKLSKKEREERLE---------ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
385-578 |
4.05e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 76.19 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 448
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskkdinklrrKVGMVFQQFNLFPHlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGKKYEKeryeKVIKACALKKDLQLLEdgdlTV-IGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:COG1126 97 NVTLAPIKVK----KMSKAEAEERAMELLE----RVgLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 524 ----AEVgkhlfqLCICQAL-HEKIT-ILVTHQLQY-LKAASHILILKDGEMVQKGTYTEFL 578
Cdd:COG1126 169 pelvGEV------LDVMRDLaKEGMTmVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1003-1223 |
4.09e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.06 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1003 VNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLH------DLRKKMS 1075
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGYRYSGDVLLGGRSIFnyrdvlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEPVLFTGTMRKN---------LDPFNEHTDEELWRaLEEVQLKEAIEDlpgkmdtELAESGSNFSVGQRQLVCLAR 1146
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNvlagvrahkLVPRKEFRGVAQAR-LTEVGLWDAVKD-------RLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1147 AILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPE 1223
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-579 |
4.09e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 342 RIKNF--LLLDELPQRKAHV----PSD---GKAIVHVQDFT-AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSL 411
Cdd:COG0488 282 RIKALekLEREEPPRRDKTVeirfPPPerlGKKVLELEGLSkSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 412 LSAVLGELPPASGLVsVHG---RIAYVSQQPWVFSG--TVRSNIlfgKKYEKERYEKVIKacalkkdlQLLED----GD- 481
Cdd:COG0488 358 LKLLAGELEPDSGTV-KLGetvKIGYFDQHQEELDPdkTVLDEL---RDGAPGGTEQEVR--------GYLGRflfsGDd 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 482 -LTVIGDrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfqlciCQALHEKIT------ILVTHQLQYL 554
Cdd:COG0488 426 aFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET---------LEALEEALDdfpgtvLLVSHDRYFL 492
|
250 260
....*....|....*....|....*..
gi 255683324 555 KA-ASHILILKDGEMVQK-GTYTEFLK 579
Cdd:COG0488 493 DRvATRILEFEDGGVREYpGGYDDYLE 519
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1001-1207 |
4.27e-15 |
|
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: 77.20 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1001 DNVNFT-YSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidkiltteigLHDLRkkMSIIP 1078
Cdd:cd03291 38 NNLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPsEGKI-----------KHSGR--ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1079 QEPVLFTGTMRKNLdPFNEHTDEELWRA-LEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNRILII 1157
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1158 DEATANVDPRTDELIQQKIREKF-AQCTVLTIAHRLNTIIDSDKIMVLDSG 1207
Cdd:cd03291 184 DSPFGYLDVFTEKEIFESCVCKLmANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1004-1195 |
5.44e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWID--------KILTTEIGLHDLRKKMS 1075
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffnqNIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEPVLFTGTMRKN----LDPFNEHTDEELwRALEEVQLKEAieDLPGKMDTELAESGSNFSVGQRQLVCLARAILKN 1151
Cdd:PRK14258 92 MVHPKPNLFPMSVYDNvaygVKIVGWRPKLEI-DDIVESALKDA--DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255683324 1152 NRILIIDEATANVDP----RTDELIQQ-KIRekfAQCTVLTIAHRLNTI 1195
Cdd:PRK14258 169 PKVLLMDEPCFGLDPiasmKVESLIQSlRLR---SELTMVIVSHNLHQV 214
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
117-534 |
6.82e-15 |
|
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: 79.79 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 117 QCAgMRLRVAMCHMIYRKAL------RLSNSamgKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVL-LWVE 189
Cdd:TIGR00954 161 ELK-LRFRVRLTRYLYSKYLsgftfyKVSNL---DSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFkLLTA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 190 IGISCLAGLAVLV-----ILLPLQSCIGKLfsslrSKTAAFTDARIRTMN-EVITGMRIIKMYAWEK--------SFADL 255
Cdd:TIGR00954 237 LGSVGPAGLFAYLfatgvVLTKLRPPIGKL-----TVEEQALEGEYRYVHsRLIMNSEEIAFYQGNKveketvmsSFYRL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 256 IANLRKKEISKIlgssylrGMNMASFFIANKV-----ILFVTFTSYVLLG-NEITASHVFVAMTLYGAVRLTVTLffPSA 329
Cdd:TIGR00954 312 VEHLNLIIKFRF-------SYGFLDNIVAKYTwsavgLVAVSIPIFDKTHpAFLEMSEEELMQEFYNNGRLLLKA--ADA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 330 IERGSEAIVSIRRIKNFLL-LDELPQ----------RKAHVPSD--------------GKAIVHVQD-FTAFWDKALDSP 383
Cdd:TIGR00954 383 LGRLMLAGRDMTRLAGFTArVDTLLQvlddvksgnfKRPRVEEIesgreggrnsnlvpGRGIVEYQDnGIKFENIPLVTP 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 384 T----LQGLSFIARPGELLAVVGPVGAGKSSLLSaVLGEL-PPASGLVSV--HGRIAYVSQQPWVFSGTVRSNILFGKKY 456
Cdd:TIGR00954 463 NgdvlIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELwPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSS 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 457 EkERYEKVIKACALKKDLQLL-------EDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 529
Cdd:TIGR00954 542 E-DMKRRGLSDKDLEQILDNVqlthileREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY 620
|
....*
gi 255683324 530 LFQLC 534
Cdd:TIGR00954 621 MYRLC 625
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
364-560 |
6.94e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 364 KAIVHVQDFTAFWDKaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPP---ASGLVSVHGR------- 431
Cdd:PRK14239 3 EPILQVSDLSVYYNK---KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHniysprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 432 --------IAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKAcALKKDLQ--LLEDGDLTVIGDRGATLSGGQKARVN 501
Cdd:PRK14239 80 dtvdlrkeIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKgaSIWDEVKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 502 LARAVYQDADIYLLDDPLSAVD----AEVGKHLFqlcicqALHEKITIL-VTHQLQylkAASHI 560
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpisaGKIEETLL------GLKDDYTMLlVTRSMQ---QASRI 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
381-548 |
7.40e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQqpwvFSG---- 444
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQ----FDNldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 -TVRSNIL-FGKKY--EKERYEKVIKAcalkkdlqLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:PRK13536 129 fTVRENLLvFGRYFgmSTREIEAVIPS--------LLEFARLESKADaRVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180
....*....|....*....|....*....
gi 255683324 520 SAVDAEvGKHLFQLCICQALHEKITILVT 548
Cdd:PRK13536 201 TGLDPH-ARHLIWERLRSLLARGKTILLT 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
385-565 |
9.14e-15 |
|
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: 73.34 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLsAVLGEL-PPASGLVSVHGR--IAYVSQQPWVFSGTVRSNILfgkkYEKERy 461
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLwPWGSGRIGMPEGedLLFLPQRPYLPLGTLREQLI----YPWDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 462 ekvikacalkkdlqlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCicqaLHE 541
Cdd:cd03223 91 -----------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KEL 137
|
170 180
....*....|....*....|....*
gi 255683324 542 KITIL-VTHQLQYLKAASHILILKD 565
Cdd:cd03223 138 GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
50-343 |
1.03e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 76.44 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIEEGTRVVQPLFLGKIIeyfekydpdDSVALHTAYG----YAAVLSMCTLILAILHHLYFYHVQCAGMRLRV 125
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLI---------DDVIPAGDLSlllwIALLLLLLALLRALLSYLRRYLAARLGQRVVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 126 AMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIAVTVLL----WVeigiscLAgLAV 200
Cdd:cd07346 73 DLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK------LT-LVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 201 LVIlLPLQSCIGKLFSSLRSKtaAFTDARIR------TMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISKILGS 270
Cdd:cd07346 146 LLL-LPLYVLILRYFRRRIRK--ASREVRESlaelsaFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLS 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 271 SYLRGMNMASFFIANkVILFVtFTSYVLLGNEITASHVFVAMT----LYGAVRLTVTLFfpSAIERgseAIVSIRRI 343
Cdd:cd07346 223 ALFSPLIGLLTALGT-ALVLL-YGGYLVLQGSLTIGELVAFLAylgmLFGPIQRLANLY--NQLQQ---ALASLERI 292
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
998-1191 |
1.04e-14 |
|
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: 73.34 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFtYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALfrlsepeGKIWidKILTTEIGLHDlRKKMSII 1077
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLW--PWGSGRIGMPE-GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1078 PQEPVLFTGTMRknldpfnehtdEELWRALEEVqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKNNRILII 1157
Cdd:cd03223 70 PQRPYLPLGTLR-----------EQLIYPWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 255683324 1158 DEATANVDPRTDELIQQKIREKFAqcTVLTIAHR 1191
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
360-573 |
1.20e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 360 PSDGKAIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIayVSQQP 439
Cdd:PRK09452 8 PSSLSPLVELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 440 -------WVFSG-------TVRSNILFGKKYEK----ERYEKVIKACALKKdlqlLEDgdltvIGDRGAT-LSGGQKARV 500
Cdd:PRK09452 83 aenrhvnTVFQSyalfphmTVFENVAFGLRMQKtpaaEITPRVMEALRMVQ----LEE-----FAQRKPHqLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 501 NLARAVYQDADIYLLDDPLSAVDAEVGKHLfQLCIcQALHEK--IT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 573
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQM-QNEL-KALQRKlgITfVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
998-1224 |
1.32e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 76.66 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVlkhlTAL------IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGL 1067
Cdd:COG1135 2 IELENLSKTFPTKGGPV----TALddvsltIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLVDgVDLTAlsEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1068 HDLRKKMSIIPQEpvlFtgtmrkNLdpfnehtdeeLWR--ALEEVQL--------KEAIE----------DLPGKMDTEL 1127
Cdd:COG1135 78 RAARRKIGMIFQH---F------NL----------LSSrtVAENVALpleiagvpKAEIRkrvaellelvGLSDKADAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1128 AE-SGsnfsvGQRQLVCLARAiLKNN-RILIIDEATANVDPRTD----ELIqQKIREKFaQCTVLTIAHRLNTI--IdSD 1199
Cdd:COG1135 139 SQlSG-----GQKQRVGIARA-LANNpKVLLCDEATSALDPETTrsilDLL-KDINREL-GLTIVLITHEMDVVrrI-CD 209
|
250 260
....*....|....*....|....*
gi 255683324 1200 KIMVLDSGRLKEYDEPYVLLQNPES 1224
Cdd:COG1135 210 RVAVLENGRIVEQGPVLDVFANPQS 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
998-1210 |
1.36e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 74.46 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-LTTEIglHDLRKKMS 1075
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGYsIRTDR--KAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEPVLFTG-TMRKNLdpfnehtdeELW---RALEEVQLKEAIE------DLPGKMDTELaesgSNFSVGQRQLVCLA 1145
Cdd:cd03263 79 YCPQFDALFDElTVREHL---------RFYarlKGLPKSEIKEEVElllrvlGLTDKANKRA----RTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 1146 RAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTI-IDSDKIMVLDSGRLK 1210
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLR 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
372-585 |
1.37e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 372 FTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHG----------RIAYVSQQ 438
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemraISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 439 PWVF-SGTVRSNILF----------GKKYEKERYEKVIKACALKKDLQlledgdlTVIGDRGAT--LSGGQKARVNLARA 505
Cdd:TIGR00955 108 DLFIpTLTVREHLMFqahlrmprrvTKKEKRERVDEVLQALGLRKCAN-------TRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 506 VYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQY--LKAASHILILKDGEMVQKGTYTEFLKSGVD 583
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
..
gi 255683324 584 FG 585
Cdd:TIGR00955 261 LG 262
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
369-570 |
1.48e-14 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 75.66 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 369 VQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLgELPPASGLVSVHG-----------RIAY--V 435
Cdd:cd03289 5 VKDLTAKYTEG-GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 436 SQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLL 515
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 516 DDPLSAVDAeVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQ 570
Cdd:cd03289 163 DEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
378-568 |
1.84e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG 444
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILFGKKYEKERYEKVikacALKKDLQLLEDgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDa 524
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPA----IFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 525 EVGKHLFQLCICQALHEK-ITIL-VTHQLQYLKAASHILILKD--GEM 568
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQnIAVLwVTHDKDEINHADKVITLQPhaGEM 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
367-589 |
2.01e-14 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 74.56 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKALdSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIA 433
Cdd:cd03288 20 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 434 YVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIY 513
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 514 LLDDPLSAVDAEVgKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL--KSGVdFGSLLK 589
Cdd:cd03288 179 IMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaqEDGV-FASLVR 254
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
385-569 |
2.20e-14 |
|
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: 72.08 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQqpwvfsgtvrsni 450
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarragIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 lfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 530
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255683324 531 FQLcICQALHEKITIL-VTHQLQYLKA-ASHILILKDGEMV 569
Cdd:cd03216 122 FKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
383-577 |
2.56e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVR 447
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGKKYEKERYEKVikaCALKKDLQLLEDGDLTvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 527
Cdd:PRK15439 105 ENILFGLPKRQASMQKM---KQLLAALGCQLDLDSS-----AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 528 KHLF-QLCICQALHEKItILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEF 577
Cdd:PRK15439 177 ERLFsRIRELLAQGVGI-VFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
998-1209 |
3.09e-14 |
|
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: 72.95 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYsldGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKK 1073
Cdd:cd03262 1 IEIKNLHKSF---GDFhVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIDglKLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQEPVLF---------TGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVCL 1144
Cdd:cd03262 78 VGMVFQQFNLFphltvleniTLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQL------SG-----GQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1145 ARAILKNNRILIIDEATANVDPrtdELIQQ--KIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDP---ELVGEvlDVMKDLAEegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1022-1226 |
3.19e-14 |
|
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: 73.52 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEigLHDLRKKMSIIPQEPVLFTG-TMRKNLDPFNEHT 1099
Cdd:cd03299 22 VERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITN--LPPEKRDISYVPQNYALFPHmTVYKNIAYGLKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1100 DEElwRALEEVQLKEAIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQ---QKI 1176
Cdd:cd03299 100 KVD--KKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLReelKKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1177 REKFaQCTVLTIAHRLNTI-IDSDKIMVLDSGRLKEYDEPYVLLQNPESLF 1226
Cdd:cd03299 176 RKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
360-552 |
3.25e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.92 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 360 PSDGKAIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPP---ASGLVSVHG---- 430
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGediy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 -----------RIAYVSQQPWVFSGTVRSNILFG--------KKYEKERYEKVIKACAL----KKDLQlledgdltvigD 487
Cdd:COG1117 82 dpdvdvvelrrRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALwdevKDRLK-----------K 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 488 RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD-AEVGKhlfqlcICQALHE---KITI-LVTHQLQ 552
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK------IEELILElkkDYTIvIVTHNMQ 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
386-550 |
3.27e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 386 QGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIayVSQQPWVFsgtvRSNILF-----GKKYEKER 460
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEY----HQDLLYlghqpGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 461 YEKVIKACALKkdlQLLEDGD----LTVIGDRG------ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 530
Cdd:PRK13538 92 LENLRFYQRLH---GPGDDEAlweaLAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170 180
....*....|....*....|
gi 255683324 531 FQLCICQALHEKITILVTHQ 550
Cdd:PRK13538 169 EALLAQHAEQGGMVILTTHQ 188
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
366-572 |
3.38e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.39 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 366 IVHVQDFTAFWDKalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPW----- 440
Cdd:PRK13647 4 IIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 441 ----------VFSGTVRSNILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGAT-LSGGQKARVNL 502
Cdd:PRK13647 82 glvfqdpddqVFSSTVWDDVAFGpvnmgldKDEVERRVEEALKAVRMWD------------FRDKPPYhLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 503 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQlcICQALHE--KITILVTHQLQY-LKAASHILILKDGEMVQKG 572
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
373-579 |
3.40e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 373 TAFWDKALDSptlqgLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQ 437
Cdd:PRK13637 16 TPFEKKALDN-----VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 438 QP--WVFSGTVRSNILFGKK----YEKERYEKVIKACALKKDlqlledgDLTVIGDRGA-TLSGGQKARVNLARAVYQDA 510
Cdd:PRK13637 91 YPeyQLFEETIEKDIAFGPInlglSEEEIENRVKRAMNIVGL-------DYEDYKDKSPfELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 511 DIYLLDDPLSAVDAEVGKHLFQLciCQALHEK---ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLK 579
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
998-1211 |
3.69e-14 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 72.89 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGP--LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDkiltteiG--LHDLRK 1072
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVD-------GepVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEPVLFT-GTMRKN----LDpFNEHTDEELWR----ALEEVQLKEAIEDLPGkmdtELaeSGsnfsvGQRQLVC 1143
Cdd:cd03293 74 DRGYVFQQDALLPwLTVLDNvalgLE-LQGVPKAEAREraeeLLELVGLSGFENAYPH----QL--SG-----GMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1144 LARAILKNNRILIIDEATANVDPRTDELIQQ---KIREKFAQcTVLTIAHRlntiID-----SDKIMVLDS--GRLKE 1211
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEellDIWRETGK-TVLLVTHD----IDeavflADRVVVLSArpGRIVA 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
996-1225 |
3.74e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.66 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTYSLDGPLVLKHL--TALIKSREKVG-IVGRTGAGKSSLISAL--FRLSEPEGKIWIDKILTTEIG---- 1066
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALnnTSLTFKKNKVTcVIGTTGSGKSTMIQLTngLIISETGQTIVGDYAIPANLKkike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1067 LHDLRKKMSIIPQEP--VLFTGTMRKNL--DPFNEHTD-EELWRALEEV-QLKEAIEDLPGKMDTELaesgsnfSVGQRQ 1140
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENkQEAYKKVPELlKLVQLPEDYVKRSPFEL-------SGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1141 LVCLARAILKNNRILIIDEATANVDPRTDE-LIQQKIR-EKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYV 1217
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
....*...
gi 255683324 1218 LLQNPESL 1225
Cdd:PRK13645 238 IFSNQELL 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
997-1208 |
4.08e-14 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 73.58 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGK-IwidKILTTEIG---LHDLR 1071
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNdV---RLFGERRGgedVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1072 KKMSII---------PQEPVL------FTGTmrknLDPFNEHTDEELWRA---LEEVQLKEAIEDLPGKMdtelaesgsn 1133
Cdd:COG1119 78 KRIGLVspalqlrfpRDETVLdvvlsgFFDS----IGLYREPTDEQRERArelLELLGLAHLADRPFGTL---------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1134 fSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIReKFAQ---CTVLTIAHRLNTIIDS-DKIMVLDSGR 1208
Cdd:COG1119 144 -SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLD-KLAAegaPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
381-576 |
4.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.96 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAY--------------VSQQP--WVFS 443
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkksllevrktvgiVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 444 GTVRSNILFGK---KYEKERYEKVIKAcALKKdlqlledgdltvIGDRGAT------LSGGQKARVNLARAVYQDADIYL 514
Cdd:PRK13639 94 PTVEEDVAFGPlnlGLSKEEVEKRVKE-ALKA------------VGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 515 LDDPLSAVDAEVGKHLFQLcicqaLH----EKITILV-THQLQYL-KAASHILILKDGEMVQKGTYTE 576
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKL-----LYdlnkEGITIIIsTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
367-572 |
4.90e-14 |
|
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: 72.31 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFT-AFWDKAldspTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------RIAYVS 436
Cdd:cd03269 1 LEVENVTkRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 437 QQPWVFSG-TVRSNILFgkkyeKERYEKVIKACALKKDLQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYL 514
Cdd:cd03269 77 EERGLYPKmKVIDQLVY-----LAQLKGLKKEEARRRIDEWLERLELSEYANkRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 515 LDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 572
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
996-1209 |
5.28e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.21 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTeigLHDL 1070
Cdd:COG1129 16 GVKALDGVSLE---------------LRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLDgepvRFRSP---RDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEPVL----------FTGTMRKNLDPFNehtdeelWRALEEvQLKEAIEDLpgKMDTELAESGSNFSVGQRQ 1140
Cdd:COG1129 78 AAGIAIIHQELNLvpnlsvaeniFLGREPRRGGLID-------WRAMRR-RARELLARL--GLDIDPDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1141 LVCLARAILKNNRILIIDEATANVDPR-TDELIQQkIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEReVERLFRI-IRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
399-576 |
5.35e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 399 AVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------------IAYVSQQPWVFSG-TVRSNILFG-KKYEKE 459
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLFPHyKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 460 RYEKVIKACALKKdlqLLedgdltvigDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA----EVGKHLFQLc 534
Cdd:PRK11144 108 QFDKIVALLGIEP---LL---------DRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERL- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 255683324 535 icqALHEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTE 576
Cdd:PRK11144 175 ---AREINIPILyVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1013-1209 |
5.35e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 72.40 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1013 LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLhDLRKKMSIIPQEPVLFTG-TMRK 1090
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDaGFATVDGFDVVKEPA-EARRRLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1091 NLDPFNEhtdeelWRALEEVQLKEAIEDLPGKMDTE--LAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRT 1168
Cdd:cd03266 98 NLEYFAG------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255683324 1169 DELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03266 172 TRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
385-547 |
5.76e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 73.15 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 449
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFG-------------------KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQD 509
Cdd:COG0411 100 VLVAaharlgrgllaallrlpraRREEREARERA---------EELLERVGLADRADEPAgNLSYGQQRRLEIARALATE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255683324 510 ADIYLLDDPLSAVDAEVGKHLFQLcIcQALHE--KITILV 547
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAEL-I-RRLRDerGITILL 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
364-587 |
6.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 364 KAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------- 430
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 RIAYVSQQP-WVFSG-TVRSNILFGKKYE----KERYEKVIKAcalkkdLQLLedgDLTVIGDRG-ATLSGGQKARVNLA 503
Cdd:PRK13650 82 KIGMVFQNPdNQFVGaTVEDDVAFGLENKgiphEEMKERVNEA------LELV---GMQDFKEREpARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 504 RAVYQDADIYLLDDPLSAVDAEVGKHLFQlcICQALHEK--ITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIK--TIKGIRDDyqMTVIsITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 255683324 581 GVDFGSL 587
Cdd:PRK13650 231 GNDLLQL 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
385-573 |
8.33e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.34 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQpwvF----SG 444
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraarrKIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILF-----GKKyEKERYEKVikacalkkdLQLLEdgdLTVIGDRG----ATLSGGQKARVNLARAVYQDADIYLL 515
Cdd:COG1135 98 TVAENVALpleiaGVP-KAEIRKRV---------AELLE---LVGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 516 DDPLSAVDAEVGKHLFQLciCQALHEK--ITI-LVTHQLQYLKA-ASHILILKDGEMVQKGT 573
Cdd:COG1135 165 DEATSALDPETTRSILDL--LKDINRElgLTIvLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
367-551 |
8.96e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKAldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------IAYVS 436
Cdd:PRK15056 7 IVVNDVTVTWRNG--HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 437 QQP---WVFSGTVRSNILFGK-------KYEKERYEKVIKACALKKDLQLLEDGDltvIGDrgatLSGGQKARVNLARAV 506
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255683324 507 YQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILV-THQL 551
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISL-LRELRDEGKTMLVsTHNL 202
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
388-580 |
1.07e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 72.56 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 388 LSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPwVFSGTVRSNI---- 450
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrckHIRMIFQDP-NTSLNPRLNIgqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 -----LFGKKYEKERYEKVIKAcaLKKdLQLLEDGDLTVIgdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 525
Cdd:COG4167 111 eeplrLNTDLTAEEREERIFAT--LRL-VGLLPEHANFYP----HMLSSGQKQRVALARALILQPKIIIADEALAALDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 526 VGKHLFQLCIcqALHEKIT---ILVTHQLQYLKAAS-HILILKDGEMVQKGTYTEFLKS 580
Cdd:COG4167 184 VRSQIINLML--ELQEKLGisyIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
385-572 |
1.28e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------------------------RIAYVSQQ 438
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 439 --PWVFSgTVRSNIL--------FGKKYEKERYEKVIKACALKKDLQlledgdltviGDRGATLSGGQKARVNLARAVYQ 508
Cdd:PRK10619 101 fnLWSHM-TVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 509 DADIYLLDDPLSAVDAE-VGKhlfQLCICQALHE--KITILVTHQLQYLK-AASHILILKDGEMVQKG 572
Cdd:PRK10619 170 EPEVLLFDEPTSALDPElVGE---VLRIMQQLAEegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
373-611 |
1.30e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 373 TAFWDKALDSptlqgLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYV 435
Cdd:PRK13641 16 TPMEKKGLDN-----ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 436 SQQP--WVFSGTVRSNILFGKK----YEKERYEKVIKAcaLKKdLQLLEDgdltVIGDRGATLSGGQKARVNLARAVYQD 509
Cdd:PRK13641 91 FQFPeaQLFENTVLKDVEFGPKnfgfSEDEAKEKALKW--LKK-VGLSED----LISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 510 ADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSgvdfGSLL 588
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD----KEWL 239
|
250 260
....*....|....*....|...
gi 255683324 589 KKENeEAEPSTAPGTPTLRKRTF 611
Cdd:PRK13641 240 KKHY-LDEPATSRFASKLEKGGF 261
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
366-583 |
1.33e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.82 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 366 IVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RI 432
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 433 AYVSQQP--WVFSGTVRSNILFGKKYEKERYEKVIKacalKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDA 510
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 511 DIYLLDDPLSAVDAeVGKHLfqlcICQALHE-----KITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVD 583
Cdd:PRK13642 160 EIIILDESTSMLDP-TGRQE----IMRVIHEikekyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
997-1225 |
1.70e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPL-VLKHLTALIKSREKVGIVGRTGAGKSS---LISALFRlsEPEGKIWIDKILTTEIGLHDLRK 1072
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEP-VLFTGTMRKNLDPFNEHTD----EELWRALEEVQLKEAIEDLPGKMDTELaesgsnfSVGQRQLVCLARA 1147
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLAVNMLDFKTREPARL-------SGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1148 ILKNNRILIIDEATANVDP--RTDEL-IQQKIREKFaQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPES 1224
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPtgRQEIMrVIHEIKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
.
gi 255683324 1225 L 1225
Cdd:PRK13642 234 M 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
385-572 |
2.35e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.32 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV--------------HGRIAYVSQQ-PWVFSG----- 444
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQHvGFVFQNfnlfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 --TVRSNILFGKKYEKeryeKVIKACALKKDLQLLEDGDLTviGDRGA---TLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:PRK11264 99 hrTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLA--GKETSyprRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 520 SAVDAE-VGKHLfqLCICQALHEKIT-ILVTHQLQYLK-AASHILILKDGEMVQKG 572
Cdd:PRK11264 173 SALDPElVGEVL--NTIRQLAQEKRTmVIVTHEMSFARdVADRAIFMDQGRIVEQG 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
395-577 |
2.53e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLL----SAVLGELPPASGL------VSVHGRIA-----------YVSQQ-PWVFSGTVRSNILF 452
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIellgrtVQREGRLArdirksrantgYIFQQfNLVNRLSVLENVLI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 453 GKKYEKERYEKVIKACALKKDLQLLEDgdLTVIG------DRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:PRK09984 110 GALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 527 GKHLFQLCICQALHEKITILVT-HQLQY-LKAASHILILKDGEMVQKGTYTEF 577
Cdd:PRK09984 188 ARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
995-1210 |
2.60e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.04 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 995 EGVIVFDNVNFTYSLDG----PLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIG- 1066
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSE--GKVYVDGLDTSDEEn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1067 LHDLRKKMSIIPQEP------------VLFTgtmRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMdtelaeSGsnf 1134
Cdd:PRK13633 80 LWDIRNKAGMVFQNPdnqivativeedVAFG---PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL------SG--- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1135 svGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLK 1210
Cdd:PRK13633 148 --GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
998-1221 |
3.23e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYsldgplvlKHL----TALIKSREKVGIVGRTGAGKSSLIS--ALFrLSEPEGKIWIDKILTTEIGlhDLR 1071
Cdd:PRK10771 2 LKLTDITWLY--------HHLpmrfDLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQDHTTTP--PSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1072 KKMSIIPQEPVLFTG-TMRKN----LDP---FNEHTDEELWRALEEVQLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVC 1143
Cdd:PRK10771 71 RPVSMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL------SG-----GQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1144 LARAILKNNRILIIDEATANVDP--RTD--ELIQQKIREKfaQCTVLTIAHRLNtiiDSDKI----MVLDSGRLkEYDEP 1215
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPalRQEmlTLVSQVCQER--QLTLLMVSHSLE---DAARIaprsLVVADGRI-AWDGP 213
|
....*.
gi 255683324 1216 YVLLQN 1221
Cdd:PRK10771 214 TDELLS 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
385-573 |
3.70e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELpPASGLVSVHGRI-------------AYVSQQ-PWVFSGTVRSNI 450
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwsaaelarhrAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 -LFGkkYEKERYEKVIKACAlkkdlQLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQ-------DADIYLLDDPLSA 521
Cdd:COG4138 91 aLHQ--PAGASSEAVEQLLA-----QLAEALGLEDKLSRPLTqLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 522 VD----AEVGKHLFQLCICQalhekITILV-THQLQY-LKAASHILILKDGEMVQKGT 573
Cdd:COG4138 164 LDvaqqAALDRLLRELCQQG-----ITVVMsSHDLNHtLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1030-1222 |
3.93e-13 |
|
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: 71.14 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1030 IVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL----RKKMSIIPQEPVLFTG-TMRKN----LDPFNEHT 1099
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPtSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLENvafgLEVQGVPR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1100 DEELWRA---LEEVQLKEAIEDLPGkmdtELaeSGsnfsvGQRQLVCLARAILKNNRILIIDEATANVDP--RT---DEL 1171
Cdd:cd03294 135 AEREERAaeaLELVGLEGWEHKYPD----EL--SG-----GMQQRVGLARALAVDPDILLMDEAFSALDPliRRemqDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 255683324 1172 IQ-QKIREKfaqcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNP 1222
Cdd:cd03294 204 LRlQAELQK----TIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
385-570 |
4.19e-13 |
|
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: 70.16 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------------RIAYVSqqpWVF-------S 443
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararlRARHVG---FVFqsfqllpT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 444 GTVRSNI-----LFGKKYEKERYEKVIKACALkkdlqlledgdltviGDRG----ATLSGGQKARVNLARAVYQDADIYL 514
Cdd:COG4181 105 LTALENVmlpleLAGRRDARARARALLERVGL---------------GHRLdhypAQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 515 LDDPLSAVDAEVGKH----LFQLcicQALHEKITILVTHQLQYLKAASHILILKDGEMVQ 570
Cdd:COG4181 170 ADEPTGNLDAATGEQiidlLFEL---NRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1004-1216 |
4.85e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKiltteiglhdlRKKMSIIPQEPV 1082
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPK-----------GLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 LFTG-TMRKNLdpfnEHTDEELWRALEEvqlKEAIEDLPGKMDTELAESG------------------------------ 1131
Cdd:COG0488 72 LDDDlTVLDTV----LDGDAELRALEAE---LEELEAKLAEPDEDLERLAelqeefealggweaearaeeilsglgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1132 ------SNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRT-----DELIQQKirekfaqCTVLTIAH-R--LNTIid 1197
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNYP-------GTVLVVSHdRyfLDRV-- 215
|
250
....*....|....*....
gi 255683324 1198 SDKIMVLDSGRLKEYDEPY 1216
Cdd:COG0488 216 ATRILELDRGKLTLYPGNY 234
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
718-970 |
5.45e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 71.00 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18563 42 LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIPW----ILIPlVPLsVVFLVlrRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRA 873
Cdd:cd18563 122 PDFLTNILMIIGIGVVLFSLNWKlallVLIP-VPL-VVWGS--YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 874 YKAEER--------CQELFDAHQDLHSeawflflTTSRWFAVrLDAICAIFVIVVAF--GSLVLAKTLNAGQVGLALSYa 943
Cdd:cd18563 198 FGQEKReikrfdeaNQELLDANIRAEK-------LWATFFPL-LTFLTSLGTLIVWYfgGRQVLSGTMTLGTLVAFLSY- 268
|
250 260 270
....*....|....*....|....*....|.
gi 255683324 944 ltlMGMF----QWSVRQSAEVENMMISVERV 970
Cdd:cd18563 269 ---LGMFygplQWLSRLNNWITRALTSAERI 296
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
381-548 |
9.03e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.60 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQqpwvFSG---- 444
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQ----FDNldpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 -TVRSNIL-FGkkyekeRYEKVIKACALKKDLQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSA 521
Cdd:PRK13537 95 fTVRENLLvFG------RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180
....*....|....*....|....*..
gi 255683324 522 VDAEvGKHLFQLCICQALHEKITILVT 548
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARGKTILLT 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1004-1215 |
1.03e-12 |
|
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: 72.14 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLS--EP-EGKI-----------WID----------- 1058
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPtSGRIiyhvalcekcgYVErpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1059 ---KILTTEIGL--------HDLRKKMSIIPQEPVLFTGTMR------KNLDPFNEHTDEELWRA---LEEVQLKEAIed 1118
Cdd:TIGR03269 85 cggTLEPEEVDFwnlsdklrRRIRKRIAIMLQRTFALYGDDTvldnvlEALEEIGYEGKEAVGRAvdlIEMVQLSHRI-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1119 lpgkmdTELAEsgsNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTII 1196
Cdd:TIGR03269 163 ------THIAR---DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|
gi 255683324 1197 D-SDKIMVLDSGRLKEYDEP 1215
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTP 253
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
350-602 |
1.13e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 350 DELPQRKAHVPSDGKAIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH 429
Cdd:PRK11607 3 DAIPRPQAKTRKALTPLLEIRNLTKSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 430 GR-IAYVS--QQP--WVFSG-------TVRSNILFGKKyeKERYEKVIKACALKKDLQLLEDGDLTviGDRGATLSGGQK 497
Cdd:PRK11607 80 GVdLSHVPpyQRPinMMFQSyalfphmTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 498 ARVNLARAVYQDADIYLLDDPLSAVDAEVgKHLFQLCICQALhEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGT 573
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLEVVDIL-ERVgvtCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 255683324 574 ------------YTEFLKSGVDFGSLLKKENEEAEPSTAPG 602
Cdd:PRK11607 234 peeiyehpttrySAEFIGSVNVFEGVLKERQEDGLVIDSPG 274
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
435-578 |
1.15e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 435 VSQQPWVFSGTVRSNILFGKkyEKERYEKVIKAC---ALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDAD 511
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 512 IYLLDDPLSAVDAEVGKHLFQLCI-CQALHEKITILVTHQLQYLKAASHILIL----KDGEMVQ-KGTYTEFL 578
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
995-1213 |
1.31e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.71 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 995 EGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlrkk 1073
Cdd:cd03220 33 GEFWALKDVSFE---------------VPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRGRVSSLLGLG----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQ----EPVLFTGTMrKNLDPfnehtdEELWRALEEV----QLKEAIeDLPGKmdtelaesgsNFSVGQRQLVCLA 1145
Cdd:cd03220 93 GGFNPEltgrENIYLNGRL-LGLSR------KEIDEKIDEIiefsELGDFI-DLPVK----------TYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1146 RAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQC-TVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1213
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
998-1226 |
1.77e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.49 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIGLHDlRKkM 1074
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmIAGLEDPTS--GEILIGGRDVTDLPPKD-RN-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLF-TGTMRKNL---------DPfnEHTDEELWRALEEVQLKEAIEDLPGkmdtELaeSGsnfsvGQRQLVCL 1144
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIafplklrkvPK--AEIDRRVREAAELLGLEDLLDRKPK----QL--SG-----GQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1145 ARAILKNNRILIIDEATANVDP------RTdELiqQKIREKFAQCTV---------LTIAhrlntiidsDKIMVLDSGRL 1209
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAklrvemRA-EI--KRLHRRLGTTTIyvthdqveaMTLA---------DRIAVMNDGRI 212
|
250
....*....|....*..
gi 255683324 1210 KEYDEPYVLLQNPESLF 1226
Cdd:COG3839 213 QQVGTPEELYDRPANLF 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1014-1223 |
1.84e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL--------SEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLF- 1084
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneearVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1085 ---------TGTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDlpgkmdtELAESGSNFSVGQRQLVCLARAILKNNRIL 1155
Cdd:PRK14267 99 hltiydnvaIGVKLNGLVKSKKELDERVEWALKKAALWDEVKD-------RLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1156 IIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHR-LNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPE 1223
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1014-1190 |
2.10e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.79 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE--PE----GKIWIDKILTTEIGLHDLRKKMSIIPQEP------ 1081
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1082 VLFT----GTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDlpgkmdtELAESGSNFSVGQRQLVCLARAILKNNRILII 1157
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|...
gi 255683324 1158 DEATANVDPRTDELIQQKIREKFAQCTVLTIAH 1190
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
349-569 |
2.31e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 349 LDELPQRKAHVPsdGKAIVHVQDFTAfwdkaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV 428
Cdd:COG1129 241 LEDLFPKRAAAP--GEVVLEVEGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 429 HGR--------------IAYVS----QQPWVFSGTVRSNI------------LFGKKYEKERYEKVIKACALKkdlqlLE 478
Cdd:COG1129 312 DGKpvrirsprdairagIAYVPedrkGEGLVLDLSIRENItlasldrlsrggLLDRRRERALAEEYIKRLRIK-----TP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 479 DGDLTVigdrgATLSGG--QKarVNLARAVYQDADIYLLDDPLSAVDaeVG-KH-LFQLcICQALHEKITILV-THQLQY 553
Cdd:COG1129 387 SPEQPV-----GNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGID--VGaKAeIYRL-IRELAAEGKAVIViSSELPE 456
|
250
....*....|....*..
gi 255683324 554 LKAASH-ILILKDGEMV 569
Cdd:COG1129 457 LLGLSDrILVMREGRIV 473
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1223 |
2.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.49 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1030 IVGRTGAGKSSLISALFRLSEPE-GKIWIDKI---------------LTTEI-GLHDLRKKMSIIPQEP--VLFTGTMRK 1090
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKyGTIQVGDIyigdkknnhelitnpYSKKIkNFKELRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1091 NL--DPFN--EHTDEELWRA---LEEVQLKeaiedlpgkmDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATAN 1163
Cdd:PRK13631 137 DImfGPVAlgVKKSEAKKLAkfyLNKMGLD----------DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1164 VDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPE 1223
Cdd:PRK13631 207 LDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1013-1223 |
3.10e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1013 LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE------PEGKI-WIDK-ILTTEIGLHDLRKKMSIIPQEPVLF 1084
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfrVEGKVtFHGKnLYAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1085 TGTMRKNL------DPFNEHTDEELWRALEEVQLKEAIEDlpgkmdtELAESGSNFSVGQRQLVCLARAILKNNRILIID 1158
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1159 EATANVDPRTDELIQQKIREKFAQCTVLTIAHRL-------------NTIIDSDKIMVldsGRLKEYDEPYVLLQNPE 1223
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqqaarvsdmtaffNVELTEGGGRY---GYLVEFDRTEKIFNSPQ 251
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
364-579 |
3.65e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 364 KAIVHVQDFTAFWD-KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV---------------- 426
Cdd:PRK13651 6 KNIVKIFNKKLPTElKALD-----NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 427 ---------------------SVHGRIAYVSQ--QPWVFSGTVRSNILFG-------KKYEKERYEKVIKACALkkDLQL 476
Cdd:PRK13651 81 ekvleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 477 LEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLfqLCICQALHE--KITILVTHQLQY- 553
Cdd:PRK13651 159 LQRSPFE--------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI--LEIFDNLNKqgKTIILVTHDLDNv 228
|
250 260 270
....*....|....*....|....*....|..
gi 255683324 554 LKAASHILILKDGEMVQKG-TY-----TEFLK 579
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGdTYdilsdNKFLI 260
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
383-572 |
4.10e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 67.36 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIayvsqqPWVFSGTVRSNI--LFGKK----- 455
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKtqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 456 --------------Y--EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRgaTLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:cd03267 109 dlpvidsfyllaaiYdlPPARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 520 SAVDA----EVGKHLFQLCicqALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 572
Cdd:cd03267 182 IGLDVvaqeNIRNFLKEYN---RERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
997-1225 |
4.39e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPLVLKHLTAL---IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG----LH 1068
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIdleVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1069 DLRKKMSIIPQEP--VLFTGTMRKNL--DPFN-----EHTDEELWRALEEVQL-KEAIEDLPGKMdtelaesgsnfSVGQ 1138
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVafGPQNfgipkEKAEKIAAEKLEMVGLaDEFWEKSPFEL-----------SGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1139 RQLVCLARAILKNNRILIIDEATANVDPRTdELIQQKIREKFAQC--TVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1215
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKA-RIEMMQLFESIHQSgqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
250
....*....|
gi 255683324 1216 YVLLQNPESL 1225
Cdd:PRK13643 229 SDVFQEVDFL 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
997-1211 |
4.91e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.06 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-LTT--EIGLHDL 1070
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPtSGRVLVDGQdLTAlsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQE---------------PVLFTGTMRKNLDPfnehTDEELwraLEEVQLKEAIEDLPgkmdtelaesgSNFS 1135
Cdd:PRK11153 81 RRQIGMIFQHfnllssrtvfdnvalPLELAGTPKAEIKA----RVTEL---LELVGLSDKADRYP-----------AQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1136 VGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQ---KIREKFAqCTVLTIAHRLNTI--IdSDKIMVLDSGRLK 1210
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEllkDINRELG-LTIVLITHEMDVVkrI-CDRVAVIDAGRLV 220
|
.
gi 255683324 1211 E 1211
Cdd:PRK11153 221 E 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
385-576 |
4.99e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQP--WVFSGTVRSN 449
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSA 521
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEE------------LRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 522 VDAEVGKHLFQLciCQALHEK---ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTE 576
Cdd:PRK13652 168 LDPQGVKELIDF--LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
385-582 |
5.22e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQ-PWVFSGTVRSNI 450
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGK-----------KYEKERYEKVIKACALKKDLQLLEDgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:PRK10575 107 AIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 520 SAVDaeVGKHLFQLCICQALHEKITILVTHQLQYLKAAS----HILILKDGEMVQKGTYTEFLKSGV 582
Cdd:PRK10575 176 SALD--IAHQVDVLALVHRLSQERGLTVIAVLHDINMAArycdYLVALRGGEMIAQGTPAELMRGET 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
998-1208 |
6.24e-12 |
|
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: 64.39 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILtteiglhdlrkKMSI 1076
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPdEGIVTWGSTV-----------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQepvlftgtmrknldpfnehtdeelwraleevqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKNNRILI 1156
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1157 IDEATANVDPRTDELIQQKIREKfaQCTVLTIAH-R--LNTIIdsDKIMVLDSGR 1208
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1014-1178 |
7.46e-12 |
|
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: 66.41 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHD-LRKKMSIIPQEPVLFTG-TMRK 1090
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1091 NLDPFNEHTdeELWRALEEVQLKEAIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDE 1170
Cdd:cd03218 95 NILAVLEIR--GLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
....*...
gi 255683324 1171 LIQQKIRE 1178
Cdd:cd03218 171 DIQKIIKI 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
384-581 |
8.26e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.08 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 384 TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASG-------------LVSVHGRIAYVSQQP---WVFSgTVR 447
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnFEKLRKHIGIVFQNPdnqFVGS-IVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFGKKYEKERYEKVIKACAlkkdlQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVS-----EALKQVDMLERADyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 527 GKHLFQLCICQALHEKITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
383-576 |
1.02e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.95 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQ----PWVfsgTVR 447
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyalyPHM---SVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFG---KKYEKERYEKVIKACAlkkdlQLLEDGDLTvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PRK11650 95 ENMAYGlkiRGMPKAEIEERVAEAA-----RILELEPLL---DRKpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 524 AevgKHLFQLCI-CQALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 576
Cdd:PRK11650 167 A---KLRVQMRLeIQRLHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
381-568 |
1.05e-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: 65.89 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------RIAYVSQQ-PWVFSG------ 444
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKiGVVFQDfrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 -TVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:cd03292 93 rNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHK----HRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 524 AEVGKHLFQLciCQALHEK-ITILV-THQLQYLKAASH-ILILKDGEM 568
Cdd:cd03292 169 PDTTWEIMNL--LKKINKAgTTVVVaTHAKELVDTTRHrVIALERGKL 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
367-594 |
1.13e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKALDSPTLQGLSFIarpgellavvGPVGAGKSSLLSAV--LGELPP---ASGLVSVHG----------- 430
Cdd:PRK14243 18 VYYGSFLAVKNVWLDIPKNQITAFI----------GPSGCGKSTILRCFnrLNDLIPgfrVEGKVTFHGknlyapdvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 ----RIAYVSQQPWVFSGTVRSNILFGKK---YE---KERYEKVIKACAL----KKDLQlledgdltvigDRGATLSGGQ 496
Cdd:PRK14243 88 evrrRIGMVFQKPNPFPKSIYDNIAYGARingYKgdmDELVERSLRQAALwdevKDKLK-----------QSGLSLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 497 KARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALHEKITI-LVTHQLQYLKAASHILILKDGEMVQKGTYT 575
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEEL--MHELKEQYTIiIVTHNMQQAARVSDMTAFFNVELTEGGGRY 234
|
250 260
....*....|....*....|...
gi 255683324 576 ----EFLKSGVDFGSLLKKENEE 594
Cdd:PRK14243 235 gylvEFDRTEKIFNSPQQQATRD 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1014-1208 |
1.17e-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: 65.38 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTTEIGLH--------DLRKKMSIIPQepVL 1083
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDgKPLDIAARNRigylpeerGLYPKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1084 FTGTMrKNLDPfnEHTDEELWRALEEVQL----KEAIEDLpgkmdtelaesgsnfSVGQRQLVCLARAILKNNRILIIDE 1159
Cdd:cd03269 93 YLAQL-KGLKK--EEARRRIDEWLERLELseyaNKRVEEL---------------SKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1160 ATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGR 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
382-573 |
1.30e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 382 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWV-FSG-T 445
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNPETqFVGrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 446 VRSNILFGKKyekeryekviKACALKKDLQLLEDGDLTVIG------DRGATLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:PRK13644 95 VEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 520 SAVDAEVGKHLFQLciCQALHE--KITILVTHQLQYLKAASHILILKDGEMVQKGT 573
Cdd:PRK13644 165 SMLDPDSGIAVLER--IKKLHEkgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
385-607 |
1.35e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 449
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGKkyEKER-----YEKVIKACAlkkdlQLLEDGDLTV-IGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSA-V 522
Cdd:COG1129 100 IFLGR--EPRRgglidWRAMRRRAR-----ELLARLGLDIdPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASlT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 523 DAEVgKHLFQlcICQALHEK-ITIL-VTHQLQYLKA-ASHILILKDGEMVqkgtyTEFLKSGVDFGSLLKK------ENE 593
Cdd:COG1129 173 EREV-ERLFR--IIRRLKAQgVAIIyISHRLDEVFEiADRVTVLRDGRLV-----GTGPVAELTEDELVRLmvgrelEDL 244
|
250
....*....|....
gi 255683324 594 EAEPSTAPGTPTLR 607
Cdd:COG1129 245 FPKRAAAPGEVVLE 258
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1013-1222 |
1.39e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.14 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1013 LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLR----KKMSIIPQEPVLFTGT 1087
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPtRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1088 MRKNLDPFN--------EHTDEELWRALEEVQLKEAIEDLPGKMdtelaesgsnfSVGQRQLVCLARAILKNNRILIIDE 1159
Cdd:PRK10070 122 TVLDNTAFGmelaginaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1160 ATANVDP--RT---DELIQQKIREkfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNP 1222
Cdd:PRK10070 191 AFSALDPliRTemqDELVKLQAKH---QRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
354-573 |
1.41e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 354 QRKAHVPSD--GKAIVHVQDFTAFWDKALDSP--TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH 429
Cdd:PRK13631 7 KKKLKVPNPlsDDIILRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 430 G-----------------------------RIAYVSQQP--WVFSGTVRSNILFG------KKYE-KERYEKVIKACALK 471
Cdd:PRK13631 87 DiyigdkknnhelitnpyskkiknfkelrrRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 472 KDLqlLEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQL 551
Cdd:PRK13631 167 DSY--LERSPFG--------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM 236
|
250 260
....*....|....*....|...
gi 255683324 552 -QYLKAASHILILKDGEMVQKGT 573
Cdd:PRK13631 237 eHVLEVADEVIVMDKGKILKTGT 259
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
708-970 |
1.54e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 66.72 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 708 ANGNITetlDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIG 787
Cdd:cd18545 32 PNGDLS---GLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 788 HMDDLLPLTFLDFI-QTLLLVvsviavaaavipWILI---------PLVPLSV--VFLVLRRYFLETSRDVKRLESTTRS 855
Cdd:cd18545 109 SLSDLLSNGLINLIpDLLTLV------------GIVIimfslnvrlALVTLAVlpLLVLVVFLLRRRARKAWQRVRKKIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 856 PVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWflfLTTSR-----WFAVRLDAICAIFVIVVAFGSLVLAKT 930
Cdd:cd18545 177 NLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKAN---MRAVRlnalfWPLVELISALGTALVYWYGGKLVLGGA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255683324 931 LNAGQVGLALSYaltlMGMFQWSVRQSAEVENMMISV----ERV 970
Cdd:cd18545 254 ITVGVLVAFIGY----VGRFWQPIRNLSNFYNQLQSAmasaERI 293
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
996-1209 |
1.68e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 65.54 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDlRKKM 1074
Cdd:cd03219 12 GLVALDDVSFS---------------VRPGEIHGLIGPNGAGKTTLFNLISGFLRPtSGSVLFDGEDITGLPPHE-IARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIP--QEPVLFTG-TMRKNLD----PFNEHTDEELWRALEEVQLKEAIED------LPGKMDtELAesgSNFSVGQRQL 1141
Cdd:cd03219 76 GIGRtfQIPRLFPElTVLENVMvaaqARTGSGLLLARARREEREARERAEEllervgLADLAD-RPA---GELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1142 VCLARAILKNNRILIIDEATANVDPR-TDELIQ--QKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEeTEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
385-614 |
1.72e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.60 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSaVLGEL-PPASGLVSVHGR-----------------IAYVSQQPWVFSG-T 445
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQdvatldadalaqlrrehFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 446 VRSNILFGKKYE-KERYEKVIKACALKKDLQLLEDgdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:PRK10535 103 AAQNVEVPAVYAgLERKQRLLRAQELLQRLGLEDR-----VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 525 EVGKHLfqLCICQALHEK--ITILVTHQLQYLKAASHILILKDGEMVQkgtyteflksgvDFGSLLKKENEEAEPSTAPG 602
Cdd:PRK10535 178 HSGEEV--MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIVR------------NPPAQEKVNVAGGTEPVVNT 243
|
250
....*....|....
gi 255683324 603 TPTLRKRT--FSEA 614
Cdd:PRK10535 244 ASGWRQFVsgFREA 257
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
990-1208 |
1.81e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 990 PGWPHEgVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIG 1066
Cdd:COG1101 13 PGTVNE-KRALDGLNLT---------------IEEGDFVTVIGSNGAGKSTLlnaIAGSLPPDS--GSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1067 LHDLRKKMSIIPQEPVLFT-GTM--------------RKNLDPFNEHTDEELWRA-LEEVQLkeaieDLPGKMDTELaes 1130
Cdd:COG1101 75 EYKRAKYIGRVFQDPMMGTaPSMtieenlalayrrgkRRGLRRGLTKKRRELFRElLATLGL-----GLENRLDTKV--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1131 gSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELI----QQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLD 1205
Cdd:COG1101 147 -GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTHNMEQALDyGNRLIMMH 223
|
...
gi 255683324 1206 SGR 1208
Cdd:COG1101 224 EGR 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
997-1211 |
2.01e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.15 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSL-DGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDL 1070
Cdd:COG4181 8 IIELRGLTKTVGTgAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAgQDLFAldEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 R-KKMSIIPQ-EPVLFTGTMRKNL----------DPFNEHTDEelwraLEEVQLKEAIEDLPGKMdtelaeSGsnfsvGQ 1138
Cdd:COG4181 88 RaRHVGFVFQsFQLLPTLTALENVmlplelagrrDARARARAL-----LERVGLGHRLDHYPAQL------SG-----GE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1139 RQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1211
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
996-1215 |
2.28e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVI-VFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI----DKILTTEIGLhD 1069
Cdd:TIGR03269 295 GVVkAVDNVSLE---------------VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPtSGEVNVrvgdEWVDMTKPGP-D 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1070 LR----KKMSIIPQEPVLFTgtMRKNLDPFNEHTDEELwraLEEVQLKEAIEDLpgKM---DTELAES-----GSNFSVG 1137
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYP--HRTVLDNLTEAIGLEL---PDELARMKAVITL--KMvgfDEEKAEEildkyPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1138 QRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKI---REKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1213
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
..
gi 255683324 1214 EP 1215
Cdd:TIGR03269 511 DP 512
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
999-1190 |
2.65e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 64.76 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 999 VFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-----LTT--EIGLHDL 1070
Cdd:COG4778 26 VLDGVSFS---------------VAAGECVALTGPSGAGKSTLLKCIYGNYLPdSGSILVRHDggwvdLAQasPREILAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKK--------MSIIPQ--------EPVLFTGTMRknldpfnehtDEELWRA---LEEVQLKEAIEDLPgkmdtelaesG 1131
Cdd:COG4778 91 RRRtigyvsqfLRVIPRvsaldvvaEPLLERGVDR----------EEARARArelLARLNLPERLWDLP----------P 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1132 SNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAH 1190
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFH 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
388-578 |
2.70e-11 |
|
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: 67.65 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 388 LSFIarPGELLAVVGPVGAGKSSLL-------SAVLGELPPASGLvsvhgRIAYVSQQPWV-FSGTVRSNILFG------ 453
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 454 --KKY-------------------EKERYEKVIKAC-ALKKDLQL--------LEDGDLTVigdrgATLSGGQKARVNLA 503
Cdd:TIGR03719 99 alDRFneisakyaepdadfdklaaEQAELQEIIDAAdAWDLDSQLeiamdalrCPPWDADV-----TKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 504 RAVYQDADIYLLDDPLSAVDAE----VGKHL--FQLCIcqalhekitILVTHQLQYL-KAASHILILKDGEMVQ-KGTYT 575
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAEsvawLERHLqeYPGTV---------VAVTHDRYFLdNVAGWILELDRGRGIPwEGNYS 244
|
...
gi 255683324 576 EFL 578
Cdd:TIGR03719 245 SWL 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
383-525 |
2.83e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 64.76 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH---------------------GRIAYVSQ---- 437
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 438 -----------QPWVFSGTvrsnilfgkkyekERYEKVIKACALKKDLQLLEdgdltvigdR-----GATLSGGQKARVN 501
Cdd:COG4778 105 iprvsaldvvaEPLLERGV-------------DREEARARARELLARLNLPE---------RlwdlpPATFSGGEQQRVN 162
|
170 180
....*....|....*....|....
gi 255683324 502 LARAVYQDADIYLLDDPLSAVDAE 525
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAA 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1007-1211 |
2.98e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.74 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1007 YSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFT 1085
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPtSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1086 GTMRKNLD-PF---NEHTDEELWRA------LEEVQLKEAIEDLPGkmdtelaesgsnfsvGQRQLVCLARAILKNNRIL 1155
Cdd:PRK10247 95 DTVYDNLIfPWqirNQQPDPAIFLDdlerfaLPDTILTKNIAELSG---------------GEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1156 IIDEATANVDP----RTDELIQQKIREKfaQCTVLTIAHRLNTIIDSDKIMVLDS--GRLKE 1211
Cdd:PRK10247 160 LLDEITSALDEsnkhNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITLQPhaGEMQE 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
385-575 |
3.37e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.84 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPWV---FSG 444
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLlpdFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 --TVRSNILFGKKYEKERYEK---VIKACALKKDLQlledgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:PRK11629 105 leNVAMPLLIGKKKPAEINSRaleMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 520 SAVDAEVGKHLFQLC-ICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYT 575
Cdd:PRK11629 174 GNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
385-550 |
3.90e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPAS--GLVSVHG---------RIAYVSQQPWVFSG-TVRSNILF 452
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 453 ------GKKYEKEryEKVIKACALKKDLQLLEDGDlTVIGD---RGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PLN03211 164 csllrlPKSLTKQ--EKILVAESVISELGLTKCEN-TIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*..
gi 255683324 524 AEVGKHLFQLCICQALHEKITILVTHQ 550
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
998-1226 |
4.12e-11 |
|
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: 64.57 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlRKKMSI 1076
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPtSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1077 IPQEPVLFT----------GTMRKNLDPfnEHTDEELWRALEEVQLkeaiEDLPGKMDTELaeSGsnfsvGQRQLVCLAR 1146
Cdd:cd03300 77 VFQNYALFPhltvfeniafGLRLKKLPK--AEIKERVAEALDLVQL----EGYANRKPSQL--SG-----GQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1147 AILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAH-RLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPE 1223
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
...
gi 255683324 1224 SLF 1226
Cdd:cd03300 224 NRF 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
999-1224 |
4.53e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 999 VFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KIL-----TTEIGLHDLR 1071
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDgKVLyfgkdIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1072 KKMSIIPQEPVLFTG-TMRKNLD-PFNEH---TDEELWRALEEVQLKEAiedLPGKMDTELAESGSNFSVGQRQLVCLAR 1146
Cdd:PRK14246 90 KEVGMVFQQPNPFPHlSIYDNIAyPLKSHgikEKREIKKIVEECLRKVG---LWKEVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1147 AILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPES 1224
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1022-1208 |
4.86e-11 |
|
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: 63.99 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIW-----IDKILTTEIglhdLRKKMSIIPQEPVLFTG-TMRKNLD- 1093
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRfdgrdITGLPPHER----ARAGIGYVPEGRRIFPElTVEENLLl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1094 -PFNEHTDEELWRaLEEV-----QLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVCLARAILKNNRILIIDEATANVDPR 1167
Cdd:cd03224 99 gAYARRRAKRKAR-LERVyelfpRLKERRKQLAGTL------SG-----GEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255683324 1168 TDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:cd03224 167 IVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGR 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
377-580 |
5.13e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.21 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 377 DKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQP 439
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 440 WVFSG-TVRSNILFGKKYE----KERYEKVIKAcalkkdlqLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYL 514
Cdd:PRK10070 116 ALMPHmTVLDNTAFGMELAginaEERREKALDA--------LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 515 LDDPLSAVDAEVGKHLF-QLCICQALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1014-1211 |
5.58e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKI-WIDKILTT-------------------EIGLHDLRK 1072
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPsQGNVsWRGEPLAKlnraqrkafrrdiqmvfqdSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEPvlftgtMRK--NLDPFN-EHTDEELwraLEEVQLKEAIED-LPGKMdtelaeSGsnfsvGQRQLVCLARAI 1148
Cdd:PRK10419 107 TVREIIREP------LRHllSLDKAErLARASEM---LRAVDLDDSVLDkRPPQL------SG-----GQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1149 LKNNRILIIDEATANVDPRTD-ELIQQ--KIREKFAQCTVLtIAHRLNTIID-SDKIMVLDSGRLKE 1211
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQaGVIRLlkKLQQQFGTACLF-ITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
393-567 |
6.51e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.97 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 393 RPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-RIAYVSQQPWV-FSGTVRSnILFGK---KYEKERYEKVIKa 467
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD-LLSSItkdFYTHPYFKTEIA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 468 calkKDLQL--LEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VGKHLfqlcicqA 538
Cdd:cd03237 101 ----KPLQIeqILDREVP-------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaskVIRRF-------A 162
|
170 180 190
....*....|....*....|....*....|
gi 255683324 539 LHEKITILVT-HQLQYLKAASHILILKDGE 567
Cdd:cd03237 163 ENNEKTAFVVeHDIIMIDYLADRLIVFEGE 192
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
997-1219 |
7.11e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.37 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMS 1075
Cdd:PRK13647 4 IIEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQrGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEP--VLFTGTMRKNL--DPFN-EHTDEELWRALEEVQLKEAIEDLPGKMDTELaesgsnfSVGQRQLVCLARAILK 1150
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVafGPVNmGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-------SYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1151 NNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIA-HRLNTIID-SDKIMVLDSGRLKEYDEPYVLL 1219
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
997-1228 |
7.80e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDK--ILTTEIGLHDLRKK 1073
Cdd:PRK13636 5 ILKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPsSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQEP--VLFTGTMRKNLD--PFNEHTDE-ELWRALEEVQLKEAIEDLPGKMDTELaesgsnfSVGQRQLVCLARAI 1148
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSfgAVNLKLPEdEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1149 LKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTI-IDSDKIMVLDSGRLkeydepyVLLQNPESL 1225
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGRV-------ILQGNPKEV 229
|
...
gi 255683324 1226 FYK 1228
Cdd:PRK13636 230 FAE 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
395-581 |
8.85e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.42 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQP--WVFSGTVRSNILFGKK 455
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFPesQLFEDTVEREIIFGPK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 456 YEKERYEKViKACALKKDLQLLEDGDltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCI 535
Cdd:PRK13646 113 NFKMNLDEV-KNYAHRLLMDLGFSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 536 -CQALHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSG 581
Cdd:PRK13646 190 sLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1003-1194 |
9.19e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 62.76 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1003 VNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGkiwiDKILTTEIGLHDLRKkmsiIPQEPV 1082
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS----GEVRWNGTPLAEQRD----EPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 LFTG---------TMRKNLD---PFNEHTDEELWRALEEVQLKeAIEDLPGkmdtelaesgSNFSVGQRQLVCLARAILK 1150
Cdd:TIGR01189 76 LYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLT-GFEDLPA----------AQLSAGQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255683324 1151 NNRILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNT 1194
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAHLARggIVLLTTHQDLGL 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
996-1208 |
9.48e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSL---ISALFRLSEPEGKIWID-------KILTTEi 1065
Cdd:PRK13549 17 GVKALDNVSLK---------------VRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTYEGEIIFEgeelqasNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1066 glhdlRKKMSIIPQEPVLFTG-TMRKNLDPFNEHT-------DEELWRA---LEEVQLkeaiedlpgkmDTELAESGSNF 1134
Cdd:PRK13549 81 -----RAGIAIIHQELALVKElSVLENIFLGNEITpggimdyDAMYLRAqklLAQLKL-----------DINPATPVGNL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1135 SVGQRQLVCLARAILKNNRILIIDEATANV-DPRTDEL--IQQKIREKFAQCtvLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVLldIIRDLKAHGIAC--IYISHKLNEVKAiSDTICVIRDGR 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1026-1224 |
1.01e-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: 65.86 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1026 EKVGIVGRTGAGKSSLISALFRLSEPEGKIWID--KILT-TEIGLHDLRKKMSIIPQEP-------------------VL 1083
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDgqDLDGlSRRALRPLRRRMQVVFQDPfgslsprmtvgqiiaeglrVH 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1084 FTGtmrknLDPfnEHTDEELWRALEEVQLKEAIedlpgkMD---TElaesgsnFSVGQRQLVCLARAILKNNRILIIDEA 1160
Cdd:COG4172 393 GPG-----LSA--AERRARVAEALEEVGLDPAA------RHrypHE-------FSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1161 TANVDpRTdelIQQKIREKFA------QCTVLTIAHRLNTI--IdSDKIMVLDSGRLKEYDEPYVLLQNPES 1224
Cdd:COG4172 453 TSALD-VS---VQAQILDLLRdlqrehGLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
998-1226 |
1.17e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 64.73 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWID-KILTteiglhDL--- 1070
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLlrmIAGFETPDS--GRILLDgRDVT------GLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEPVLF---T-------GTMRKNLDPfnEHTDEELWRALEEVQLkeaiEDLPGKMDTELaeSGsnfsvGQRQ 1140
Cdd:COG3842 76 KRNVGMVFQDYALFphlTvaenvafGLRMRGVPK--AEIRARVAELLELVGL----EGLADRYPHQL--SG-----GQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1141 LVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREkfaqctvltIAHRLN-TII----D-------SDKIMVLDSGR 1208
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRR---------LQRELGiTFIyvthDqeealalADRIAVMNDGR 213
|
250
....*....|....*...
gi 255683324 1209 LKEYDEPYVLLQNPESLF 1226
Cdd:COG3842 214 IEQVGTPEEIYERPATRF 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
395-578 |
1.21e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQ----------QPWVFSGTVRSNIL 451
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQnattpgditvQELVARGRYPHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 452 FgKKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 530
Cdd:PRK10253 113 F-TRWRKEDEEAVTKA---------MQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 531 FQLcICQALHEKITIL--VTHQL-QYLKAASHILILKDGEMVQKGTYTEFL 578
Cdd:PRK10253 183 LEL-LSELNREKGYTLaaVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
964-1215 |
1.27e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 964 MISVERV-IEY------TDLEKEAPWECKKRPppgwpHEGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGA 1036
Cdd:COG1134 4 MIEVENVsKSYrlyhepSRSLKELLLRRRRTR-----REEFWALKDVSFE---------------VERGESVGIIGRNGA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1037 GKSSLISALFRLSEP-EGKIWIDKILTTEIGL-----HDL--RkkmsiipqEPVLFTGTMRKnldpfneHTDEELWRALE 1108
Cdd:COG1134 64 GKSTLLKLIAGILEPtSGRVEVNGRVSALLELgagfhPELtgR--------ENIYLNGRLLG-------LSRKEIDEKFD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1109 EV----QLKEAIeDLPGK-----MDTELAesgsnFSVgqrqlvclarAILKNNRILIIDEATAnVdprTDELIQQKIREK 1179
Cdd:COG1134 129 EIvefaELGDFI-DQPVKtyssgMRARLA-----FAV----------ATAVDPDILLVDEVLA-V---GDAAFQKKCLAR 188
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 255683324 1180 FAQ-----CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1215
Cdd:COG1134 189 IRElresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
998-1208 |
1.52e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.47 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidkiltTEIGL------HDL 1070
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdAGKI-------TVLGVpvparaRLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEPVL-FTGTMRKNLDPFNEHTDEELwRALEEV--QLKEaIEDLPGKMDTELAEsgsnFSVGQRQLVCLARA 1147
Cdd:PRK13536 113 RARIGVVPQFDNLdLEFTVRENLLVFGRYFGMST-REIEAVipSLLE-FARLESKADARVSD----LSGGMKRRLTLARA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1148 ILKNNRILIIDEATANVDPRTDELIQQKIREKFAQC-TVLTIAH------RLntiidSDKIMVLDSGR 1208
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVLEAGR 249
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
381-578 |
1.57e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.80 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPPASGLV---SVHGRIA----------YVSQQPWVFSG- 444
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVdglKVNDPKVderlirqeagMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILFGKKyekeRYEKVIKACALKKDLQLLEDGDLtviGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPLS 520
Cdd:PRK09493 93 TALENVMFGPL----RVRGASKEEAEKQARELLAKVGL---AERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 521 AVDAEVGKHLfqLCICQALHEK--ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFL 578
Cdd:PRK09493 166 ALDPELRHEV--LKVMQDLAEEgmTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
381-548 |
1.63e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------IAYVSQQPwvfsgtvrsni 450
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLP----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 lfGKKYEKERYEKVIKACALK-KDLQLLEDGDLTVIGDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PRK13543 92 --GLKADLSTLENLHFLCGLHgRRAKQMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*
gi 255683324 524 AEvGKHLFQLCICQALHEKITILVT 548
Cdd:PRK13543 170 LE-GITLVNRMISAHLRGGGAALVT 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1016-1223 |
1.74e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.87 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1016 KHLTALIksrekvgivGRTGAGKSSLISALFRLSE--PE----GKIWID--KILTTEIGLHDLRKKMSIIPQEPVLFTGT 1087
Cdd:PRK14239 31 NEITALI---------GPSGSGKSTLLRSINRMNDlnPEvtitGSIVYNghNIYSPRTDTVDLRKEIGMVFQQPNPFPMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1088 MRKN----LDPFNEHTDEELWRALEEVQLKEAIEDlpgKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATAN 1163
Cdd:PRK14239 102 IYENvvygLRLKGIKDKQVLDEAVEKSLKGASIWD---EVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1164 VDPRTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPE 1223
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
363-568 |
1.97e-10 |
|
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: 61.29 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 363 GKAIVHVQDFTAfwdkaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------- 431
Cdd:cd03215 1 GEPVLEVRGLSV-------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 432 ---IAYVS----QQPWVFSGTVRSNILFGkkyekeryekvikacalkkdlqlledgdltvigdrgATLSGG--QKarVNL 502
Cdd:cd03215 74 ragIAYVPedrkREGLVLDLSVAENIALS------------------------------------SLLSGGnqQK--VVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 503 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKA-ASHILILKDGEM 568
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
383-569 |
1.99e-10 |
|
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: 61.89 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVS------------VHGRIAYVSQQPWVFSG-TV 446
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngipykefaekYPGEIIYVSEEDVHFPTlTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RSNILFgkkyekeryekvikACALKkdlqlledGDLTVigdRGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:cd03233 101 RETLDF--------------ALRCK--------GNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 255683324 527 GKHLFQlCICQALHE-KITILVThqlqyLKAAS--------HILILKDGEMV 569
Cdd:cd03233 154 ALEILK-CIRTMADVlKTTTFVS-----LYQASdeiydlfdKVLVLYEGRQI 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
385-573 |
2.72e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP--PASGLVSVHGRI-------------------AYVSQ--QPwV 441
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVtlngeplaaidaprlarlrAVLPQaaQP-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 442 FSGTVRSNILFGkkyekeRYEKVIKACALKKdlqllEDGDL-----------TVIGDRGATLSGGQKARVNLARAVYQ-- 508
Cdd:PRK13547 96 FAFSAREIVLLG------RYPHARRAGALTH-----RDGEIawqalalagatALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 509 -------DADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITIL-VTHQLQYlkAASH---ILILKDGEMVQKGT 573
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNL--AARHadrIAMLADGAIVAHGA 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1004-1209 |
2.79e-10 |
|
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: 61.62 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKI-LTTEIGlhDLRKKMSIIPQEP 1081
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsGRATVAGHdVVREPR--EVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1082 VLFTG-TMRKNLDPF-------NEHTDEELWRALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLVCLARAILKNNR 1153
Cdd:cd03265 83 SVDDElTGWENLYIHarlygvpGAERRERIDELLDFVGLLEAADRLV-----------KTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1154 ILIIDEATANVDPRTDELIQ---QKIREKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWeyiEKLKEEFGM-TILLTTHYMEEAEQlCDRVAIIDHGRI 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
395-573 |
2.80e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGKKYEK---- 458
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVGYGLKMLGvpke 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 459 ERYEKVIKACALKkdlqlledgDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKhlfqlcicq 537
Cdd:PRK11432 112 ERKQRVKEALELV---------DLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR--------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 538 ALHEKI----------TILVTH-QLQYLKAASHILILKDGEMVQKGT 573
Cdd:PRK11432 174 SMREKIrelqqqfnitSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-583 |
3.38e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDKaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAvLGELPPASGLVSVHGRIAYVSQ--------- 437
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 438 ------------QPWVFSGTVRSNILFGKK----YEKERYEKVIKACALKKDLQlleDGDLTVIGDRGATLSGGQKARVN 501
Cdd:PRK14258 84 nrlrrqvsmvhpKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLW---DEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 502 LARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITI-LVTHQLQYLKAASHILIL------KDGEMVQKGTY 574
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMvIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEFGLT 240
|
....*....
gi 255683324 575 TEFLKSGVD 583
Cdd:PRK14258 241 KKIFNSPHD 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
367-593 |
3.83e-10 |
|
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: 64.05 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 367 VHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLG--ELPPASGLVSVH----------GRIAY 434
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyvERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 435 VSQQP--------------WVFSGTVRSN------ILFGKK---YEKER-YEKVIKAC---------ALKKDLQLLEDGD 481
Cdd:TIGR03269 78 VGEPCpvcggtlepeevdfWNLSDKLRRRirkriaIMLQRTfalYGDDTvLDNVLEALeeigyegkeAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 482 LT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVT-HQLQYL-KAAS 558
Cdd:TIGR03269 158 LShRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIeDLSD 237
|
250 260 270
....*....|....*....|....*....|....*
gi 255683324 559 HILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENE 593
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECE 272
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
385-576 |
3.91e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.90 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------------IAYVSQQpwvF----SG 444
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarrqIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILFGKKYEKERYEKvIKacalKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PRK11153 98 TVFDNVALPLELAGTPKAE-IK----ARVTELLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 524 AEVGKHLFQLC--ICQALHekITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYTE 576
Cdd:PRK11153 173 PATTRSILELLkdINRELG--LTIvLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
398-542 |
4.13e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.11 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 398 LAVVGPVGAGKSSLLSAVLGELPPASGLV--SVHGRIAYVSQQPwVFSGTVRSNILFgkkYEKERYEKVIKAcALKKDLq 475
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHH-VDGLDLSSNPLL---YMMRCFPGVPEQ-KLRAHL- 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 476 lledGDLTVIGDRGA----TLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAEV-GKHLFQLCICQALHEK 542
Cdd:PLN03073 612 ----GSFGVTGNLALqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPsnhldLDAVEALIqGLVLFQGGVLMVSHDE 684
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
392-525 |
4.55e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 392 ARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQqpWV---FSGTVRSNI-----LFGKKYEKEryeK 463
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLrsitdDLGSSYYKS---E 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 464 VIKACALKKdlqlLEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 525
Cdd:PRK13409 437 IIKPLQLER----LLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1017-1209 |
4.64e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 60.97 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1017 HLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTeiGLHDLRKKMSIIPQEPVLFTG-TMRKNLD- 1093
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1094 ---P---FNEHTDEELWRALEEVQLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVCLARAILKNNRILIIDEATANVDP- 1166
Cdd:cd03298 94 glsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL------SG-----GERQRVALARVLVRDKPVLLLDEPFAALDPa 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 255683324 1167 RTDELIQ--QKIREKfAQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03298 163 LRAEMLDlvLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
395-572 |
4.65e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.12 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLG-----------------ELPPASGLVSVhgriayvsqqpwVFSG-------TVRSNI 450
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGleditsgdlfigekrmnDVPPAERGVGM------------VFQSyalyphlSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGKKYEK----ERYEKVIKACALKKDLQLLEDgdltvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA-- 524
Cdd:PRK11000 97 SFGLKLAGakkeEINQRVNQVAEVLQLAHLLDR--------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAal 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 525 ------EVGKhlfqlcicqaLHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKG 572
Cdd:PRK11000 169 rvqmriEISR----------LHKRLgrtMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
381-580 |
5.05e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.93 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQP-WVFSG-T 445
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirkKIGIIFQNPdNQFIGaT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 446 VRSNILFG---KKYEKERYEKVIKACALKKDLQLLEDGDltvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 522
Cdd:PRK13632 101 VEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKE-------PQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 523 DA----EVGKHLFQLcicQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:PRK13632 174 DPkgkrEIKKIMVDL---RKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
348-573 |
5.38e-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: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 348 LLDELPQR-KAHVPSDGKAIVHVQDF-------------TAFWDKALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLS 413
Cdd:COG4172 256 LLAAEPRGdPRPVPPDAPPLLEARDLkvwfpikrglfrrTVGHVKAVD-----GVSLTLRRGETLGLVGESGSGKSTLGL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 414 AVLGeLPPASGLVSVHG----------------RIAYVSQQPwvFSG-----TVRS------NILFGKKYEKERYEKVIk 466
Cdd:COG4172 331 ALLR-LIPSEGEIRFDGqdldglsrralrplrrRMQVVFQDP--FGSlsprmTVGQiiaeglRVHGPGLSAAERRARVA- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 467 acalkkdlQLLEDGDLtvigDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALH 540
Cdd:COG4172 407 --------EALEEVGL----DPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDL--LRDLQ 472
|
250 260 270
....*....|....*....|....*....|....*..
gi 255683324 541 EK--IT-ILVTHQLQYLKAASH-ILILKDGEMVQKGT 573
Cdd:COG4172 473 REhgLAyLFISHDLAVVRALAHrVMVMKDGKVVEQGP 509
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-580 |
7.20e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAY-------------------VSQQPWV 441
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiklrkevgmVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 442 FSG-TVRSNILFGKKY----EKERYEKVIKACalkkdlqLLEDGDLTVIGDR----GATLSGGQKARVNLARAVYQDADI 512
Cdd:PRK14246 102 FPHlSIYDNIAYPLKShgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 513 YLLDDPLSAVDAeVGKHLFQLCICQALHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:PRK14246 175 LLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
391-561 |
7.85e-10 |
|
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: 60.84 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 391 IARPGELLAVVGPVGAGKSSLLSAVLGELPPASGL------------------------------VSVHGRIAYVSQQPW 440
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkllegdVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 441 VFSGTVRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:cd03236 102 AVKGKVGE--LLKKKDERGKLDELVDQLELRHVL------------DRNiDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 520 SAVDaeVGKHLFQLCICQAL--HEKITILVTHQ---LQYLKAASHIL 561
Cdd:cd03236 168 SYLD--IKQRLNAARLIRELaeDDNYVLVVEHDlavLDYLSDYIHCL 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
393-573 |
8.13e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 393 RPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------------IAYVSQQP--WVFSGTVRSNILFG 453
Cdd:PRK13634 31 PSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkplrkkVGIVFQFPehQLFEETVEKDICFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 454 -------KKYEKERYEKVIKACALKKDLQlledgdltvigDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 525
Cdd:PRK13634 111 pmnfgvsEEDAKQKAREMIELVGLPEELL-----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 526 VGKHLFQLciCQALHEK---ITILVTHQL----QYlkaASHILILKDGEMVQKGT 573
Cdd:PRK13634 180 GRKEMMEM--FYKLHKEkglTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGT 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
385-569 |
9.09e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.87 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV----------SVHGRIAYVSQqpwVF---------SGT 445
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklPEYKRAKYIGR---VFqdpmmgtapSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 446 VRSNILF----GKKY---------EKERY-EKVikacalkKDLQL-LEDGdltvIGDRGATLSGGQKARVNLARAVYQDA 510
Cdd:COG1101 99 IEENLALayrrGKRRglrrgltkkRRELFrELL-------ATLGLgLENR----LDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 511 DIYLLDDPLSAVD----AEVgkhlfqlcicQALHEKI-------TILVTHQLQY-LKAASHILILKDGEMV 569
Cdd:COG1101 168 KLLLLDEHTAALDpktaALV----------LELTEKIveennltTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
385-569 |
9.49e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 449
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 IL------FGKKYEKERYEKVIKACALKKDLQLleDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPlSAV- 522
Cdd:COG3845 101 IVlgleptKGGRLDRKAARARIRELSERYGLDV--DPDAKV-----EDLSVGEQQRVEILKALYRGARILILDEP-TAVl 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 523 -DAEVgKHLFQlcICQAL-HEKITIL-VTHQLQYLKAASH-ILILKDGEMV 569
Cdd:COG3845 173 tPQEA-DELFE--ILRRLaAEGKSIIfITHKLREVMAIADrVTVLRRGKVV 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
385-556 |
9.57e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQQ-------PWVFS-------GTVRS 448
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKlyldttlPLTVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILfgkkyekERYEKVIKACALKKDLQlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 528
Cdd:PRK09544 100 DIL-------PALKRVQAGHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|
gi 255683324 529 HLFQLcICQALHEK--ITILVTHQLQYLKA 556
Cdd:PRK09544 158 ALYDL-IDQLRRELdcAVLMVSHDLHLVMA 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
383-579 |
9.63e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP---ASGLVSVHG-------------RIAYVSQQP-WVFSG- 444
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGitltaktvwdireKVGIVFQNPdNQFVGa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TVRSNILFGKKYEKERYEKVIKACAlkkdlQLLED-GDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVR-----DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 524 AEVGKHLFQLCICQALHEKITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLK 579
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
385-582 |
1.01e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.71 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------IAYVSQQ--------PWvfsGTVRSNI 450
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdLYALSEAerrrllrtEW---GFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFGKKYE-------KERYEKV-------IKACALKKdLQLLEDgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 516
Cdd:PRK11701 99 RDGLRMQvsaggniGERLMAVgarhygdIRATAGDW-LERVEI-DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 517 DPLSAVDAEVGKHLFQLC--ICQALHEKItILVTHQLQYLKAASH-ILILKDGEMVQKG-----------TYTEFLKSGV 582
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLrgLVRELGLAV-VIVTHDLAVARLLAHrLLVMKQGRVVESGltdqvlddpqhPYTQLLVSSV 255
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1024-1213 |
1.04e-09 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 60.00 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1024 SREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKIL--TTEIGLH--DLRKKMSIIPQEPVLFTG-TMRKNLdpfne 1097
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDgGTIVLNGTVlfDSRKKINlpPQQRKIGLVFQQYALFPHlNVRENL----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1098 htdEELWRALEEVQLKEAIEDLPGKMD-TELAESGS-NFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQK 1175
Cdd:cd03297 97 ---AFGLKRKRNREDRISVDELLDLLGlDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255683324 1176 IRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1213
Cdd:cd03297 174 LKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
997-1216 |
1.04e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKilTTEIGlhdlrkkms 1075
Cdd:COG0488 315 VLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPdSGTVKLGE--TVKIG--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1076 IIPQEpvlftgtmRKNLDPfnehtDeelWRALEEVQlkeaiEDLPGKMDTELAE-------SG-------SNFSVGQRQL 1141
Cdd:COG0488 382 YFDQH--------QEELDP-----D---KTVLDELR-----DGAPGGTEQEVRGylgrflfSGddafkpvGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1142 VCLARAILKNNRILIIDEATANVDPRTDELIQQKIREkFaQCTVLTIAH-R--LNTIidSDKIMVLDSGRLKEYDEPY 1216
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-F-PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREYPGGY 514
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
711-935 |
1.04e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 61.04 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 711 NITETLDLSWYLGIYAGLTAVTVLFGIArSLLVFYILVNASQTLHNRM----FESILKAPVLFFDRNPIGRILNRFSKDI 786
Cdd:cd18557 25 TIIKGGDLDVLNELALILLAIYLLQSVF-TFVRYYLFNIAGERIVARLrrdlFSSLLRQEIAFFDKHKTGELTSRLSSDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 787 GHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIP----WILIPLVPLSVVFLVLRRYFLETSRDVkrLESTTRSPvfSHLS 862
Cdd:cd18557 104 SVLQSAVTDNLSQLLRNILQVIGGLIILFILSWkltlVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 863 SSLQGLWTIRAYKAEERCQELFDAH-QDLHSEAWFLFLTTSRWFAV-RLDAICAIFVIVVAFGSLVLAKTLNAGQ 935
Cdd:cd18557 180 ESLSNIRTVRSFSAEEKEIRRYSEAlDRSYRLARKKALANALFQGItSLLIYLSLLLVLWYGGYLVLSGQLTVGE 254
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
381-580 |
1.14e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV--SVHGRIAYVSQQPwvfsgtvrsnilfgkkyek 458
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQDH------------------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 459 eryekvikACALKKDLQLLE---------DGDLTVIGDRG-------------ATLSGGQKARVNLARAVYQDADIYLLD 516
Cdd:PRK15064 392 --------AYDFENDLTLFDwmsqwrqegDDEQAVRGTLGrllfsqddikksvKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 517 DPLSAVDAEVGKHLfqlciCQAL--HEKITILVTHQLQYLKA-ASHILILKDGEMVQ-KGTYTEFLKS 580
Cdd:PRK15064 464 EPTNHMDMESIESL-----NMALekYEGTLIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
392-525 |
1.23e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 392 ARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAY----VSQQpwvFSGTVRSNI-------LFGKKYEKEr 460
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyISPD---YDGTVEEFLrsantddFGSSYYKTE- 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 461 yekVIKACALKKdlqlLEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 525
Cdd:COG1245 439 ---IIKPLGLEK----LLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
385-572 |
1.29e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLgELPPASG----------------LVSVHGRIAYVSQQPWVfSGTVRS 448
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGeiwfdgqplhnlnrrqLLPVRHRIQVVFQDPNS-SLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NIL----------FGKKYEKERYEKVIKAcalkkdlqLLEDG-DLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDD 517
Cdd:PRK15134 380 NVLqiieeglrvhQPTLSAAQREQQVIAV--------MEEVGlDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 518 PLSAVDAEVGKHLFQLC-ICQALHEKITILVTHQLQYLKAASH-ILILKDGEMVQKG 572
Cdd:PRK15134 452 PTSSLDKTVQAQILALLkSLQQKHQLAYLFISHDLHVVRALCHqVIVLRQGEVVEQG 508
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
998-1234 |
1.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 60.53 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPL---VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG----LHD 1069
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPtQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1070 LRKKMSIIPQ--EPVLFTGTMRKNL----DPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELaesgsnfSVGQRQLVC 1143
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFEL-------SGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1144 LARAILKNNRILIIDEATANVDPR-TDELIQqkIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLL 1219
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKgRKELMT--LFKKLHQsgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIF 233
|
250
....*....|....*
gi 255683324 1220 QNPESLFYKmvqQLG 1234
Cdd:PRK13649 234 QDVDFLEEK---QLG 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1005-1215 |
1.45e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1005 FTYSlDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE--GKIWIDKILT-TEIGLHDLRKKMSIIPQEP 1081
Cdd:PRK13638 9 FRYQ-DEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkgAVLWQGKPLDySKRGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1082 vlftgtmrkNLDPFNEHTDEELWRALEEVQLKEAieDLPGKMDTELAESGSN---------FSVGQRQLVCLARAILKNN 1152
Cdd:PRK13638 87 ---------EQQIFYTDIDSDIAFSLRNLGVPEA--EITRRVDEALTLVDAQhfrhqpiqcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1153 RILIIDEATANVDPRTDELIQQKIREKFAQCTVLTI-AHRLNTIID-SDKIMVLDSGRLKEYDEP 1215
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
363-577 |
1.48e-09 |
|
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: 62.26 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 363 GKAIVHVQDFT-AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVhG---RIAYVSQQ 438
Cdd:TIGR03719 319 GDKVIEAENLTkAFGDKLL----IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GetvKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 439 pwvfsgtvRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GA-------TLSGGQ 496
Cdd:TIGR03719 394 --------RDAL----DPNKTVWEEI-------------SGGlDIIKLGKReipsrayvgrfnfkGSdqqkkvgQLSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 497 KARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfqlciCQALHEKI------TILVTHQLQYL-KAASHILILK-DGEM 568
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVET---------LRALEEALlnfagcAVVISHDRWFLdRIATHILAFEgDSHV 519
|
250
....*....|
gi 255683324 569 VQ-KGTYTEF 577
Cdd:TIGR03719 520 EWfEGNFSEY 529
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
373-573 |
1.65e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 373 TAFWDKALDSPTLQglsfiARPGELLAVVGPVGAGKSSLLS------------AVLGELPPASGLVSV------HGRIAY 434
Cdd:PRK13645 20 TPFEFKALNNTSLT-----FKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIkevkrlRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 435 VSQQP--WVFSGTVRSNILFGKKYEKERYEKVIKACA-LKKDLQLLEDgdltVIGDRGATLSGGQKARVNLARAVYQDAD 511
Cdd:PRK13645 95 VFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPeLLKLVQLPED----YVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 512 IYLLDDPLSAVDAEVGKHLFQLCI-CQALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 573
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFErLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
385-523 |
1.79e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASG----------LVSVHGR----IAYVSQQPWVFSgtvRSNI 450
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisLLPLHARarrgIGYLPQEASIFR---RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 lfgkkyekerYEKVIKACALKKDL----------QLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:PRK10895 96 ----------YDNLMAVLQIRDDLsaeqredranELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
....
gi 255683324 520 SAVD 523
Cdd:PRK10895 166 AGVD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
990-1210 |
1.85e-09 |
|
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: 61.76 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 990 PGWPHE-GVIVFDNVNFT-YSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP--EGKIWID-KILT 1062
Cdd:TIGR02633 247 PHEPHEiGDVILEARNLTcWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGkfEGNVFINgKPVD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1063 TEIGLHDLRKKMSIIPQE-------PVLFTGtmrKN-----LDPFNEHT--DEE-----LWRALEEVQLKEAIEDLPGkm 1123
Cdd:TIGR02633 327 IRNPAQAIRAGIAMVPEDrkrhgivPILGVG---KNitlsvLKSFCFKMriDAAaelqiIGSAIQRLKVKTASPFLPI-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1124 dtelaesgSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTD----ELIQQKIREKFAqctVLTIAHRLNTIID-S 1198
Cdd:TIGR02633 402 --------GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyeiyKLINQLAQEGVA---IIVVSSELAEVLGlS 470
|
250
....*....|..
gi 255683324 1199 DKIMVLDSGRLK 1210
Cdd:TIGR02633 471 DRVLVIGEGKLK 482
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1022-1215 |
2.02e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG---LHDLRKKMSIIPQEPvlFTgtmrkNLDPfnE 1097
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPtSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YA-----SLNP--R 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1098 HTDEELwraLEEV----------QLKEAIEDLpgkmdteLAESGSN----------FSVGQRQLVCLARAILKNNRILII 1157
Cdd:COG4608 112 MTVGDI---IAEPlrihglaskaERRERVAEL-------LELVGLRpehadrypheFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 1158 DEATANVDPRtdelIQ-------QKIREKFaQCTVLTIAHRLNTI--IdSDKIMVLDSGRLKE-------YDEP 1215
Cdd:COG4608 182 DEPVSALDVS----IQaqvlnllEDLQDEL-GLTYLFISHDLSVVrhI-SDRVAVMYLGKIVEiaprdelYARP 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
996-1209 |
2.05e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.58 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTE------ 1064
Cdd:COG3845 17 GVVANDDVSLT---------------VRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIDgkpvRIRSPRdaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1065 IGlhdlrkkMsiIPQEPVLFtgtmrknlDPFnehT--------DEELWRALeeVQLKEAIEDLpgkmdTELAES-G---- 1131
Cdd:COG3845 82 IG-------M--VHQHFMLV--------PNL---TvaenivlgLEPTKGGR--LDRKAARARI-----RELSERyGldvd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1132 -----SNFSVGQRQLVCLARAILKNNRILIIDEATANVDPR-TDELIqqKIREKFAQ--CTVLTIAHRLNTIID-SDKIM 1202
Cdd:COG3845 135 pdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQeADELF--EILRRLAAegKSIIFITHKLREVMAiADRVT 212
|
....*..
gi 255683324 1203 VLDSGRL 1209
Cdd:COG3845 213 VLRRGKV 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
385-573 |
2.05e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.51 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRiayvsqqPwvFSGTVRSNIlfGkkY--EkER-- 460
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-------P--LDPEDRRRI--G--YlpE-ERgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 461 Y--EKVI-------------KACALKKDLQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:COG4152 83 YpkMKVGeqlvylarlkglsKAEAKRRADEWLERLGLGdRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 525 eVGKHLFQlcicQALHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKGT 573
Cdd:COG4152 163 -VNVELLK----DVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1002-1225 |
2.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.71 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1002 NVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKKMSIIP 1078
Cdd:PRK13639 6 DLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPtSGEVLIKgePIKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1079 QEP--VLFTGTMRKNL--DPFNEHTDEElwraleEVQ--LKEAIEdlpgKMDTELAESGS--NFSVGQRQLVCLARAILK 1150
Cdd:PRK13639 85 QNPddQLFAPTVEEDVafGPLNLGLSKE------EVEkrVKEALK----AVGMEGFENKPphHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1151 NNRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRLNTI-IDSDKIMVLDSGRLKEYDEPYVLLQNPESL 1225
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
385-572 |
2.63e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 449
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGK--------------KYEKERYEKVIKACALKKDLqlledgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLL 515
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDL------DEKV-----ANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 516 DDPLSAV-DAEVgKHLFqLCICQALHE-KITILVTHQLQYLKA-ASHILILKDGEMVQKG 572
Cdd:PRK09700 170 DEPTSSLtNKEV-DYLF-LIMNQLRKEgTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1003-1207 |
3.21e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.27 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1003 VNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGkiwiDKILTTEIGLHDLRKkmsiIPQEPV 1082
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA----GRVLLNGGPLDFQRD----SIARGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 LFTG---------TMRKNLDPFNE-HTDEELWRALEEVQLKeAIEDLPGkmdtelaesgSNFSVGQRQLVCLARAILKNN 1152
Cdd:cd03231 76 LYLGhapgikttlSVLENLRFWHAdHSDEQVEEALARVGLN-GFEDRPV----------AQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1153 RILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNtiIDSDKIMVLDSG 1207
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARggMVVLTTHQDLG--LSEAGARELDLG 199
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
397-572 |
3.37e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 397 LLAVVGPVGAGKSSLLSAV-----LGELPPASGLVSVHGRIAY---------------VSQQPWVFSG-TVRSNILFGKK 455
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpievrrevgmVFQYPNPFPHlTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 456 YEK---------ERYEKVIKACALKKDLQlledgdlTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeV 526
Cdd:PRK14267 112 LNGlvkskkeldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-V 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 527 GKHLFQLCICQALHEKITILVTHQ-LQYLKAASHILILKDGEMVQKG 572
Cdd:PRK14267 184 GTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
708-935 |
3.52e-09 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 59.73 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 708 ANGNITETlDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIG 787
Cdd:cd18541 30 TAGTLTAS-QLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 788 HMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWI----LIPLVPLSVVFLVLRRYFLETSRDVKrlESttrspvFSHLSS 863
Cdd:cd18541 109 AVRMALGPGILYLVDALFLGVLVLVMMFTISPKLtliaLLPLPLLALLVYRLGKKIHKRFRKVQ--EA------FSDLSD 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 864 SLQ----GLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAI-FVIVVAFGS-LVLAKTLNAGQ 935
Cdd:cd18541 181 RVQesfsGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLsFLIVLWYGGrLVIRGTITLGD 258
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
669-970 |
3.57e-09 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 59.72 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 669 FFIIFLVLLNMVGQVF--YVLQDwwlshwankqgALNN-TRNANGNITETLD-LSWYLGIYAGLTAVTVLFgiarSLLVF 744
Cdd:cd18547 2 ILVIILAIISTLLSVLgpYLLGK-----------AIDLiIEGLGGGGGVDFSgLLRILLLLLGLYLLSALF----SYLQN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 745 YILVNASQ----TLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPW 820
Cdd:cd18547 67 RLMARVSQrtvyDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 821 ---ILIPLVPLSVVFLVL-----RRYFLETSRDVKRLEsttrspvfSHLSSSLQGLWTIRAYKAEERCQELFDAH-QDLH 891
Cdd:cd18547 147 ltlIVLVTVPLSLLVTKFiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEInEELY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 892 SEAWflfltTSRWFA------VR-LDAIcaIFVIVVAFGS-LVLAKTLNAGQVGLALSYALTLMGMF-----QWSVRQSA 958
Cdd:cd18547 219 KASF-----KAQFYSgllmpiMNfINNL--GYVLVAVVGGlLVINGALTVGVIQAFLQYSRQFSQPInqisqQINSLQSA 291
|
330
....*....|..
gi 255683324 959 evenmMISVERV 970
Cdd:cd18547 292 -----LAGAERV 298
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1014-1209 |
3.96e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGkiwiDKILTTEIGLHDLRKKMSIIPQEPVLFTgtMRKNLD 1093
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA----GELLAGTAPLAEAREDTRLMFQDARLLP--WKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1094 P----FNEHTDEELWRALEEVQLKEAIEDLPGkmdtelAESGsnfsvGQRQLVCLARAILKNNRILIIDEATANVDPRTD 1169
Cdd:PRK11247 101 NvglgLKGQWRDAALQALAAVGLADRANEWPA------ALSG-----GQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 255683324 1170 ELIQQKIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:PRK11247 170 IEMQDLIESLWQQhgFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
382-579 |
4.03e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 382 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGeLPPASGLVSVHGRI-------------AYVSQQ-PWVFSGTVr 447
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQqTPPFAMPV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 snilF-------GKKYEKERYEKVIKACAlkkdlQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQ-------DADIY 513
Cdd:PRK03695 87 ----FqyltlhqPDKTRTEAVASALNEVA-----EALGLDDK--LGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 514 LLDDPLSAVDAEVGKHLFQLC--ICQAlheKITILVT-HQLQY-LKAASHILILKDGEMVQKGTYTEFLK 579
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLseLCQQ---GIAVVMSsHDLNHtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
666-1215 |
4.09e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 666 ASWFFIIFLVLLNMVGQVFYVLQDWWLSHwankqgALNNTRNANgnitetldlSWYLGIYAGLTAVTVLFGIARSLLVFY 745
Cdd:COG4615 10 ESRWLLLLALLLGLLSGLANAGLIALINQ------ALNATGAAL---------ARLLLLFAGLLVLLLLSRLASQLLLTR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 746 ILVNASQTLHNRMFESILKAPVLFFDRnpIG--RILNRFSKDIGHMDD---LLPLTFLDFIQTLL----LVvsviavaaa 816
Cdd:COG4615 75 LGQHAVARLRLRLSRRILAAPLERLER--IGaaRLLAALTEDVRTISQafvRLPELLQSVALVLGclayLA--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 817 vipWILIPLVPLSVVFLVLRR--YFLETSRDVKRLE--STTRSPVFSHLSSSLQGLWTIRAYKAeeRCQELFDAH----- 887
Cdd:COG4615 144 ---WLSPPLFLLTLVLLGLGVagYRLLVRRARRHLRraREAEDRLFKHFRALLEGFKELKLNRR--RRRAFFDEDlqpta 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 888 ---QDLHSEAWFLFLTTSRW-----FAVrldaicaIFVIVVAFGSLVLAKTLNAGQVGLALSY----------ALTLMGM 949
Cdd:COG4615 219 eryRDLRIRADTIFALANNWgnllfFAL-------IGLILFLLPALGWADPAVLSGFVLVLLFlrgplsqlvgALPTLSR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 950 FQWSVRQSAEVEnmmisvervieyTDLEKEAPWECKKRPPPGWPHEGVIVFDNVNFTYSLD--------GPLvlkHLTal 1021
Cdd:COG4615 292 ANVALRKIEELE------------LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEdgdegftlGPI---DLT-- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFtgtmRKNLDPFNEHTD 1100
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPEsGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1101 EELWRALEEVQLKE--AIEDlpGK-MDTELaesgsnfSVGQRQLVCLARAILKNNRILIIDEATANVDPR-----TDELI 1172
Cdd:COG4615 431 ARARELLERLELDHkvSVED--GRfSTTDL-------SQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELL 501
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 255683324 1173 QQ-KIREKfaqcTVLTIAHrlntiiD------SDKIMVLDSGRLKEYDEP 1215
Cdd:COG4615 502 PElKARGK----TVIAISH------DdryfdlADRVLKMDYGKLVELTGP 541
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1004-1209 |
4.68e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALF-RLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPV 1082
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 L---FT-------GTMRKNLDPfnEHTDEELWRALEEVQLkeaiEDLPGKMDTELaeSGsnfsvGQRQLVCLARAIL--- 1149
Cdd:PRK13548 87 LsfpFTveevvamGRAPHGLSR--AEDDALVAAALAQVDL----AHLAGRDYPQL--SG-----GEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1150 ---KNNRILIIDEATANVDPRTDELIQQKIREkFAQ---CTVLTIAHRLN-TIIDSDKIMVLDSGRL 1209
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQ-LAHergLAVIVVLHDLNlAARYADRIVLLHQGRL 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
987-1211 |
4.94e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 987 RPPPGWPhegVIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEI 1065
Cdd:PRK10522 315 QAFPDWQ---TLELRNVTFAYQ-DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPqSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1066 GLHDLRKKMSIIPQEPVLFTgtmrKNLDPFNEHTDEELWRA-LEEVQLKEAIEDLPGKMdtelaeSGSNFSVGQRQLVCL 1144
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFD----QLLGPEGKPANPALVEKwLERLKMAHKLELEDGRI------SNLKLSKGQKKRLAL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRTDELIQQKI--REKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKE 1211
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHFRREFYQVLlpLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
388-580 |
6.14e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.65 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 388 LSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVfSGTVRSNI---- 450
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqRIRMIFQDPST-SLNPRQRIsqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 ----LFGKKYEKERYEKVIKAcALKKdLQLLEDGdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:PRK15112 111 dfplRLNTDLEPEQREKQIIE-TLRQ-VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 527 GKHLFQLCI-CQALHEKITILVTHQLQYLKAAS-HILILKDGEMVQKGTYTEFLKS 580
Cdd:PRK15112 185 RSQLINLMLeLQEKQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLAS 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
378-580 |
6.24e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 58.91 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP---ASGLVSVHG-----------------RIAYVSQ 437
Cdd:COG0444 19 KAVD-----GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllklsekelrkirgrEIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 438 QPW-----VFsgTVRSNI-----LFGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDRGA----TLSGGQKARVNLA 503
Cdd:COG0444 94 DPMtslnpVM--TVGDQIaeplrIHGGLSKAEARERAI---------ELLERVGLPDPERRLDryphELSGGMRQRVMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 504 RAVYQDADIYLLDDPLSAVDAEVgkhlfqlcicQA--------LHEKI---TILVTHQL---QYLkaASHILILKDGEMV 569
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTI----------QAqilnllkdLQRELglaILFITHDLgvvAEI--ADRVAVMYAGRIV 230
|
250
....*....|.
gi 255683324 570 QKGTYTEFLKS 580
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
50-315 |
6.45e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 58.94 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGI-FTLIEEGTRVVQPLFLGKII-EYFEKYDPDDSVALHTAYGYAAVLsmctLILAILHHLYFYHVQCAGMR----L 123
Cdd:cd18544 1 FILALlLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLLLALLYLGLL----LLSFLLQYLQTYLLQKLGQRiiydL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 124 RVAmchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ--VTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAgLAVL 201
Cdd:cd18544 77 RRD----LFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNElfTSGLVTLIGDLLLLIGILIAMFLLNWRLALIS-LLVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 202 VILLPL----QSCIGKLFSSLRSKTA---AFtdarirtMNEVITGMRIIKMYAWEKS----FADLIANLRK---KEIskI 267
Cdd:cd18544 152 PLLLLAtylfRKKSRKAYREVREKLSrlnAF-------LQESISGMSVIQLFNREKRefeeFDEINQEYRKanlKSI--K 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 255683324 268 LGSSYLRGMNMASFFIankVILFVTFTSYVLLGNEITAShVFVAMTLY 315
Cdd:cd18544 223 LFALFRPLVELLSSLA---LALVLWYGGGQVLSGAVTLG-VLYAFIQY 266
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
998-1225 |
6.83e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPLVLKHL---TALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKI-WI------------DKI 1060
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALdnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDtGTIeWIfkdeknkkktkeKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1061 LTTEIGLH-----------DLRKKMSIIPQ--EPVLFTGTMRKNL--DPFNEHTDEElwRALEEVqlKEAIEdLPGKMDT 1125
Cdd:PRK13651 83 VLEKLVIQktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRA--AKYIE-LVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1126 ELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPR-TDELIqqKIREKFAQC--TVLTIAHRLNTIID-SDKI 1201
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEIL--EIFDNLNKQgkTIILVTHDLDNVLEwTKRT 235
|
250 260
....*....|....*....|....
gi 255683324 1202 MVLDSGRLKEYDEPYVLLQNPESL 1225
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILSDNKFL 259
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
393-584 |
7.14e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 393 RPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV-----------------HGRIAYVSQQP--WVFSGTVRSNILFG 453
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvRKKVGVVFQFPesQLFEETVLKDVAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 454 KK---YEKERYEKV----IKACALKKdlQLLEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:PRK13643 110 PQnfgIPKEKAEKIaaekLEMVGLAD--EFWEKSPFE--------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 527 GKHLFQLciCQALHE--KITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSgVDF 584
Cdd:PRK13643 180 RIEMMQL--FESIHQsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE-VDF 237
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
718-970 |
8.84e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 58.21 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18542 38 LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIPWI-LIPLVPLSVVFLVLRRYFletsrdvKRLEsttrsPVFSH-------LSSSLQ--- 866
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLtLISLAIIPFIALFSYVFF-------KKVR-----PAFEEireqegeLNTVLQenl 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 867 -GLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAI-FVIVVAFGS-LVLAKTLNAGQVGLALSYa 943
Cdd:cd18542 186 tGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLqIVLVLWVGGyLVINGEITLGELVAFISY- 264
|
250 260 270
....*....|....*....|....*....|.
gi 255683324 944 ltlMGMFQWSVRQSAEVENMM----ISVERV 970
Cdd:cd18542 265 ---LWMLIWPVRQLGRLINDMsrasASAERI 292
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1014-1176 |
1.01e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDkilttEIGLHDL--------RKKMSIIPQEP---- 1081
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFD-----GQPLHNLnrrqllpvRHRIQVVFQDPnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1082 --------VLFTG--TMRKNLDPfnEHTDEELWRALEEVQLK-EAIEDLPgkmdtelaesgSNFSVGQRQLVCLARAILK 1150
Cdd:PRK15134 376 nprlnvlqIIEEGlrVHQPTLSA--AQREQQVIAVMEEVGLDpETRHRYP-----------AEFSGGQRQRIAIARALIL 442
|
170 180
....*....|....*....|....*.
gi 255683324 1151 NNRILIIDEATANVDpRTdelIQQKI 1176
Cdd:PRK15134 443 KPSLIILDEPTSSLD-KT---VQAQI 464
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
998-1225 |
1.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSLDGPL---VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKIL----TTEIGLHD 1069
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTtGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1070 LRKKMSIIPQ--EPVLFTGTMRKNLD--PFNEHTDeelwraLEEVqlKEAIEDLPGKMDTE---LAESGSNFSVGQRQLV 1142
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIfgPKNFKMN------LDEV--KNYAHRLLMDLGFSrdvMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1143 CLARAILKNNRILIIDEATANVDPRTDELIQ---QKIREKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVL 1218
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMrllKSLQTDENK-TIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
....*..
gi 255683324 1219 LQNPESL 1225
Cdd:PRK13646 234 FKDKKKL 240
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
381-523 |
1.18e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------RIAYvsQQPWVFSG---------T 445
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTY--QKQLCFVGhrsginpylT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 446 VRSNILFGKKYEKERYEkVIKACALKKDLQLLedgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-ITELCRLFSLEHLI---DYPC-----GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
996-1182 |
1.29e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKiltTEIGLHDLRKKM 1074
Cdd:PRK13539 14 GRVLFSGLSFT---------------LAAGEALVLTGPNGSGKTTLLRLIAGLLPPAaGTIKLDG---GDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SII----PQEPVLftgTMRKNLD---PFNEHTDEELWRALEEVQLkEAIEDLPGKMdtelaesgsnFSVGQRQLVCLARA 1147
Cdd:PRK13539 76 HYLghrnAMKPAL---TVAENLEfwaAFLGGEELDIAAALEAVGL-APLAHLPFGY----------LSAGQKRRVALARL 141
|
170 180 190
....*....|....*....|....*....|....*
gi 255683324 1148 ILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ 1182
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQ 176
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
395-567 |
1.48e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASG--------LVSVHGRIAYVSQQ----PWvfsGTVRSNILFGKKYE-KERY 461
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtapLAEAREDTRLMFQDarllPW---KKVIDNVGLGLKGQwRDAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 462 EKVIKACALkkdlqlledgdltviGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQ 537
Cdd:PRK11247 115 LQALAAVGL---------------ADRAnewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170 180 190
....*....|....*....|....*....|..
gi 255683324 538 ALHEKITI-LVTHQLQYLKA-ASHILILKDGE 567
Cdd:PRK11247 180 WQQHGFTVlLVTHDVSEAVAmADRVLLIEEGK 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1004-1226 |
1.67e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdlRKKMSIIPQEPV 1082
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPtEGQIFIDGEDVTHRSIQ--QRDICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 LFTG-TMRKNLdpfnEHTDEELWRALEEV--QLKEAIE--DLPGKMDTELAEsgsnFSVGQRQLVCLARAILKNNRILII 1157
Cdd:PRK11432 89 LFPHmSLGENV----GYGLKMLGVPKEERkqRVKEALElvDLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1158 DEATANVDPRTDELIQQKIREKFAQ--CTVLTIAH-RLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNPESLF 1226
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
394-575 |
2.01e-08 |
|
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: 55.06 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 394 PGELLAVVGPVGAGKSSLLSAVLgelppasglvsvhgriayvsqqpWVFSGtvRSNILFGKKYEKERYekvIKACAlkkD 473
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-----------------------LALGG--AQSATRRRSGVKAGC---IVAAV---S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 474 LQLLedgdLTVIGdrgatLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTH 549
Cdd:cd03227 69 AELI----FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170 180
....*....|....*....|....*.
gi 255683324 550 QLQYLKAASHILILKdgeMVQKGTYT 575
Cdd:cd03227 140 LPELAELADKLIHIK---KVITGVYK 162
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
385-550 |
2.08e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP--PASGLVSVhgriayvsqqPWVFSGTVRSNI-LFGKKYEKERY 461
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV----------PDNQFGREASLIdAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 462 EKVIKACALkkdlqlledGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD---AEVGKHLFQLcICQA 538
Cdd:COG2401 116 VELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQK-LARR 185
|
170
....*....|...
gi 255683324 539 LheKIT-ILVTHQ 550
Cdd:COG2401 186 A--GITlVVATHH 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
385-576 |
2.16e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.17 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR---------------IAYVSQQP--WVFSGTVR 447
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 448 SNILFG----KKYEKERYEKVIKACAlKKDLQLLEDGDLtvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:PRK13636 102 QDVSFGavnlKLPEDEVRKRVDNALK-RTGIEHLKDKPT-------HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 524 AEVGKHLFQLCICQALHEKITILV-THQLQYLKA-ASHILILKDGEMVQKGTYTE 576
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLyCDNVFVMKEGRVILQGNPKE 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1008-1207 |
2.22e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1008 SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKiwidkilTTEIGLHDLRK-------KMSI--IP 1078
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG-------TLEIGGNPCARltpakahQLGIylVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1079 QEPVLFTG-TMRKNLdpfnehtdeeLWR----ALEEVQLKEAIEDLPGKMDteLAESGSNFSVGQRQLVCLARAILKNNR 1153
Cdd:PRK15439 93 QEPLLFPNlSVKENI----------LFGlpkrQASMQKMKQLLAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 1154 ILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDSG 1207
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQgVGIVFISHKLPEIRQlADRISVMRDG 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1001-1210 |
2.28e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1001 DNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRlSEP---EGKIWID-KILTTEIGLHDL------ 1070
Cdd:PRK13549 279 DDVSFS---------------LRRGEILGIAGLVGAGRTELVQCLFG-AYPgrwEGEIFIDgKPVKIRNPQQAIaqgiam 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 ----RKKMSIIPQEPVLFTGTMrKNLDPFNEHT--DEelwrALEEVQLKEAIEDLPGKMDTELAESGsNFSVGQRQLVCL 1144
Cdd:PRK13549 343 vpedRKRDGIVPVMGVGKNITL-AALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVL 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRTD----ELIQQKIREKFAqctVLTIAHRLNTIID-SDKIMVLDSGRLK 1210
Cdd:PRK13549 417 AKCLLLNPKILILDEPTRGIDVGAKyeiyKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKLK 484
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
383-612 |
2.32e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 383 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------------IAYVSQQPWVFSG-TVRSN 449
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILF-----GKKYEKERYEkvIKAcalkkdlqLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 523
Cdd:TIGR01257 1024 ILFyaqlkGRSWEEAQLE--MEA--------MLEDTGLHHKRNEEAQdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 524 AEVGKHLFQLcICQALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKGTyTEFLKSGVDFGSLL----KKENEEAEPS 598
Cdd:TIGR01257 1094 PYSRRSIWDL-LLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT-PLFLKNCFGTGFYLtlvrKMKNIQSQRG 1171
|
250
....*....|....
gi 255683324 599 TAPGTPTLRKRTFS 612
Cdd:TIGR01257 1172 GCEGTCSCTSKGFS 1185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
385-570 |
2.84e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQ-PWVFSGTVRSN 449
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQElHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGK--------KYEKERYEKVIKACALKKDLqlleDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSA 521
Cdd:PRK11288 100 LYLGQlphkggivNRRLLNYEAREQLEHLGVDI----DPDTPL-----KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 255683324 522 VDAEVGKHLFQLcICQALHE-KITILVTHQLQYLKAASH-ILILKDGEMVQ 570
Cdd:PRK11288 171 LSAREIEQLFRV-IRELRAEgRVILYVSHRMEEIFALCDaITVFKDGRYVA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
385-569 |
2.93e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.65 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAYVSQQPWVFsgtVRSNI--LFGKKY---EK 458
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKNREVPF---LRRQIgmIFQDHHllmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 459 ERYEKV----IKACALKKDLQLLEDGDLTVIG--DRGAT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 528
Cdd:PRK10908 95 TVYDNVaiplIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 529 HLFQLcicqaLHE----KITILV-THQLQYLKAASH-ILILKDGEMV 569
Cdd:PRK10908 175 GILRL-----FEEfnrvGVTVLMaTHDIGLISRRSYrMLTLSDGHLH 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1004-1208 |
2.98e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.91 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEPEGKIWIDKILTTEIGLHDL-RKKMSIIPQ 1079
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1080 EPVLFTG-TMRKNLDPFNEHT-------DEELWRALEEVQLKEAIEDLPgkmdteLAESGSNFSVGQRQLVCLARAILKN 1151
Cdd:TIGR02633 86 ELTLVPElSVAENIFLGNEITlpggrmaYNAMYLRAKNLLRELQLDADN------VTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1152 NRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1004-1223 |
3.46e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.06 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL-SEPEGKIWIDKILTTEIGLHD-LRKKMSIIPQEP 1081
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1082 VLFtgtmrKNLDPF-NEHTDEELWRALEEVQLKEAIEDLPGKMD-TELAES-GSNFSVGQRQLVCLARAILKNNRILIID 1158
Cdd:PRK10895 88 SIF-----RRLSVYdNLMAVLQIRDDLSAEQREDRANELMEEFHiEHLRDSmGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1159 EATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPE 1223
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
997-1209 |
4.29e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 997 VIVFDNVNFTYsLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIW-----IDKILTTEIGLhdL 1070
Cdd:PRK10908 1 MIRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSaGKIWfsghdITRLKNREVPF--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1071 RKKMSIIPQEP-VLFTGTMRKNLD-PF------NEHTDEELWRALEEVQLKEAIEDLPGKMdtelaesgsnfSVGQRQLV 1142
Cdd:PRK10908 78 RRQIGMIFQDHhLLMDRTVYDNVAiPLiiagasGDDIRRRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1143 CLARAILKNNRILIIDEATANVDPRTDELIqQKIREKFAQ--CTVLTIAHRLNTIIDSD-KIMVLDSGRL 1209
Cdd:PRK10908 147 GIARAVVNKPAVLLADEPTGNLDDALSEGI-LRLFEEFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
388-580 |
4.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 388 LSFIARPgeLLAVVGPVGAGKSSLLSAVLGELPPASG-------------------LVSVHGRIAYVSQQPWVFSGTVRS 448
Cdd:PRK14271 42 MGFPARA--VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdVLEFRRRVGMLFQRPNPFPMSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGKKYEKERYEKVIKACALKKdlqLLEDGDLTVIGDRGAT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 524
Cdd:PRK14271 120 NVLAGVRAHKLVPRKEFRGVAQAR---LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 525 EVGKHLFQLciCQALHEKIT-ILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 580
Cdd:PRK14271 197 TTTEKIEEF--IRSLADRLTvIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1030-1213 |
4.74e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1030 IVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILtteiglHDLRKKMSIIP---------QEPVLFTG-TMRKNLDPFNE 1097
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPqKGRIVLnGRVL------FDAEKGICLPPekrrigyvfQDARLFPHyKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1098 HTDEELWRALeeVQLKeAIEDLpgkmdteLAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVD-PRTDELIQ--Q 1174
Cdd:PRK11144 103 KSMVAQFDKI--VALL-GIEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPylE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255683324 1175 KIREKFaQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYD 1213
Cdd:PRK11144 173 RLAREI-NIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
391-523 |
5.31e-08 |
|
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: 57.10 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 391 IARPGELLAVVGPVGAGKSSLLSAVLGELPP------------------------------ASGLVSVHGRIAYVSQQPW 440
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 441 VFSGTVRSnILfgKKY-EKERYEKVIKACALKKDLqlleDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPL 519
Cdd:COG1245 175 VFKGTVRE-LL--EKVdERGKLDELAEKLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 255683324 520 SAVD 523
Cdd:COG1245 241 SYLD 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
385-573 |
5.49e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 449
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 450 ILFGKKY-EKERYEKVIKACAlkkDL--QLLEDGdltviGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWVY---ELfpRLHERR-----IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 255683324 527 GKHLFQLcICQALHEKITILVTHQ--LQYLKAASHILILKDGEMVQKGT 573
Cdd:PRK11614 173 IQQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDT 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
394-569 |
6.01e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 394 PGELLAVVGPVGAGKSSLLSAVLGELPPASGlvsvhgriayvsqqpwvfsgtvrsnilfgkkyekeryeKVIKACALKKD 473
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------GVIYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 474 LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQAL-----HEKITILVT 548
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILT 122
|
170 180
....*....|....*....|.
gi 255683324 549 HQLQYLKAASHILILKDGEMV 569
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
381-523 |
6.34e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA-SGLVSVHGR--------------IAYVSQQ---PWVF 442
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRrrgsgetiwdikkhIGYVSSSlhlDYRV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 443 SGTVRSNILFGKKYEKERYEKVIKAcalkkdLQLLEDGDLTVIGDRGAT-------LSGGQKARVNLARAVYQDADIYLL 515
Cdd:PRK10938 352 STSVRNVILSGFFDSIGIYQAVSDR------QQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVKHPTLLIL 425
|
....*...
gi 255683324 516 DDPLSAVD 523
Cdd:PRK10938 426 DEPLQGLD 433
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
395-576 |
6.67e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASG----------------LVSVHGRIAYVSQQPWVFSG-TVRSNILFGKKYE 457
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGeilfdgenipamsrsrLYTVRKRMSMLFQSGALFTDmNVFDNVAYPLREH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 458 KERYEKVIKACALKKdlqlledgdLTVIGDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 531
Cdd:PRK11831 113 TQLPAPLLHSTVMMK---------LEAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 532 QLcICQALHE-KIT-ILVTHQL-QYLKAASHILILKDGEMVQKGTYTE 576
Cdd:PRK11831 184 KL-ISELNSAlGVTcVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
385-569 |
8.02e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP-----------------------PASGLVSVHGRIAYVSQQpwv 441
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiywsgsplkasnirdtERAGIVIIHQELTLVPEL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 442 fsgTVRSNILFGK----KYEKERYEKVIKAC-ALKKDLQLLEDGDLTVIGDRGatlsGGQKARVNLARAVYQDADIYLLD 516
Cdd:TIGR02633 94 ---SVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255683324 517 DPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASH-ILILKDGEMV 569
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDtICVIRDGQHV 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
391-523 |
8.20e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 391 IARPGELLAVVGPVGAGKSSLLSAVLGELPP------------------------------ASGLVSVHGRIAYVSQQPW 440
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdyeeepswdevlkrfrgtelqnyfkklYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 441 VFSGTVRSniLFGKKYEKERYEKVIKACALKKDLqlleDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLS 520
Cdd:PRK13409 175 VFKGKVRE--LLKKVDERGKLDEVVERLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
...
gi 255683324 521 AVD 523
Cdd:PRK13409 242 YLD 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
375-576 |
9.76e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 375 FWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAYVSQQPWVfsgTVRSNI--- 450
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWR---AVRSDIqmi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 -----------------------LFGKKYEKERYEKVIKACALKkdLQLLEDgdltVIGDRGATLSGGQKARVNLARAVY 507
Cdd:PRK15079 104 fqdplaslnprmtigeiiaeplrTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 508 QDADIYLLDDPLSAVDAEVGKHLFQLciCQALHEKI---TILVTHQLQYLKAAS-HILILKDGEMVQKGTYTE 576
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNL--LQQLQREMglsLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYDE 248
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1004-1225 |
1.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEP 1081
Cdd:PRK13652 8 DLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPtSGSVLIRGEPITKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1082 --VLFTGTMRKNL--DPFNEHTDEE-LWRALEEVQLKEAIEDLPGKMDTELaesgsnfSVGQRQLVCLARAILKNNRILI 1156
Cdd:PRK13652 88 ddQIFSPTVEQDIafGPINLGLDEEtVAHRVSSALHMLGLEELRDRVPHHL-------SGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 1157 IDEATANVDPR-TDELIQ--QKIREKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPESL 1225
Cdd:PRK13652 161 LDEPTAGLDPQgVKELIDflNDLPETYGM-TVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-568 |
1.07e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 351 ELPQR---KAHVPsdGKAIVHVQDFTAfwdkaLDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVS 427
Cdd:PRK10982 234 SLTQRfpdKENKP--GEVILEVRNLTS-----LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTIT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 428 VHGR--------------IAYVSQQ----------PWVFSGTVrSNIlfgKKYeKERYeKVIKACALKKDLQLLED---- 479
Cdd:PRK10982 307 LHGKkinnhnaneainhgFALVTEErrstgiyaylDIGFNSLI-SNI---RNY-KNKV-GLLDNSRMKSDTQWVIDsmrv 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 480 ---GDLTVIGdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQL-QYLK 555
Cdd:PRK10982 381 ktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLG 456
|
250
....*....|...
gi 255683324 556 AASHILILKDGEM 568
Cdd:PRK10982 457 ITDRILVMSNGLV 469
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
378-569 |
1.13e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSL---LSAVL------GEL--------------PPASGLVSVHGRIAY 434
Cdd:PRK13549 19 KALD-----NVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYphgtyeGEIifegeelqasnirdTERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 435 VSQQpwvfsgTVRSNILFGKKYEKE---RYEKVIKAC-ALKKDLQLLEDGDLTViGDrgatLSGGQKARVNLARAVYQDA 510
Cdd:PRK13549 94 VKEL------SVLENIFLGNEITPGgimDYDAMYLRAqKLLAQLKLDINPATPV-GN----LGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 511 DIYLLDDPLSAVDAEVGKHLFQLcICQALHEKIT-ILVTHQLQYLKAAS-HILILKDGEMV 569
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDI-IRDLKAHGIAcIYISHKLNEVKAISdTICVIRDGRHI 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
385-568 |
1.19e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------RIAYVSQQ-PWVFSG-------TV 446
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeeaRAKLRAKHvGFVFQSfmliptlNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 447 RSNI-----LFGkkyEKERYEKViKACALKKDLQLledgdltviGDR----GATLSGGQKARVNLARAVYQDADIYLLDD 517
Cdd:PRK10584 106 LENVelpalLRG---ESSRQSRN-GAKALLEQLGL---------GKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 518 PLSAVDAEVGKH----LFQLcicQALHEKITILVTHQLQYLKAASHILILKDGEM 568
Cdd:PRK10584 173 PTGNLDRQTGDKiadlLFSL---NREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1004-1223 |
1.36e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.37 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE------GKIWID--KILTTEIGL-HDLRKKM 1074
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDtaRSLSQQKGLiRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTG-TMRKNL--DPF---NEHTDEELWRALEEVqlkeAIEDLPGKMDTelaeSGSNFSVGQRQLVCLARAI 1148
Cdd:PRK11264 88 GFVFQNFNLFPHrTVLENIieGPVivkGEPKEEATARARELL----AKVGLAGKETS----YPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1149 LKNNRILIIDEATANVDPrtdEL-------IQQKIREKFaqcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQ 1220
Cdd:PRK11264 160 AMRPEVILFDEPTSALDP---ELvgevlntIRQLAQEKR---TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
...
gi 255683324 1221 NPE 1223
Cdd:PRK11264 234 DPQ 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
998-1209 |
1.41e-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: 53.41 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHD------- 1069
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLPPKDrdiamvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1070 ----LRKKMSIIpqEPVLFTGTMRKnldpfneHTDEELWRALEEVQLKEAIEDLPGKMDTELaeSGsnfsvGQRQLVCLA 1145
Cdd:cd03301 79 qnyaLYPHMTVY--DNIAFGLKLRK-------VPKDEIDERVREVAELLQIEHLLDRKPKQL--SG-----GQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1146 RAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAH-RLNTIIDSDKIMVLDSGRL 1209
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1029-1209 |
1.47e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1029 GIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTEIGLHdlrKKMSIIPQE----PVLftgTMRKNLdpFNEH- 1098
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPdAGSILIDgqemRFASTTAALA---AGVAIIYQElhlvPEM---TVAENL--YLGQl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1099 ------TDEELWRALEEVQLKEAIEDL-PgkmDTELAEsgsnFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDEL 1171
Cdd:PRK11288 106 phkggiVNRRLLNYEAREQLEHLGVDIdP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 255683324 1172 IQQKIREKFAQCTV-LTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:PRK11288 179 LFRVIRELRAEGRViLYVSHRMEEIFAlCDAITVFKDGRY 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-576 |
1.84e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPP---ASGLVSVHG-------------RIAYVSQQP-WV 441
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPearVSGEVYLDGqdifkmdvielrrRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 442 FSGTVRSNILFGKKY------EKERYEKVIKAcaLKKdLQLLEDgdltvIGDR----GATLSGGQKARVNLARAVYQDAD 511
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvksKKELQERVRWA--LEK-AQLWDE-----VKDRldapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 512 IYLLDDPLSAVDAEVGKHLFQLCIcqALHEKITI-LVTH-QLQYLKAASHILILKDGEMVQKGTYTE 576
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFL--ELKKDMTIvLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
995-1208 |
2.45e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.04 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 995 EGVIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWI-DKILTTEIglHDLRK 1072
Cdd:PRK13537 5 VAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLcGEPVPSRA--RHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQ----EPVLftgTMRKNLDPFNEHTDEELWRALEEVQLKEAIEDLPGKMDTELAEsgsnFSVGQRQLVCLARAI 1148
Cdd:PRK13537 81 RVGVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1149 LKNNRILIIDEATANVDPRTDELIQQKIREKFAQC-TVLTIAH------RLntiidSDKIMVLDSGR 1208
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGR 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
999-1168 |
3.28e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.23 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 999 VFDNVNFTYSldgplvlkhltaliksREKV-GIVGRTGAGKSSLISALFRLSEPE-GKIWID--KILT-TEIGLHDLRKK 1073
Cdd:PRK11831 22 IFDNISLTVP----------------RGKItAIMGPSGIGKTTLLRLIGGQIAPDhGEILFDgeNIPAmSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQEPVLFTG-TMRKNLD-PFNEHTD--EELWRA-----LEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLVCL 1144
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAyPLREHTQlpAPLLHStvmmkLEAVGLRGAAKLMP-----------SELSGGMARRAAL 154
|
170 180
....*....|....*....|....
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRT 1168
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPIT 178
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
718-970 |
3.44e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 53.26 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18546 38 LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIPW----ILIPLVPLSVVFLVLRRYfletSRDVKRLESTTRSPVFSHLSSSLQGLWTIRA 873
Cdd:cd18546 118 VQLVVSLLTLVGIAVVLLVLDPRlalvALAALPPLALATRWFRRR----SSRAYRRARERIAAVNADLQETLAGIRVVQA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 874 YKAEERCQELFDAHQDLHSEAwflFLTTSRWFA-----VRLDAICAIFVIVVAFGSLVLAKTLNAGqvglALSYALTLMG 948
Cdd:cd18546 194 FRRERRNAERFAELSDDYRDA---RLRAQRLVAiyfpgVELLGNLATAAVLLVGAWRVAAGTLTVG----VLVAFLLYLR 266
|
250 260
....*....|....*....|....*.
gi 255683324 949 MFQWSVRQSAEVENM----MISVERV 970
Cdd:cd18546 267 RFFAPIQQLSQVFDSyqqaRAALEKI 292
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
373-572 |
3.63e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.09 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 373 TAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPAS---------------GLVSVHGRIAYVSQ 437
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKgavlwqgkpldyskrGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 438 QP--WVFSGTVRSNILFGKK----YEKERYEKVIKACALkKDLQLLEDGDLTVigdrgatLSGGQKARVNLARAVYQDAD 511
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRnlgvPEAEITRRVDEALTL-VDAQHFRHQPIQC-------LSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 512 IYLLDDPLSAVDAEVGKHLFQL---CICQALHekiTILVTHQLQYLKAASH-ILILKDGEMVQKG 572
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIirrIVAQGNH---VIISSHDIDLIYEISDaVYVLRQGQILTHG 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1026-1212 |
3.73e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1026 EKVGIVGRTGAGKSSLISALFRLSEPEGKIW------IDKILT-TEIGLHDLR-KKMSIIPQEPVlftgtmrKNLDPFNE 1097
Cdd:PRK09473 43 ETLGIVGESGSGKSQTAFALMGLLAANGRIGgsatfnGREILNlPEKELNKLRaEQISMIFQDPM-------TSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1098 HTD------------------EELWRALEEVQLKEAIEdlpgKMDTELAEsgsnFSVGQRQLVCLARAILKNNRILIIDE 1159
Cdd:PRK09473 116 VGEqlmevlmlhkgmskaeafEESVRMLDAVKMPEARK----RMKMYPHE----FSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1160 ATANVDPRTDELIQQKIRE---KFaQCTVLTIAHRLNTIIDS-DKIMVLDSGRLKEY 1212
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEY 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1018-1209 |
3.76e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 53.09 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1018 LTALIksrekvgivGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL---- 1092
Cdd:PRK11231 30 ITALI---------GPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELvayg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1093 -DPFNEH------TDEEL-WRALEEVQlkeaIEDLPGKMDTELaeSGsnfsvGQRQLVCLARAILKNNRILIIDEATANV 1164
Cdd:PRK11231 101 rSPWLSLwgrlsaEDNARvNQAMEQTR----INHLADRRLTDL--SG-----GQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 1165 D-PRTDELIQQkIREKFAQC-TVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:PRK11231 170 DiNHQVELMRL-MRELNTQGkTVVTVLHDLNQASRyCDHLVVLANGHV 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
363-518 |
3.95e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 363 GKAIVHVQDFT-AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVhG---RIAYVSQQ 438
Cdd:PRK11819 321 GDKVIEAENLSkSFGDRLL----IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvKLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 439 pwvfsgtvRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GA-------TLSGGQ 496
Cdd:PRK11819 396 --------RDAL----DPNKTVWEEI-------------SGGlDIIKVGNReipsrayvgrfnfkGGdqqkkvgVLSGGE 450
|
170 180
....*....|....*....|..
gi 255683324 497 KARVNLARAVYQDADIYLLDDP 518
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEP 472
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1004-1222 |
4.08e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 54.08 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQEPV 1082
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTaGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 L---FTGTM---------RKNLDPFNEHTDEELWRALEEVQLkEAIEDLPgkmDTELaeSGsnfsvGQRQLVCLARAILK 1150
Cdd:PRK09536 88 LsfeFDVRQvvemgrtphRSRFDTWTETDRAAVERAMERTGV-AQFADRP---VTSL--SG-----GERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 1151 NNRILIIDEATANVD----PRTDELIQQKIREKFaqcTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNP 1222
Cdd:PRK09536 157 ATPVLLLDEPTASLDinhqVRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1015-1226 |
4.97e-07 |
|
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: 52.34 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1015 LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-------KILTTEIGL----HDLRKKMSIIpqEPV 1082
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGgedatdvPVQERNVGFvfqhYALFRHMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1083 LFTGTMRKNLDPFNEHT-DEELWRALEEVQLKEAIEDLPgkmdtelaesgSNFSVGQRQLVCLARAILKNNRILIIDEAT 1161
Cdd:cd03296 96 AFGLRVKPRSERPPEAEiRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 1162 ANVDPRTDELIQQKIREKFAQCTVLTI--AHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPESLF 1226
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1014-1224 |
5.53e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWID--KILTTEIGLHDLRKKMSIIPQEPVLFTG-TMR 1089
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDglKVNDPKVDERLIRQEAGMVFQQFYLFPHlTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1090 KNLDPFNEHTdeelwRALEEVQLKEAIEDLPGKMDteLAESG----SNFSVGQRQLVCLARAILKNNRILIIDEATANVD 1165
Cdd:PRK09493 96 ENVMFGPLRV-----RGASKEEAEKQARELLAKVG--LAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 1166 PrtdELIQQ--KIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPES 1224
Cdd:PRK09493 169 P---ELRHEvlKVMQDLAEegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
712-970 |
6.82e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 52.57 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 712 ITETLDLSWYL-GIYAGLTAVTVLFGIARSLLVFYIlvnASQTLHN-RM--FESILKAPVLFFDRNPIGRILNRFSKDIG 787
Cdd:cd18565 46 PADPRGQLWLLgGLTVAAFLLESLFQYLSGVLWRRF---AQRVQHDlRTdtYDHVQRLDMAFFEDRQTGDLMSVLNNDVN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 788 HMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWI-LIPLVPLSVVFLVLRRYfletSRDVKRLESTTRSPV---FSHLSS 863
Cdd:cd18565 123 QLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLaLVALLPVPLIIAGTYWF----QRRIEPRYRAVREAVgdlNARLEN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 864 SLQGLWTIRAYKAE--ERcQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFVIVVAFGSLV-------LAKTLNAG 934
Cdd:cd18565 199 NLSGIAVIKAFTAEdfER-ERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWvldgpplFTGTLTVG 277
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 255683324 935 qvglALSYALTLMGMFQWSVRQSAEV----ENMMISVERV 970
Cdd:cd18565 278 ----TLVTFLFYTQRLLWPLTRLGDLidqyQRAMASAKRV 313
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
718-970 |
6.95e-07 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 52.42 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18552 38 LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIPW------ILIPLVPLSVVFLV--LRRYfletSRDVkrLESTTRspVFSHLSSSLQGLW 869
Cdd:cd18552 118 TVLVRDPLTVIGLLGVLFYLDWKltlialVVLPLAALPIRRIGkrLRKI----SRRS--QESMGD--LTSVLQETLSGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 870 TIRAYKAEERCQELFDAhqdlhsEAWFLFLTTSRWFAVR---------LDAICAIFVIVVAfGSLVLAKTLNAGQVglaL 940
Cdd:cd18552 190 VVKAFGAEDYEIKRFRK------ANERLRRLSMKIARARalssplmelLGAIAIALVLWYG-GYQVISGELTPGEF---I 259
|
250 260 270
....*....|....*....|....*....|....
gi 255683324 941 SYaLTLMGMFQWSVRQ----SAEVENMMISVERV 970
Cdd:cd18552 260 SF-ITALLLLYQPIKRlsnvNANLQRGLAAAERI 292
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
986-1246 |
7.68e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 986 KRPPPGWPhEGVIVfDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEI 1065
Cdd:TIGR01257 919 ERELPGLV-PGVCV-KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1066 GLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWralEEVQLK-EAIEDLPGkMDTELAESGSNFSVGQRQLVCL 1144
Cdd:TIGR01257 997 NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW---EEAQLEmEAMLEDTG-LHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1145 ARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTI-IDSDKIMVLDSGRLKEYDEPYVLLQNPE 1223
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKNCFG 1152
|
250 260 270
....*....|....*....|....*....|
gi 255683324 1224 SLFY-------KMVQQLGKGEAAALTETAK 1246
Cdd:TIGR01257 1153 TGFYltlvrkmKNIQSQRGGCEGTCSCTSK 1182
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
987-1226 |
8.41e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.92 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 987 RPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEI 1065
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPtAGQIMLDGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1066 GLHdlRKKMSIIPQEPVLFTG-TMRKNLdPFNEHTDEelwraLEEVQLKEAIEDLPG--KMDTELAESGSNFSVGQRQLV 1142
Cdd:PRK11607 87 PPY--QRPINMMFQSYALFPHmTVEQNI-AFGLKQDK-----LPKAEIASRVNEMLGlvHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1143 CLARAILKNNRILIIDEATANVDPRTDELIQQK---IREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLL 1219
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
....*..
gi 255683324 1220 QNPESLF 1226
Cdd:PRK11607 239 EHPTTRY 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
993-1211 |
1.02e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 993 PHEGVIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEG------KIWIDKILTTE 1064
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGglvqcdKMLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1065 IGLHDLRKK---------MSIIPQEPV-----LFT------GTMRKNLDPFNEHTDEELWRALEEVQLKEAiedlpgkmD 1124
Cdd:PRK10261 88 IELSEQSAAqmrhvrgadMAMIFQEPMtslnpVFTvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEA--------Q 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1125 TELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIR--EKFAQCTVLTIAHRLNTIID-SDKI 1201
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEiADRV 239
|
250
....*....|
gi 255683324 1202 MVLDSGRLKE 1211
Cdd:PRK10261 240 LVMYQGEAVE 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1000-1221 |
1.09e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.42 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1000 FDNVNFTYsldGPLVLKHLTAL-IKSREKVGIVGRTGAGKSSLISALfrLSEP---EGKIWID-KILTTEIGLHDLRKKM 1074
Cdd:PRK11614 8 FDKVSAHY---GKIQALHEVSLhINQGEIVTLIGANGAGKTTLLGTL--CGDPratSGRIVFDgKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPVLFTG-TMRKNLDPFNEHTDEELWRaleevQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKNNR 1153
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 1154 ILIIDEATANVDPrtdeLIQQKIREKFAQC-----TVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQN 1221
Cdd:PRK11614 158 LLLLDEPSLGLAP----IIIQQIFDTIEQLreqgmTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1014-1236 |
1.10e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.51 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLftgtmRKNL 1092
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPsEGSIVVNGQTINLVRDKDGQLKVADKNQLRLL-----RTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1093 DPFNEHTDeeLWR---ALEEVQlkEAIEDLPGKMDTE--------LAESG----------SNFSVGQRQLVCLARAILKN 1151
Cdd:PRK10619 95 TMVFQHFN--LWShmtVLENVM--EAPIQVLGLSKQEareravkyLAKVGideraqgkypVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1152 NRILIIDEATANVDPrtdELIQQ--KIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEPYVLLQNPESlf 1226
Cdd:PRK10619 171 PEVLLFDEPTSALDP---ELVGEvlRIMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS-- 245
|
250
....*....|
gi 255683324 1227 yKMVQQLGKG 1236
Cdd:PRK10619 246 -PRLQQFLKG 254
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
385-589 |
1.62e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.23 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAYVSQQPW-VFSGTVRsnILF----GKKYEK 458
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEpLAKLNRAQRkAFRRDIQ--MVFqdsiSAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 459 ERYEKVI-----------KACALKKDLQLLE--DGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAe 525
Cdd:PRK10419 106 KTVREIIreplrhllsldKAERLARASEMLRavDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL- 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 526 vgkhLFQLCICQ---ALHEKITI---LVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLK 589
Cdd:PRK10419 185 ----VLQAGVIRllkKLQQQFGTaclFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQ 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-512 |
1.86e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 351 ELPQRKAHVPSdGKAIVHVQDFTAFWDKALdsPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG 430
Cdd:COG3845 243 LLRVEKAPAEP-GEVVLEVENLSVRDDRGV--PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 431 R--------------IAYVSQQPW----VFSGTVRSNILFGkKYEKERYEK--VIKACALKKD-LQLLEDGDL--TVIGD 487
Cdd:COG3845 320 EditglsprerrrlgVAYIPEDRLgrglVPDMSVAENLILG-RYRRPPFSRggFLDRKAIRAFaEELIEEFDVrtPGPDT 398
|
170 180
....*....|....*....|....*..
gi 255683324 488 RGATLSGG--QKarVNLARAVYQDADI 512
Cdd:COG3845 399 PARSLSGGnqQK--VILARELSRDPKL 423
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
724-952 |
2.22e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 51.00 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 724 IYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTFLDFIQT 803
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 804 LLLVVSVIAVAAAVIPWI-LIPLVPLSVVFLVLRRYfletSRDVKRLESTTRspvfSHLSSS-------LQGLWTIRAYK 875
Cdd:cd18572 121 LVQLVGGLAFMFSLSWRLtLLAFITVPVIALITKVY----GRYYRKLSKEIQ----DALAEAnqvaeeaLSNIRTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 876 AEERCQELFDAHQDLHSE-------AWFLFLTTSRWfavrLDAICAIFVIVVAfGSLVLAKTLNAGQVGLALSYALTLMG 948
Cdd:cd18572 193 TEEREARRYERALDKALKlsvrqalAYAGYVAVNTL----LQNGTQVLVLFYG-GHLVLSGRMSAGQLVTFMLYQQQLGE 267
|
....
gi 255683324 949 MFQW 952
Cdd:cd18572 268 AFQS 271
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
50-299 |
2.26e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 50.87 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIeeGTRVVQ---PLFLGKIIEYFEKYDPDDSVALHtaygYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVA 126
Cdd:cd18541 1 YLLGILFLI--LVDLLQlliPRIIGRAIDALTAGTLTASQLLR----YALLILLLALLIGIFRFLWRYLIFGASRRIEYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 127 MCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIF--LHFLWAGPLQAIAVTVLLWVEIGISCLAglavlVIL 204
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPgiLYLVDALFLGVLVLVMMFTISPKLTLIA-----LLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 205 LPLQSCIGKLFSSL---RSKTA--AFTDarirtMN----EVITGMRIIKMYAWE----KSFADLIANLRKKEIS------ 265
Cdd:cd18541 150 LPLLALLVYRLGKKihkRFRKVqeAFSD-----LSdrvqESFSGIRVIKAFVQEeaeiERFDKLNEEYVEKNLRlarvda 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255683324 266 -------KILGSSYLRGMNMASFFIANKVIL---FVTFTSYVLL 299
Cdd:cd18541 225 lffpligLLIGLSFLIVLWYGGRLVIRGTITlgdLVAFNSYLGM 268
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
754-924 |
3.56e-06 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 50.50 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 754 LHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF----LDFIqTLLLVVSVIAVAAAVIPWILIPLVPLs 829
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLmniwLDMI-TIIIAICIMLVLNPKLTFVSLVIFPF- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 830 vvFLVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFD-AHQDLHSEAwflfLTTSRWFAVR 908
Cdd:cd18554 159 --YILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDkRNGHFLTRA----LKHTRWNAKT 232
|
170 180
....*....|....*....|
gi 255683324 909 LDAICAIF----VIVVAFGS 924
Cdd:cd18554 233 FSAVNTITdlapLLVIGFAA 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1004-1207 |
4.49e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI--------LTTEIGLHDLRKKM 1074
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPtKGTITINNInynkldhkLAAQLGIGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 SIIPQEPV---LFTGtmrknldpfnEHTDEELWRA----LEEVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARA 1147
Cdd:PRK09700 90 SVIDELTVlenLYIG----------RHLTKKVCGVniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 1148 ILKNNRILIIDEATANV-DPRTDEL--IQQKIREKFAqcTVLTIAHRLNTIID-SDKIMVLDSG 1207
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLtNKEVDYLflIMNQLRKEGT--AIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
362-570 |
4.93e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 362 DGKAIVHVQDFTAFwdkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR---------- 431
Cdd:PRK09700 261 AHETVFEVRNVTSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsplda 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 432 ----IAYVSQ---QPWVFSG-TVRSNILFGKKYEKERYEKVIKACALKKDLQLLED--GDLTV----IGDRGATLSGGQK 497
Cdd:PRK09700 336 vkkgMAYITEsrrDNGFFPNfSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqrELLALkchsVNQNITELSGGNQ 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 498 ARVNLARAVYQDADIYLLDDPLSAVD----AEVGKHLFQLcicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQ 570
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQL----ADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
718-970 |
5.29e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.79 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18540 41 LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIP----WILIPLVPLSVVFLVLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWTIRA 873
Cdd:cd18540 121 VDLVWGITYMIGILIVMLILNWklalIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 874 YKAEERCQELFDAH-QDLHSEawflflttsrwfAVRLDAICAIFVIVVAF-------------GSLVLAKTLNAGQVGLA 939
Cdd:cd18540 197 LVREEKNLREFKELtEEMRRA------------SVRAARLSALFLPIVLFlgsiatalvlwygGILVLAGAITIGTLVAF 264
|
250 260 270
....*....|....*....|....*....|.
gi 255683324 940 LSYALTLMGMFQWSVRQSAEVENMMISVERV 970
Cdd:cd18540 265 ISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
378-569 |
5.35e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDSPTLQglsfiARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQ-PWVF 442
Cdd:PRK10982 12 KALDNVNLK-----VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 443 SGTVRSNILFGkkyekeRYEK----VIKACALKKDLQLLEDGDLTV-IGDRGATLSGGQKARVNLARAVYQDADIYLLDD 517
Cdd:PRK10982 87 QRSVMDNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 518 PLSAVDAEVGKHLFQlcICQALHEK--ITILVTHQL-QYLKAASHILILKDGEMV 569
Cdd:PRK10982 161 PTSSLTEKEVNHLFT--IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWI 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
380-573 |
6.32e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 380 LDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQP--W 440
Cdd:PRK13649 18 FEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkKVGLVFQFPesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 441 VFSGTVRSNILFGKK---YEKERYEKVikacALKKdlqlledgdLTVIG------DRGA-TLSGGQKARVNLARAVYQDA 510
Cdd:PRK13649 98 LFEETVLKDVAFGPQnfgVSQEEAEAL----AREK---------LALVGiseslfEKNPfELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 511 DIYLLDDPLSAVDAEVGKHLFQLciCQALHEK-ITI-LVTHQLQYL-KAASHILILKDGEMVQKGT 573
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTL--FKKLHQSgMTIvLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
995-1191 |
7.17e-06 |
|
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: 50.52 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 995 EGVIVFDNVNFTySLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLisalFRLSepeGKIW--IDKILTTeiglhDLRK 1072
Cdd:TIGR00954 449 DNGIKFENIPLV-TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL----FRIL---GELWpvYGGRLTK-----PAKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1073 KMSIIPQEPVLFTGTMRKNL------DPFNEH--TDEELWRALEEVQLK---------EAIEDLpgkMDTelaesgsnFS 1135
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIiypdssEDMKRRglSDKDLEQILDNVQLThilereggwSAVQDW---MDV--------LS 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 1136 VGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREkfAQCTVLTIAHR 1191
Cdd:TIGR00954 585 GGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
385-572 |
1.03e-05 |
|
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: 47.91 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGElppaSGLVSVHGRIAYVSQqpwvfsgtvrsNILFGKKYEKER---- 460
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----PKYEVTEGEILFKGE-----------DITDLPPEERARlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 461 ----YEKVIKACALKKDLQLLEDGdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlcIC 536
Cdd:cd03217 81 lafqYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE--VI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 255683324 537 QALHEKIT--ILVTHQ---LQYLKaASHILILKDGEMVQKG 572
Cdd:cd03217 148 NKLREEGKsvLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1014-1234 |
1.11e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.57 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILttEIGLhdLRKKMSIIPQEPVLFTGTMRknL 1092
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPdEGVIKRNGKL--RIGY--VPQKLYLDTTLPLTVNRFLR--L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1093 DPFNEHTDeeLWRALEEVQLKEAIEDLPGKMdtelaesgsnfSVGQRQLVCLARAILKNNRILIIDEATANVDPRTD--- 1169
Cdd:PRK09544 93 RPGTKKED--ILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQval 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1170 -ELIQQKIREkfAQCTVLTIAHRLNTII-DSDKIMVLD-----SGrlkeydEPYVLLQNPE--SLF-YKMVQQLG 1234
Cdd:PRK09544 160 yDLIDQLRRE--LDCAVLMVSHDLHLVMaKTDEVLCLNhhiccSG------TPEVVSLHPEfiSMFgPRGAEQLG 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1014-1193 |
1.27e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.44 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNL 1092
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPaHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1093 DPFNEHTDEEL---WRALEEVQLKEAIEdlpGKMDTELA-ESGSNFSVGQRQLVCLARAILKNNRILIIDEATA--NVDP 1166
Cdd:PRK10253 102 VARGRYPHQPLftrWRKEDEEAVTKAMQ---ATGITHLAdQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTwlDISH 178
|
170 180
....*....|....*....|....*....
gi 255683324 1167 RTD--ELIQQKIREKfaQCTVLTIAHRLN 1193
Cdd:PRK10253 179 QIDllELLSELNREK--GYTLAAVLHDLN 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1004-1209 |
1.42e-05 |
|
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: 47.52 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1004 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE---GKIWIDKILTTEIGLHDlRKKMSII--P 1078
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvteGEILFKGEDITDLPPEE-RARLGIFlaF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1079 QEPVLFTGTmrKNLDpfnehtdeeLWRALEEvqlkeaiedlpgkmdtelaesgsNFSVGQRQLVCLARAILKNNRILIID 1158
Cdd:cd03217 84 QYPPEIPGV--KNAD---------FLRYVNE-----------------------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 255683324 1159 EATANVDPRTDELIQQKIRE-KFAQCTVLTIAH--RLNTIIDSDKIMVLDSGRL 1209
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
148-569 |
1.43e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.41 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 148 TGQIVNLLSNDVnkfDQVTIFLHFLwAGPLQAIAVTV-----LLWVEIGIsCLAGLAVLVILLPL-QSCIGKLFSSLRsK 221
Cdd:COG4615 104 AARLLAALTEDV---RTISQAFVRL-PELLQSVALVLgclayLAWLSPPL-FLLTLVLLGLGVAGyRLLVRRARRHLR-R 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 222 TAAFTDARIRTMNEVITGMRIIKMYAwEKSFA----DLIANLRKKEISKILG-SSYLRGMNMAS--FFIANKVILFVtFT 294
Cdd:COG4615 178 AREAEDRLFKHFRALLEGFKELKLNR-RRRRAffdeDLQPTAERYRDLRIRAdTIFALANNWGNllFFALIGLILFL-LP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 295 SYVLLGNEITASHVFVAMTLYGAVrLTVTLFFPSAIErgseAIVSIRRIKNfllLDELPQRKAHVPSDGKAIVHVQDFT- 373
Cdd:COG4615 256 ALGWADPAVLSGFVLVLLFLRGPL-SQLVGALPTLSR----ANVALRKIEE---LELALAAAEPAAADAAAPPAPADFQt 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 374 --------AFWDKALDSP-TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------RIAYVSQ 437
Cdd:COG4615 328 lelrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpvtadnREAYRQL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 438 qpwvFSgTVRSNI-LFGKKYEKERYEKVIKACALKKDLQLleDGDLTVIGDRGAT--LSGGQKARVNLARAVYQDADIYL 514
Cdd:COG4615 408 ----FS-AVFSDFhLFDRLLGLDGEADPARARELLERLEL--DHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILV 480
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255683324 515 LD------DPlsavdaeVGKHLFQLCICQALHE--KITILVTHQLQYLKAASHILILKDGEMV 569
Cdd:COG4615 481 FDewaadqDP-------EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1022-1205 |
1.51e-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: 47.79 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDkiltteiglhdlRKKMSIIPQE-PVLFTGTMRKNL-DPFNEH 1098
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPdEGDIEIE------------LDTVSYKPQYiKADYEGTVRDLLsSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1099 TDEELWRAleEVQLKEAIEDLpgkMDTELAEsgsnFSVGQRQLVCLARAILKNNRILIIDEATANVDPRtDELIQQKIRE 1178
Cdd:cd03237 90 YTHPYFKT--EIAKPLQIEQI---LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|..
gi 255683324 1179 KFA---QCTVLTIAHRLnTIID--SDKIMVLD 1205
Cdd:cd03237 160 RFAennEKTAFVVEHDI-IMIDylADRLIVFE 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
996-1208 |
1.53e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSL---ISALFRLSEPEGKIWIDKiltTEIGLHDLR- 1071
Cdd:NF040905 13 GVKALDDVNLS---------------VREGEIHALCGENGAGKSTLmkvLSGVYPHGSYEGEILFDG---EVCRFKDIRd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1072 ---KKMSIIPQE----PVL------FTGtmrknldpfNEHT-------DEELWRA---LEEVQLKEAiedlPgkmDTELA 1128
Cdd:NF040905 75 seaLGIVIIHQElaliPYLsiaeniFLG---------NERAkrgvidwNETNRRArelLAKVGLDES----P---DTLVT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1129 ESGsnfsVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDS 1206
Cdd:NF040905 139 DIG----VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRvADSITVLRD 214
|
..
gi 255683324 1207 GR 1208
Cdd:NF040905 215 GR 216
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
718-970 |
1.56e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 48.25 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLlpLTF 797
Cdd:cd18543 38 LWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF--LAF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDF-IQTLLLVVSVIAVAAAVIPWI----LIPLVPLSVVFLVLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWTIR 872
Cdd:cd18543 116 GPFlLGNLLTLVVGLVVMLVLSPPLalvaLASLPPLVLVARRFRRRYFPASRRAQDQAGD----LATVVEESVTGIRVVK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 873 AYKAEERCQELFDAHQDLhseawfLFLT-------TSRWFAVrLDAICAI-FVIVVAFGS-LVLAKTLNAGQVgLALSya 943
Cdd:cd18543 192 AFGRERRELDRFEAAARR------LRATrlraarlRARFWPL-LEALPELgLAAVLALGGwLVANGSLTLGTL-VAFS-- 261
|
250 260 270
....*....|....*....|....*....|.
gi 255683324 944 lTLMGMFQWSVRQSAEVENM----MISVERV 970
Cdd:cd18543 262 -AYLTMLVWPVRMLGWLLAMaqraRAAAERV 291
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
385-550 |
1.87e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHGR---------IAYVSQQPwVFSG--TVRSNI 450
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNGRpldssfqrsIGYVQQQD-LHLPtsTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFG---------KKYEKERY-EKVIKacalkkdlqLLEDGDL--TVIGDRGATLSGGQKARVNLA-RAVYQDADIYLLDD 517
Cdd:TIGR00956 858 RFSaylrqpksvSKSEKMEYvEEVIK---------LLEMESYadAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDE 928
|
170 180 190
....*....|....*....|....*....|....
gi 255683324 518 PLSAVDAEVGKHLFQLCICQALHEKiTILVT-HQ 550
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQ-AILCTiHQ 961
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
996-1208 |
1.96e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTTEIGLHDLRKK 1073
Cdd:PRK10982 10 GVKALDNVNLK---------------VRPHSIHALMGENGAGKSTLLKCLFGIYQKdSGSILFQgKEIDFKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1074 MSIIPQE--PVLFTGTMrKNL--------DPFNEHtdEELWRaleevQLKEAIEDLpgKMDTELAESGSNFSVGQRQLVC 1143
Cdd:PRK10982 75 ISMVHQElnLVLQRSVM-DNMwlgryptkGMFVDQ--DKMYR-----DTKAIFDEL--DIDIDPRAKVATLSVSQMQMIE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 1144 LARAILKNNRILIIDEATANVDPRTDE---LIQQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGR 1208
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNhlfTIIRKLKER--GCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
399-567 |
1.96e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 399 AVVGPVGAGKSSLLSAVL----GELPPASGLVSVHGRIAyvsqqpwvFSGTVRSNI------LFGKKYEKERYEKVIKAC 468
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLI--------REGEVRAQVklafenANGKKYTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 469 AlkkdlqLLEDGDLTVIGDRG-ATLSGGQKA------RVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfqlcICQALHE 541
Cdd:cd03240 98 I------FCHQGESNWPLLDMrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN--------IEESLAE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 255683324 542 KIT----------ILVTHQLQYLKAASHIL-ILKDGE 567
Cdd:cd03240 164 IIEerksqknfqlIVITHDEELVDAADHIYrVEKDGR 200
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
381-572 |
1.98e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPasGLVSVHGRIAY--VSQQPWVFSGTVRSNIL------F 452
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLdgKPVAPCALRGRKIATIMqnprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 453 G-----KKYEKERYEKVIKACALKKDLQLLEDGDLtviGDRGATL-------SGGQKARVNLARAVYQDADIYLLDDPLS 520
Cdd:PRK10418 93 NplhtmHTHARETCLALGKPADDATLTAALEAVGL---ENAARVLklypfemSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 521 AVDAEVGKHLFQLCicqalhEKIT-------ILVTHQLQYL-KAASHILILKDGEMVQKG 572
Cdd:PRK10418 170 DLDVVAQARILDLL------ESIVqkralgmLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
713-970 |
2.13e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 47.96 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 713 TETLDLSWYLGIyaGLTAVTV---LFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFsKDIGHM 789
Cdd:cd18566 35 NESIPTLQVLVI--GVVIAILlesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 790 DDLLP----LTFLD----FIQTLLLvvsviavAAAVIPWILIPLVPLSVVFLV-------LRRYFLETSR-DVKRlestt 853
Cdd:cd18566 112 REFLTgqalLALLDlpfvLIFLGLI-------WYLGGKLVLVPLVLLGLFVLVaillgpiLRRALKERSRaDERR----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 854 rspvFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAwflFLTTSRwFAVRLDAICAIF-----VIVVAFGS-LVL 927
Cdd:cd18566 180 ----QNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYA---GFKVAK-INAVAQTLGQLFsqvsmVAVVAFGAlLVI 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 255683324 928 AKTLNAGQ-------VGLALSYALTLMGMfqWSVRQSAEVenmmiSVERV 970
Cdd:cd18566 252 NGDLTVGAliactmlSGRVLQPLQRAFGL--WTRFQQVRV-----AVRRL 294
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
971-1209 |
2.30e-05 |
|
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: 47.33 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 971 IEYTDL-------EKEAPWECKKRPPPGWPHEGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLIS 1043
Cdd:cd03267 1 IEVSNLsksyrvySKEPGLIGSLKSLFKRKYREVEALKGISFT---------------IEKGEIVGFIGPNGAGKTTTLK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1044 ALFRLSEP-EGKI-------WIDKIltteiglhDLRKKMSIIPQE--------PVLftgtmrknlDPFNEHTDeeLWRaL 1107
Cdd:cd03267 66 ILSGLLQPtSGEVrvaglvpWKRRK--------KFLRRIGVVFGQktqlwwdlPVI---------DSFYLLAA--IYD-L 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1108 EEVQLKEAIEDLPGKMDTE--LAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQC 1183
Cdd:cd03267 126 PPARFKKRLDELSELLDLEelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynRERGT 205
|
250 260
....*....|....*....|....*..
gi 255683324 1184 TVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:cd03267 206 TVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
121-343 |
2.32e-05 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 47.80 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 121 MRLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIA-VTVLLWVEIGISCLAGL 198
Cdd:cd18552 72 RDLRNDL----FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGlLGVLFYLDWKLTLIALV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 199 AVLVILLPLQScIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISKILGSSYLR 274
Cdd:cd18552 148 VLPLAALPIRR-IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSS 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 275 GMN--MASFFIAnkVILFvtFTSYVLLGNEITASHvFVA-----MTLYGAVRLTVTLFfpSAIERGseaIVSIRRI 343
Cdd:cd18552 227 PLMelLGAIAIA--LVLW--YGGYQVISGELTPGE-FISfitalLLLYQPIKRLSNVN--ANLQRG---LAAAERI 292
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
395-579 |
2.38e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-RIAYVSQQpwvfsgtvrsnilfgkkyekeryekvikacalkkd 473
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY----------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 474 lqlledgdltvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVT-HQLQ 552
Cdd:cd03222 70 ----------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVeHDLA 133
|
170 180
....*....|....*....|....*..
gi 255683324 553 YLKAASHILILKDGEmvqKGTYTEFLK 579
Cdd:cd03222 134 VLDYLSDRIHVFEGE---PGVYGIASQ 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
996-1190 |
2.88e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 996 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILttEIGLHDlrkkm 1074
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADsGRIHCGTKL--EVAYFD----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 siipqepvlftgTMRKNLDPfnEHTDEE-LWRALEEV----QLKEAIEDL------PGKMDTEL-AESGsnfsvGQRQLV 1142
Cdd:PRK11147 389 ------------QHRAELDP--EKTVMDnLAEGKQEVmvngRPRHVLGYLqdflfhPKRAMTPVkALSG-----GERNRL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 1143 CLARAILKNNRILIIDEATANVDPRTDELIQQKIREkfAQCTVLTIAH 1190
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS--YQGTVLLVSH 495
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
50-267 |
2.89e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 47.48 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGI-FTLIEEGTRVVQPLFLGKIIeyfekydpDDSVALHTAYG---YAAVLsmctLILAILHHLYFY----------- 114
Cdd:cd18543 1 LILALlAALLATLAGLAIPLLTRRAI--------DGPIAHGDRSAlwpLVLLL----LALGVAEAVLSFlrrylagrlsl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 115 HVQcAGMRLRvamchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVeigISC 194
Cdd:cd18543 69 GVE-HDLRTD------LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLV---LSP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 195 LAGLAVLVILLPLqscigkLFSSLRSKTAAFTDARI---------RTMNEVITGMRIIKMYAWEKS----FADLIANLRK 261
Cdd:cd18543 139 PLALVALASLPPL------VLVARRFRRRYFPASRRaqdqagdlaTVVEESVTGIRVVKAFGRERReldrFEAAARRLRA 212
|
....*.
gi 255683324 262 KEISKI 267
Cdd:cd18543 213 TRLRAA 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
378-566 |
2.89e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQP---- 439
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISEDRkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 440 WVFSGTVRSNI------LFGKKY-------EKERYEKVIKACALK---KDLQlledgdltvIGdrgaTLSGGQKARVNLA 503
Cdd:PRK10762 341 LVLGMSVKENMsltalrYFSRAGgslkhadEQQAVSDFIRLFNIKtpsMEQA---------IG----LLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 504 RAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITI-LVTHQL-QYLKAASHILILKDG 566
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIiLVSSEMpEVLGMSDRILVMHEG 471
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1022-1178 |
3.12e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.31 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALfrlsepEGKIWIDKILTTEIGL------------HDLRKKMSiipqepvlFTGTMR 1089
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHL------SGLITGDKSAGSHIELlgrtvqregrlaRDIRKSRA--------NTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1090 KNLDPFNEHTDEE-----------LWRA----LEEVQLKEAIEDLPGKMDTELA-ESGSNFSVGQRQLVCLARAILKNNR 1153
Cdd:PRK09984 93 QQFNLVNRLSVLEnvligalgstpFWRTcfswFTREQKQRALQALTRVGMVHFAhQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180
....*....|....*....|....*
gi 255683324 1154 ILIIDEATANVDPRTDELIQQKIRE 1178
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRD 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1014-1193 |
3.30e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGK--IWIDKILTT--EIGLHDLR-KKMSIIPQEPVLftgtm 1088
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvIFNGQPMSKlsSAAKAELRnQKLGFIYQFHHL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1089 rknLDPFNehtdeelwrALEEVQLKEAIEDLPGKMDTE-----LAESG---------SNFSVGQRQLVCLARAILKNNRI 1154
Cdd:PRK11629 99 ---LPDFT---------ALENVAMPLLIGKKKPAEINSralemLAAVGlehranhrpSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 1155 LIIDEATANVDPRTDELIQQKIRE-KFAQCTV-------LTIAHRLN 1193
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGElNRLQGTAflvvthdLQLAKRMS 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
378-578 |
3.61e-05 |
|
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: 47.87 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV----------------HGR----IAYVSQ 437
Cdd:TIGR03269 298 KAVD-----NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRakryIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 438 QPWVFS-GTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 516
Cdd:TIGR03269 373 EYDLYPhRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 517 DPLSAVDAeVGKHLFQLCICQALHE--KITILVTHQLQY-LKAASHILILKDGEMVQKGTYTEFL 578
Cdd:TIGR03269 453 EPTGTMDP-ITKVDVTHSILKAREEmeQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
378-569 |
3.82e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 378 KALDSPTL-QGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-RIAYVSQQPWVFSG----------- 444
Cdd:PRK11288 261 DGLKGPGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkae 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 ------TVRSNI-------------LFGKKYEKERYEKVIKACALKKdlqllEDGDlTVIGdrgaTLSGGQKARVNLARA 505
Cdd:PRK11288 341 giipvhSVADNInisarrhhlragcLINNRWEAENADRFIRSLNIKT-----PSRE-QLIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 506 VYQDADIYLLDDPLSAVDaeVG-KHLfqlcICQALHE----KITIL-VTHQL-QYLKAASHILILKDGEMV 569
Cdd:PRK11288 411 LSEDMKVILLDEPTRGID--VGaKHE----IYNVIYElaaqGVAVLfVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
50-346 |
4.13e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 47.11 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSvaLHTAYGYAAVLSMCTLILAILHHLYFYHvqcagMRLRVAmcH 129
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSS--GYYLGVYAALLVLASVLLVLLRWLLFVL-----AGLRAS--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 130 MIYRKALR-LSNSAMG---KTTTGQIVNLLSNDVNKFDQV--TIFLHFLWAGpLQAIAVTVLlwveIGISCLAGLAVLVI 203
Cdd:cd18580 73 RLHDKLLRsVLRAPMSffdTTPSGRILNRFSKDIGLIDEElpLALLDFLQSL-FSVLGSLIV----IAIVSPYFLIVLPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 204 LLPLQSCIGKLFSS----LR-----SKTAAFTdarirTMNEVITGMRIIKMYAWEKSFADLiaNLRKKEISkiLGSSYLr 274
Cdd:cd18580 148 LLVVYYLLQRYYLRtsrqLRrleseSRSPLYS-----HFSETLSGLSTIRAFGWQERFIEE--NLRLLDAS--QRAFYL- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 275 gMNMASF-------FIANKVILFVTFTSyVLLGNEITASHVFVAMTLygAVRLTVTLFFpsAIERGSE---AIVSIRRIK 344
Cdd:cd18580 218 -LLAVQRwlglrldLLGALLALVVALLA-VLLRSSISAGLVGLALTY--ALSLTGSLQW--LVRQWTEletSMVSVERIL 291
|
..
gi 255683324 345 NF 346
Cdd:cd18580 292 EY 293
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
998-1195 |
5.56e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.41 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 998 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALF---RLSepEGKIWIDKILTTEIglhdLRKKM 1074
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMgfvRLA--SGKISILGQPTRQA----LQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1075 -SIIPQE-------PVLF-----------TGTMRKNldpfNEHTDEELWRALEEVQLKEAIEDLPGKMdtelaesgsnfS 1135
Cdd:PRK15056 80 vAYVPQSeevdwsfPVLVedvvmmgryghMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGEL-----------S 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255683324 1136 VGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRLNTI 1195
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSV 205
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
722-970 |
6.02e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 46.74 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 722 LGIYAGLTAVTVLFGIARSLLVF---YILVNASQ----TLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLP 794
Cdd:cd18564 50 LALLLLAAAALVGIALLRGLASYagtYLTALVGQrvvlDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 795 LTFLDFI-QTLLLVVSVIAVAaavipWI-----LIPLVPLSVVFLVLRRY---FLETSRDVKRLESTtrspVFSHLSSSL 865
Cdd:cd18564 130 SGVLPLLtNLLTLVGMLGVMF-----WLdwqlaLIALAVAPLLLLAARRFsrrIKEASREQRRREGA----LASVAQESL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 866 QGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAIFV-IVVAFGS-LVLAKTLNAGQVGLALSYA 943
Cdd:cd18564 201 SAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTaLVLWFGAwLVLAGRLTPGDLLVFLAYL 280
|
250 260
....*....|....*....|....*..
gi 255683324 944 LTLMGMFQWSVRQSAEVENMMISVERV 970
Cdd:cd18564 281 KNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
351-568 |
6.12e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 351 ELPQRKaHVPSDGKAIVHVQDFTA--FWDkaldsptlqgLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV 428
Cdd:PRK15439 254 ELPGNR-RQQAAGAPVLTVEDLTGegFRN----------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIML 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 429 HGR--------------IAYVS---QQP---------W-VFSGTVRSNILFGK-KYEKERYEKVIKACALKkdlqlLEDG 480
Cdd:PRK15439 323 NGKeinalstaqrlargLVYLPedrQSSglyldaplaWnVCALTHNRRGFWIKpARENAVLERYRRALNIK-----FNHA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 481 DLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQL-QYLKAASH 559
Cdd:PRK15439 398 EQAA-----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLeEIEQMADR 472
|
....*....
gi 255683324 560 ILILKDGEM 568
Cdd:PRK15439 473 VLVMHQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
385-569 |
6.40e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.31 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSaVL---GELPPASGLVSVHGR---------IAYVSQQPwVFSG--TVRSNI 450
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLD-VLagrKTAGVITGEILINGRpldknfqrsTGYVEQQD-VHSPnlTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 451 LFgkkyekeryekvikACALkkdlqlledgdltvigdRGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGkhl 530
Cdd:cd03232 101 RF--------------SALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA--- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 531 fqLCICQALhEKI-----TILVT-HQ--LQYLKAASHILILK-DGEMV 569
Cdd:cd03232 145 --YNIVRFL-KKLadsgqAILCTiHQpsASIFEKFDRLLLLKrGGKTV 189
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
50-299 |
6.49e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 46.38 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIF-TLIEEGTRVVQPLFLGKIIEYFEkydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 128
Cdd:cd18778 1 LILTLLcALLSTLLGLVPPWLIRELVDLVT----IGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 129 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVtiFLHflwAGP------LQAIAVTVLLwveIGISCLagLAVLV 202
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERL--IAD---GIPqgitnvLTLVGVAIIL---FSINPK--LALLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 203 IL-LPLQSCIGKLFsslrSKTA--AFTDARIRT--MNEV----ITGMRIIKMYAWEKSFADlianlRKKEISKILGSSYL 273
Cdd:cd18778 147 LIpIPFLALGAWLY----SKKVrpRYRKVREALgeLNALlqdnLSGIREIQAFGREEEEAK-----RFEALSRRYRKAQL 217
|
250 260
....*....|....*....|....*.
gi 255683324 274 RGMNMASFFiaNKVILFVTFTSYVLL 299
Cdd:cd18778 218 RAMKLWAIF--HPLMEFLTSLGTVLV 241
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
50-291 |
6.79e-05 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 46.24 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDpDDSVALHTAyGYAAVLSMCTLILAILHHLYFYHV-QCAGMRLRvamc 128
Cdd:cd18548 2 ILAPLFKLLEVLLELLLPTLMADIIDEGIANG-DLSYILRTG-LLMLLLALLGLIAGILAGYFAAKAsQGFGRDLR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 129 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIAVTVLLwveIGISclAGLA-VLVILLP 206
Cdd:cd18548 76 KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNfVMMLLRMLVRAPIMLIGAIIMA---FRIN--PKLAlILLVAIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 207 LQSCI--------GKLFSSLRSKtaafTDARIRTMNEVITGMRIIKMYAWE----KSFADLIANLRKKEIS--KILGSsy 272
Cdd:cd18548 151 ILALVvflimkkaIPLFKKVQKK----LDRLNRVVRENLTGIRVIRAFNREdyeeERFDKANDDLTDTSLKagRLMAL-- 224
|
250
....*....|....*....
gi 255683324 273 lrgMNMASFFIANKVILFV 291
Cdd:cd18548 225 ---LNPLMMLIMNLAIVAI 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1125-1208 |
8.40e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.75 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1125 TELA-ESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPR-TDELIQ--QKIREKFaQCTVLTIAHRLNTIID-SD 1199
Cdd:PRK11300 144 LEHAnRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKeTKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSD 222
|
....*....
gi 255683324 1200 KIMVLDSGR 1208
Cdd:PRK11300 223 RIYVVNQGT 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1014-1223 |
1.03e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSslISAL--FRL------SEPEGKIWI---DKILTTEIGLHDLR-KKMSIIPQEP 1081
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKS--VTALsiLRLlpsppvVYPSGDIRFhgeSLLHASEQTLRGVRgNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1082 VLftgtmrkNLDPFneHTDE--------------------ELWRALEEVQLKEA---IEDLPGKMdtelaeSGsnfsvGQ 1138
Cdd:PRK15134 102 MV-------SLNPL--HTLEkqlyevlslhrgmrreaargEILNCLDRVGIRQAakrLTDYPHQL------SG-----GE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1139 RQLVCLARAILKNNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLKEYDEP 1215
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRA 241
|
....*...
gi 255683324 1216 YVLLQNPE 1223
Cdd:PRK15134 242 ATLFSAPT 249
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
50-326 |
1.04e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 45.92 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIEEGTRVVQPLFLGKIIEyfeKYDPD-DSVALHTaygYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 128
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAID---EYIPNgDLSGLLI---IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 129 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNK----FDQ--VTIFLHFLwagPLQAIAVTVLLW-VEIGISCLAGLAVL 201
Cdd:cd18545 77 QDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSlsdlLSNglINLIPDLL---TLVGIVIIMFSLnVRLALVTLAVLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 202 VILL-PLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEK----SFADLIANLRKkeiskilgsSYLRGM 276
Cdd:cd18545 154 VLVVfLLRRRARKAWQRVRKKISNLNAY----LHESISGIRVIQSFAREDeneeIFDELNRENRK---------ANMRAV 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 277 NMASFF---------IANKVILFvtFTSYVLLGNEITAShVFVAMTLYgavrltVTLFF 326
Cdd:cd18545 221 RLNALFwplvelisaLGTALVYW--YGGKLVLGGAITVG-VLVAFIGY------VGRFW 270
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1026-1165 |
1.23e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1026 EKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIG-LHDLRKKMSIIPQEPVlftgtmrKNLDPFNEHTDE 1101
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESqGGEIIFNgqRIDTLSPGkLQALRRDIQFIFQDPY-------ASLDPRQTVGDS 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 1102 --ELWRALEEVQLKEAIEDLP------GKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVD 1165
Cdd:PRK10261 424 imEPLRVHGLLPGKAAAARVAwllervGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
50-321 |
1.51e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 45.12 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIF-TLIEEGTRVVQPLFLGKIIeyfekydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAG----MRLR 124
Cdd:cd18551 1 LILALLlSLLGTAASLAQPLLVKNLI--------DALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGervvLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 125 vamcHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQV--TIFLHFLwAGPLQAIAVTVLL----WVEIGISCLAGL 198
Cdd:cd18551 73 ----RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELitSGLPQLV-TGVLTVVGAVVLMflldWVLTLVTLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 199 AVLVILLPLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEKSFAdlianlrkKEISKILGSSYLRGMNM 278
Cdd:cd18551 148 LAFLIILPLGRRIRKASKRAQDALGELSAA----LERALSAIRTVKASNAEERET--------KRGGEAAERLYRAGLKA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 255683324 279 ASFF-IANKVILFVTFTSyvllgneitashvFVAMTLYGAVRLT 321
Cdd:cd18551 216 AKIEaLIGPLMGLAVQLA-------------LLVVLGVGGARVA 246
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
385-594 |
1.55e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSqqpwVFSG-----TVRSNILFgKKYEKE 459
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA----ISAGlsgqlTGIENIEF-KMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 460 RYEKVIKACaLKKDLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSavdaeVGKHLF-QLCIcQA 538
Cdd:PRK13546 115 FKRKEIKAM-TPKIIEFSELGEF--IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS-----VGDQTFaQKCL-DK 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 255683324 539 LHE-----KITILVTHQL-QYLKAASHILILKDGEMVQKG-------TYTEFLKsgvDFGSLLKKENEE 594
Cdd:PRK13546 186 IYEfkeqnKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGelddvlpKYEAFLN---DFKKKSKAEQKE 251
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1024-1197 |
1.64e-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: 43.13 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1024 SREKVGIVGRTGAGKSSLISALFRLSEPEGKiwidkiltteiglhdlrkkmsiipqepvlftGTMRKNLDPFNEHTDEEL 1103
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-------------------------------GVIYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1104 WraleevqlkeaiedlpgkmDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTDELIQQ-------KI 1176
Cdd:smart00382 50 L-------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrllLL 110
|
170 180
....*....|....*....|.
gi 255683324 1177 REKFAQCTVLTIAHRLNTIID 1197
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGP 131
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1029-1049 |
1.92e-04 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 42.71 E-value: 1.92e-04
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
351-533 |
1.92e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 351 ELPQRKAHVPSD-GKAIVHVQDFTAfWDKalDSPTLQ---GLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPAS-GL 425
Cdd:PRK13549 243 ELTALYPREPHTiGEVILEVRNLTA-WDP--VNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 426 VSVHGR--------------IAYVS----QQPWVFSGTVRSNIL--------FGKKYEKERYEKVIkacalKKDLQLLE- 478
Cdd:PRK13549 320 IFIDGKpvkirnpqqaiaqgIAMVPedrkRDGIVPVMGVGKNITlaaldrftGGSRIDDAAELKTI-----LESIQRLKv 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 479 ---DGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEVGKHLFQL 533
Cdd:PRK13549 395 ktaSPELAI-----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQL 451
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
392-429 |
2.07e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 43.64 E-value: 2.07e-04
10 20 30
....*....|....*....|....*....|....*...
gi 255683324 392 ARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH 429
Cdd:COG3709 2 SGPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFAR 39
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1010-1222 |
2.18e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1010 DGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDL----RKK-----MSIIPQ 1079
Cdd:PRK15093 17 DGWVkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLspreRRKlvghnVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1080 EPvlftgtmRKNLDPfNEHTDEEL------------------WRALEEVQL--KEAIEDLPGKMDT---ELAEsgsnfsv 1136
Cdd:PRK15093 97 EP-------QSCLDP-SERVGRQLmqnipgwtykgrwwqrfgWRKRRAIELlhRVGIKDHKDAMRSfpyELTE------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1137 GQRQLVCLARAILKNNRILIIDEATANVDPRTdeliQQKIREKFAQ------CTVLTIAHRLNTIID-SDKIMVLDSGRL 1209
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTT----QAQIFRLLTRlnqnnnTTILLISHDLQMLSQwADKINVLYCGQT 237
|
250
....*....|...
gi 255683324 1210 KEYDEPYVLLQNP 1222
Cdd:PRK15093 238 VETAPSKELVTTP 250
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
125-313 |
2.78e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.39 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 125 VAMCHMIYRKALRLSNSAMGK----------TT-TGQIVNLLSNDVNKFD-----QVTIFLHFLwagpLQAIAVTVLL-- 186
Cdd:cd18606 57 LLLAYLGIRASKRLHNKALKRvlrapmsffdTTpLGRILNRFSKDTDVLDnelpdSLRMFLYTL----SSIIGTFILIii 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 187 ---WVEIGISCLAGLAVLVILLPLQSC--IGKLFSSLRSKT-AAFtdarirtmNEVITGMRIIKMYAWEKSFadlIANLR 260
Cdd:cd18606 133 ylpWFAIALPPLLVLYYFIANYYRASSreLKRLESILRSFVyANF--------SESLSGLSTIRAYGAQDRF---IKKNE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255683324 261 KkeiskilgssYLRGMNMASF--------------FIANKVILFVTFTSyVLLGNEITASHVFVAMT 313
Cdd:cd18606 202 K----------LIDNMNRAYFltianqrwlairldLLGSLLVLIVALLC-VTRRFSISPSSTGLVLS 257
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
385-579 |
3.03e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.31 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------RIAYVSQQPWVFsG---------TVR-S 448
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRIGVVF-GqrsqlwwdlPAIdS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 449 NILFGKKYE--KERYEKVIKACAlkkdlQLLEDGDLTVIGDRgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 526
Cdd:COG4586 117 FRLLKAIYRipDAEYKKRLDELV-----ELLDLGELLDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 527 gkhlfQLCICQALHE-----KITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTEFLK 579
Cdd:COG4586 190 -----KEAIREFLKEynrerGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
492-580 |
3.38e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 492 LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKIT-ILVTHQLQYL-KAASHILILKDGEMV 569
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDLALVaEAAHKIIVMYAGQVV 233
|
90
....*....|.
gi 255683324 570 QKGTYTEFLKS 580
Cdd:PRK11022 234 ETGKAHDIFRA 244
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1028-1047 |
3.44e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 44.37 E-value: 3.44e-04
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
49-343 |
4.06e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 43.96 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 49 YLILGIFTLIEEGTRVVQPLFLGKIIeyfekydpdDSVALHTAYGYAAVLSMCTLILAILH------HLYFYHV--QCAG 120
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII---------DSVIGGGLRELLWLLALLILGVALLRgvfrylQGYLAEKasQKVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 121 MRLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFLHFLWAGPLQAI-----AVTVLLW--VEIGIS 193
Cdd:cd18542 72 YDLRNDL----YDHLQRLSFSFHDKARTGDLMSRCTSDV---DTIRRFLAFGLVELVRAVllfigALIIMFSinWKLTLI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 194 CLAGLAVLVIL-LPLQSCIGKLFSSLRSKTAAFTdariRTMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISkil 268
Cdd:cd18542 145 SLAIIPFIALFsYVFFKKVRPAFEEIREQEGELN----TVLQENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIK--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 269 gSSYLRGMNMA-SFFIANKVILFVT-FTSYVLLGNEITAShVFVAMTLYgavrlTVTLFFP--------SAIERgseAIV 338
Cdd:cd18542 218 -LAKLLAKYWPlMDFLSGLQIVLVLwVGGYLVINGEITLG-ELVAFISY-----LWMLIWPvrqlgrliNDMSR---ASA 287
|
....*
gi 255683324 339 SIRRI 343
Cdd:cd18542 288 SAERI 292
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
723-950 |
5.15e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 43.59 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 723 GIYAGLTAVTVLFG---IARSLLVF---YILVNASQTLHNRM----FESILKAPVLFFDRNPIGRILNRFSkDIGHMDDL 792
Cdd:cd18570 36 GDINLLNIISIGLIllyLFQSLLSYirsYLLLKLSQKLDIRLilgyFKHLLKLPLSFFETRKTGEIISRFN-DANKIREA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 793 LPLTFLD-FIQTLLLVVSVIAVAAAVIP--WILIPLVPL-SVVFLVLRRYFLETSRDVKRLESTTRspvfSHLSSSLQGL 868
Cdd:cd18570 115 ISSTTISlFLDLLMVIISGIILFFYNWKlfLITLLIIPLyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 869 WTIRAYKAEERCQELFDAHqdlhseawFLFLTTSRWFAVRLDAICAIF---------VIVVAFGS-LVLAKTLNAGQVgl 938
Cdd:cd18570 191 ETIKSLNAEEQFLKKIEKK--------FSKLLKKSFKLGKLSNLQSSIkglisligsLLILWIGSyLVIKGQLSLGQL-- 260
|
250
....*....|..
gi 255683324 939 aLSYaLTLMGMF 950
Cdd:cd18570 261 -IAF-NALLGYF 270
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1027-1047 |
5.81e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 40.68 E-value: 5.81e-04
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1027-1190 |
6.79e-04 |
|
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: 43.77 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1027 KVGIVGRTGAGKSSLISALFRL-SEPEGKIWIDKILTteIGlhdlrkkmsIIPQEPVL-FTGTMRKN-----------LD 1093
Cdd:TIGR03719 33 KIGVLGLNGAGKSTLLRIMAGVdKDFNGEARPQPGIK--VG---------YLPQEPQLdPTKTVRENveegvaeikdaLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1094 PFNEHT------DEELWRALEE-VQLKEAIE-----DLPGKMdtELAESG----------SNFSVGQRQLVCLARAILKN 1151
Cdd:TIGR03719 102 RFNEISakyaepDADFDKLAAEqAELQEIIDaadawDLDSQL--EIAMDAlrcppwdadvTKLSGGERRRVALCRLLLSK 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 255683324 1152 NRILIIDEATANVDPRTDELIQQKIREkfAQCTVLTIAH 1190
Cdd:TIGR03719 180 PDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
379-523 |
8.73e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 379 ALDSPTLQglsfIARpGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------------RIAYVSQqpwvfsG 444
Cdd:NF033858 16 ALDDVSLD----IPA-GCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQ------G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 ---------TVRSNI-----LFGKKyEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQD 509
Cdd:NF033858 85 lgknlyptlSVFENLdffgrLFGQD-AAERRRRI---------DELLRATGLAPFADRPAgKLSGGMKQKLGLCCALIHD 154
|
170
....*....|....
gi 255683324 510 ADIYLLDDPLSAVD 523
Cdd:NF033858 155 PDLLILDEPTTGVD 168
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
715-927 |
9.95e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 42.47 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 715 TLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLP 794
Cdd:cd18576 32 TASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 795 LTFLDFIQTLLLVVSVIAVAAAVIP----WILIPLVPLSVVFLVLRRYFLETSRDVK-RLESTTrspvfSHLSSSLQGLW 869
Cdd:cd18576 112 TTLAEFLRQILTLIGGVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIR 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 255683324 870 TIRAYKAEERCQELFDAHQDlhsEAWFLFLTTSRWfavrlDAICAIFVIVVAFGSLVL 927
Cdd:cd18576 187 VVKAFTREDYEIERYRKALE---RVVKLALKRARI-----RALFSSFIIFLLFGAIVA 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
718-928 |
1.16e-03 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 42.42 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18551 35 SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 798 LDFIQTLLLVVSVIAVAAAVIPW---ILIPLVPLSVVFLV-----LRRYFLETSRDVKRLEsttrspvfSHLSSSLQGLW 869
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAFLIILplgrrIRKASKRAQDALGELS--------AALERALSAIR 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255683324 870 TIRAYKAEERCQELFDAHQDlhsEAWFLFLTTSRWFAV-----RLdAICAIFVIVVAFGSLVLA 928
Cdd:cd18551 187 TVKASNAEERETKRGGEAAE---RLYRAGLKAAKIEALigplmGL-AVQLALLVVLGVGGARVA 246
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1028-1215 |
1.57e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1028 VGIVGRTGAGKSSLISALF-----RLSEPEGKIWIDKILT----TEIG-----LHDLRKKMSIIPQE----PVLFTGTMR 1089
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSgelipNLGDYEEEPSWDEVLKrfrgTELQnyfkkLYNGEIKVVHKPQYvdliPKVFKGKVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1090 KNLdpfnEHTDEElwRALEEVQLKEAIEDLpgkMDTELaesgSNFSVGQRQLVCLARAILKNNRILIIDEATANVDPRTD 1169
Cdd:PRK13409 182 ELL----KKVDER--GKLDEVVERLGLENI---LDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 255683324 1170 ELIQQKIREKFAQCTVLTIAHRLnTIID--SDKIMVLdsgrlkeYDEP 1215
Cdd:PRK13409 249 LNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA-------YGEP 288
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
724-785 |
1.91e-03 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 41.73 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 724 IYAGLTAVTVLFGIARSLLVfYILVNASQT----LHNRMFESILKAPVLFFDRNPIGRILNRFSKD 785
Cdd:cd18573 43 FALALLGVFVVGAAANFGRV-YLLRIAGERivarLRKRLFKSILRQDAAFFDKNKTGELVSRLSSD 107
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1014-1178 |
1.99e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 41.17 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1014 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHdLRKKMSI--IPQEPVLFTG-TMR 1089
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEDITHLPMH-KRARLGIgyLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1090 KNLDPFNEHTD-------EELWRALEEVQLkeaiedlpgkmdTELAES-GSNFSVGQRQLVCLARAILKNNRILIIDEAT 1161
Cdd:COG1137 97 DNILAVLELRKlskkereERLEELLEEFGI------------THLRKSkAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170
....*....|....*..
gi 255683324 1162 ANVDPRTDELIQQKIRE 1178
Cdd:COG1137 165 AGVDPIAVADIQKIIRH 181
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
381-575 |
2.23e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 381 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLG--ELPPASGLVSVHGR--------------IAYVSQQPWVFSG 444
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllelspedragegIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 445 TvrSNILF-------GKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 516
Cdd:PRK09580 93 V--SNQFFlqtalnaVRSYrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255683324 517 DPLSAVDAEVGKHLFQLCICQALHEKITILVTHQ---LQYLKaASHILILKDGEMVQKGTYT 575
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDFT 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
50-298 |
2.25e-03 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 41.62 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIEEGTRVVQPLFLGKII-EYFEKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFY---HV-QCAGMRLR 124
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIdLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRlmaRVsQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 125 VAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQV--TIFLHFLwAGPLQAIAVTVLLWVeigISCLAGLAVLV 202
Cdd:cd18547 82 KDL----FEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQAlsQSLTQLI-SSILTIVGTLIMMLY---ISPLLTLIVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 203 ILlPLQSCIGKLFSSlrsKTAAFTDARIRT-------MNEVITGMRIIKMYAWE----KSFADLIANLRKkeiskilgSS 271
Cdd:cd18547 154 TV-PLSLLVTKFIAK---RSQKYFRKQQKAlgelngyIEEMISGQKVVKAFNREeeaiEEFDEINEELYK--------AS 221
|
250 260
....*....|....*....|....*....
gi 255683324 272 YlrgmnMASFF--IANKVILFVTFTSYVL 298
Cdd:cd18547 222 F-----KAQFYsgLLMPIMNFINNLGYVL 245
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
50-207 |
2.30e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 41.68 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 50 LILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSVALHTAY---GYAAvLSMCTLILAILHHLYFYHvqcAGMRlrva 126
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYylgIYAL-ISLLSVLLGTLRYLLFFF---GSLR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 127 MCHMIYRkalRLSNSAMG-------KTTTGQIVNLLSNDVNKFDqvtiflhflwagplQAIAVTVLLWVEIGISCLAGLA 199
Cdd:cd18604 74 ASRKLHE---RLLHSVLRaplrwldTTPVGRILNRFSKDIETID--------------SELADSLSSLLESTLSLLVILI 136
|
....*...
gi 255683324 200 VLVILLPL 207
Cdd:cd18604 137 AIVVVSPA 144
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1135-1226 |
2.80e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.55 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1135 SVGQRQLVCLARAILKNNRILIIDEATANVDP--RTDELIQQKIREKFAQCTVLTIAH-RLNTIIDSDKIMVLDSGRLKE 1211
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQ 214
|
90
....*....|....*
gi 255683324 1212 YDEPYVLLQNPESLF 1226
Cdd:PRK11000 215 VGKPLELYHYPANRF 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
385-524 |
2.82e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 385 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELppASGLVSVHGRIAY-----------------------------V 435
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNT--DGFHIGVEGVITYdgitpeeikkhyrgdvvynaetdvhfphlT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 436 SQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKK-DLQLLEDgdlTVIGD---RGatLSGGQKARVNLARAVYQDAD 511
Cdd:TIGR00956 155 VGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMATyGLSHTRN---TKVGNdfvRG--VSGGERKRVSIAEASLGGAK 229
|
170
....*....|...
gi 255683324 512 IYLLDDPLSAVDA 524
Cdd:TIGR00956 230 IQCWDNATRGLDS 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
395-568 |
3.37e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 395 GELLAVVGPVGAGKSSLLSAVLGELPPASG-------LVSVHGRIAYVSQQPWVFSGTVrsniLF-------GKKYEKER 460
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGeilldgkPVTAEQPEDYRKLFSAVFTDFH----LFdqllgpeGKPANPAL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 461 YEKVIKACALKKDLQLlEDGDLTVIgdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALH 540
Cdd:PRK10522 425 VEKWLERLKMAHKLEL-EDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQE 498
|
170 180
....*....|....*....|....*....
gi 255683324 541 EKITIL-VTHQLQYLKAASHILILKDGEM 568
Cdd:PRK10522 499 MGKTIFaISHDDHYFIHADRLLEMRNGQL 527
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1028-1215 |
4.24e-03 |
|
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: 41.31 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1028 VGIVGRTGAGKSSLISALF-----RLSEPEGKIWIDKILT----TEIGLH--DLRK---KMSIIPQE----PVLFTGTMR 1089
Cdd:COG1245 102 TGILGPNGIGKSTALKILSgelkpNLGDYDEEPSWDEVLKrfrgTELQDYfkKLANgeiKVAHKPQYvdliPKVFKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1090 KNLdpfnEHTDEelwRALeevqLKEAIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILKNNRILIIDEATANVDprtd 1169
Cdd:COG1245 182 ELL----EKVDE---RGK----LDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---- 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 1170 elIQQKIR-----EKFAQC--TVLTIAHRLnTIID--SDKIMVLdsgrlkeYDEP 1215
Cdd:COG1245 245 --IYQRLNvarliRELAEEgkYVLVVEHDL-AILDylADYVHIL-------YGEP 289
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
718-805 |
4.64e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 40.54 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 718 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPIGRILNRFSKDIGHMDDLLPLTF 797
Cdd:cd18550 38 LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTL 117
|
....*...
gi 255683324 798 LDFIQTLL 805
Cdd:cd18550 118 TSVVSNVV 125
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1135-1207 |
4.67e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 4.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255683324 1135 SVGQRQLVCLARAILKNNRILIIDEAT-ANVDPRTDELIQQkIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDSG 1207
Cdd:PRK10762 143 SIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLFRV-IRELKSQgRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1022-1205 |
5.06e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1022 IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidkiltteiglhDLRKKMSIIPQE-PVLFTGTMRKNLDPFNEHT 1099
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPdEGEV-------------DPELKISYKPQYiKPDYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 1100 DEELWRalEEVQLKEAIEDLpgkMDTELAE-SGsnfsvGQRQLVCLARAILKNNRILIIDEATANVDP----RTDELIQQ 1174
Cdd:PRK13409 429 GSSYYK--SEIIKPLQLERL---LDKNVKDlSG-----GELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRR 498
|
170 180 190
....*....|....*....|....*....|...
gi 255683324 1175 KIREKFAqcTVLTIAHRLnTIID--SDKIMVLD 1205
Cdd:PRK13409 499 IAEEREA--TALVVDHDI-YMIDyiSDRLMVFE 528
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
362-434 |
6.74e-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: 40.44 E-value: 6.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255683324 362 DGKAIVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKS-SLLSaVLGELPPasGLVSVHGRIAY 434
Cdd:COG4172 2 MSMPLLSVEDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPD--PAAHPSGSILF 73
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
399-558 |
7.87e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 399 AVVGPVGAGKSSLLSA---VLGE----LPPASGLVSVHGRIayvsqQPWVFSGTVRsnILFGKKYekeryekvikacalk 471
Cdd:cd03239 26 AIVGPNGSGKSNIVDAicfVLGGkaakLRRGSLLFLAGGGV-----KAGINSASVE--ITFDKSY--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 472 kdlQLLEDGDLTVIgdrgatLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILV 547
Cdd:cd03239 84 ---FLVLQGKVEQI------LSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVI 154
|
170
....*....|.
gi 255683324 548 THQLQYLKAAS 558
Cdd:cd03239 155 TLKKEMFENAD 165
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
121-315 |
8.86e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 39.80 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 121 MRLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFLHFLwagpLQAIAVTVLLWVEIGISCL---AG 197
Cdd:cd18563 76 ADLRRDL----YEHLQRLSLSFFDKRQTGSLMSRVTSDT---DRLQDFLSDG----LPDFLTNILMIIGIGVVLFslnWK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255683324 198 LAVLVIL-LPLQSCIGKLFS-SLRSKTAAFTDARIR---TMNEVITGMRIIKMYAWEKS----FADLIANLRkkEISKIL 268
Cdd:cd18563 145 LALLVLIpVPLVVWGSYFFWkKIRRLFHRQWRRWSRlnsVLNDTLPGIRVVKAFGQEKReikrFDEANQELL--DANIRA 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 255683324 269 GSSYLRGMNMASFFIANKVILFVTFTSYVLLGNEITAShVFVAMTLY 315
Cdd:cd18563 223 EKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLSY 268
|
|
| |
